Granted Patent
B2
US 12,343,341 · App. 17/492,427 · Granted Jul 1, 2025
Synthetic lethality and the treatment of cancer
Inventors:
Luc G. Berthiaume (Edmonton, CA); Erwan Beauchamp (Rennes, FR); Conganige Maneka Anne Perinpanayagam (Edmonton, CA); Chuiyee Yap (Edmonton, CA)
Assignee:
PACYLEX PHARMACEUTICALS INC.
A61K31/496A61K31/12A61K31/191A61K31/28A61K31/7105A61K31/713A61K45/06C07K16/40C12Q1/686G01N33/5091G01N33/574G01N33/57496
View Patent ↗
Loading inventors, assignments & file history…
Abstract
Described herein are compounds, compositions and methods for treatment of cancer. Also described are methods and uses for identifying subject with cancer that are suitable for treatment with the compounds, composition and methods are described herein. In one aspect of the present invention, there is provided a method of treating a subject having a cancer deficient in NMT2, comprising: administering to said subject an NMT inhibitor.
Claims (16)
1. A method of treating a cancer in a human subject, comprising:
identifying that the human subject is suitable for treatment with an inhibitor of NMT1 protein by
measuring an N-myristoyltransferase 1 (NMT1) protein level in a sample containing cancer cells obtained from the human subject using a device configured to measure NMT1 protein,
measuring an N-myristoyltransferase 2 (NMT2) protein level in the sample containing cancer cells using a device configured to measure NMT2 protein,
determining from the measured NMT1 and NMT2 protein levels that NMT1 protein is present in the sample containing cancer cells and that the NMT2 protein level in the sample containing cancer cells is low or absent as compared to an NMT2 protein level present in a normal human B-Cell, thereby identifying the human subject as suitable for treatment with the inhibitor of NMT1 protein; and
administering the inhibitor of NMT1 inhibitor to the human subject, wherein said NMT1 inhibitor is DDD85646, or a derivative thereof.
2. The method of claim 1 , wherein said cancer is cancer is a lymphoma.
3. The method of claim 2 , wherein said lymphoma is a B cell lymphoma.
4. The method of claim 3 , wherein said B cell lymphoma is follicular lymphoma, diffuse large B-cell lymphoma, mantle cell lymphoma, B-CLL/SLL, immunocytoma/Waldenstrom's, MALT-type/monocytoid B cell lymphoma, Burkitt's lymphoma, a pediatric lymphoma, or anaplastic large cell lymphoma.
5. The method of claim 1 , wherein said cancer is Burkitt's lymphoma.
6. The method of claim 1 , further comprising administering a chemotherapeutic agent to the human subject.
7. The method of claim 6 , wherein said chemotherapeutic agent is CHOP, GAP-BOP, m-BACOD, ProMACE-MOPP, ProMACE-CytaBOM, MACOP-B, IMVP-16, MIME, DHAP, ESHAP, CEFF (B), CAMP, VABCD, ABDIC, CBVD, PCVP, CEP, EVA, MOPLACE, MIME, MINE, MTX-CHOP, CEM, CEVD, CAVP, EVAP, or EPOCH.
8. The method of claim 7 , wherein said cancer is cancer is a lymphoma.
9. The method of claim 8 , wherein said lymphoma is a B cell lymphoma.
10. The method of claim 9 , wherein said B cell lymphoma is follicular lymphoma, diffuse large B-cell lymphoma, mantle cell lymphoma, B-CLL/SLL, immunocytoma/Waldenstrom's, MALT-type/monocytoid B cell lymphoma, Burkitt's lymphoma, a pediatric lymphoma, or anaplastic large cell lymphoma.
11. The method of claim 6 , wherein said cancer is Burkitt's lymphoma.
Assignments (1)
ASSIGNMENT OF ASSIGNOR'S INTEREST
Recorded Oct 1, 2021
From: BERTHIAUME, LUC G.; BEAUCHAMP, ERWAN; YAP, CHUIYEE; PERINPANAYAGAM, CONGANIGE MANEKA ANNE
To: PACYLEX PHARMACEUTICALS INC.
Reel/Frame 057688/0664 →
Continuity (4)
Continuation
14234312
Provisional Application
61510686
· Jul 22, 2011
References Cited (400)
US 5164414A
· Vincent et al.
· 1992
[cited by applicant]
US 7449464B2
· Martin et al.
· 2008
[cited by applicant]
US 7662818B2
· Martin et al.
· 2010
[cited by applicant]
US 7981889B2
· Martin et al.
· 2011
[cited by applicant]
US 20030180292A1
· Hanna et al.
· 2003
[cited by applicant]
AU 2004220321B2
· 2010
[cited by applicant]
AU 2010202197A1
· 2010
[cited by applicant]
BR PI0408284A
· 2006
[cited by applicant]
BR PI0417056A
· 2007
[cited by applicant]
BR 112014001430A2
· 2017
[cited by applicant]
CA 2547077A1
· 2005
[cited by applicant]
CA 2670837A1
· 2008
[cited by applicant]
CA 2517629C
· 2011
[cited by applicant]
CN 101631466A
· 2010
[cited by applicant]
CN 1788000B
· 2010
[cited by applicant]
CN 1905864B
· 2011
[cited by applicant]
CN 102107008A
· 2011
[cited by applicant]
CO 5650256A2
· 2006
[cited by applicant]
DK 1633724T3
· 2011
[cited by applicant]
EC SP056094A
· 2006
[cited by applicant]
EP 2305221A1
· 2011
[cited by applicant]
EP 1633724B1
· 2011
[cited by applicant]
EP 1684736B1
· 2011
[cited by applicant]
ES 2364140T3
· 2011
[cited by applicant]
HR P2005A2
· 2005
[cited by applicant]
IL 176013A1
· 2015
[cited by applicant]
IS 8052A
· 2005
[cited by applicant]
JP H04210916A
· 1992
[cited by applicant]
JP 2007516241A
· 2007
[cited by applicant]
JP 2007520557A
· 2007
[cited by applicant]
JP 4027406B2
· 2007
[cited by applicant]
JP 2009079056A
· 2009
[cited by applicant]
JP 4268651B2
· 2009
[cited by applicant]
JP 2016506362A2
· 2016
[cited by applicant]
JP 6270719B2
· 2018
[cited by applicant]
KR 102164964B1
· 2020
[cited by applicant]
MA 27758A1
· 2006
[cited by applicant]
MX 05009661A
· 2006
[cited by applicant]
NO 20054625A
· 2005
[cited by applicant]
NO 20063078
· 2006
[cited by applicant]
NZ 542680A
· 2008
[cited by applicant]
NZ 547984A
· 2009
[cited by applicant]
NZ 737605B
· 2022
[cited by applicant]
PT 1633724E
· 2011
[cited by applicant]
RU 2413515C2
· 2011
[cited by applicant]
SI 1633724T1
· 2011
[cited by applicant]
WO 2004080976A1
· 2004
[cited by applicant]
WO 2005012305A2
· 2005
[cited by applicant]
WO 2005012524A1
· 2005
[cited by applicant]
WO 2005053662A1
· 2005
[cited by applicant]
WO 2005076843A2
· 2005
[cited by applicant]
WO 2006014729A2
· 2006
[cited by applicant]
WO 2006086043A2
· 2006
[cited by applicant]
WO 2008076965A1
· 2008
[cited by applicant]
WO 2010026365A1
· 2010
[cited by applicant]
WO 2013013302A1
· 2013
[cited by applicant]
WO 2014067002A1
· 2014
[cited by applicant]
ZA 200507097B
· 2006
[cited by applicant]
ZA 200605340B
· 2007
[cited by applicant]
Ducker et al. “Two N-Myristoyltransferase Isozymes Play Unique Roles in Protein Myristoylation, Proliferation, and Apoptosis,” Mol Cancer Res 2005;3(8). Aug. 2005, 463-476. (Year: 2005).
[cited by examiner]
Selvakumar et al. “Potential role of N-myristoyltransferase in cancer,” Progress in Lipid Research 46 (2007) 1-36. (Year: 2007).
[cited by examiner]
Shrivastav et al. “N-myristoyltransferase: A potential novel diagnostic marker for colon cancer,” Journal of Translational Medicine 2007, 5:58, 1-6. (Year: 2007).
[cited by examiner]
Hirsch et al., “Easily Reversible Desthiobiotin Binding to Streptavidin, Avidin, and Other Biotin-binding Proteins: Uses for Protein Labeling, Detection, and Isolation,” Analytical Biochemistry, Sep. 2002, vol. 308 (2),…
[cited by applicant]
Hobeika et al., “Testing Gene Function Early in the B Cell Lineage in Mb1-cre Mice.,” Proceedings of the National Academy of Sciences of the United States of America, Sep. 2006, vol. 103 (37), pp. 13789-13794.
[cited by applicant]
Hu et al., “Myristoylated Naked2 Antagonizes Wnt-beta-catenin Activity by Degrading Dishevelled-1 at the Plasma Membrane,” The Journal of Biological Chemistry, Apr. 2010, vol. 285 (18), pp. 13561-13568.
[cited by applicant]
Hudson et al., “Sect 2.4: Viable Lymphocyte Count,” found in Practical Immunology, Blackwell Scientific Publications, Oxford, England, 1976, 29-32.
[cited by applicant]
Hummel et al., “A Biologic Definition of Burkitt's Lymphoma From Transcriptional and Genomic Profiling,” The New England Journal of Medicine, Jun. 2006, vol. 354 (23), pp. 2419-2430.
[cited by applicant]
Inoue et al., “Ordering of Caspases in Cells Undergoing Apoptosis by the Intrinsic Pathway,” Cell Death and Differentiation, 2009, vol. 16 (7), pp. 1053-1061.
[cited by applicant]
International Patent Application No. PCT/CA2012/000696, International Preliminary Report on Patentability dated Feb. 6, 2014.
[cited by applicant]
International Patent Application No. PCT/CA2012/000696, International Search Report dated Nov. 7, 2012.
[cited by applicant]
International Patent Application No. PCT/CA2013/050821, International Preliminary Report on Patentability dated May 14, 2015.
[cited by applicant]
International Patent Application No. PCT/CA2013/050821, International Search Report dated Feb. 5, 2014.
[cited by applicant]
International Patent Application No. PCT/CA2016/050846, International Preliminary Report on Patentability dated Feb. 1, 2018.
[cited by applicant]
International Patent Application No. PCT/CA2016/050846, International Search Report and Written Opinion dated Sep. 14, 2016.
[cited by applicant]
Israel Patent Application No. 230575, Office Action dated Apr. 25, 2021—English Translation not available.
[cited by applicant]
Israel Patent Application No. 230575, Office Action dated Jan. 8, 2020—English Translation Available.
[cited by applicant]
Israel Patent Application No. 230575, Office Action dated May 23, 2018—English Translation available.
[cited by applicant]
Israel Patent Application No. IL230575, Office Action dated Dec. 11, 2016—English Translation available.
[cited by applicant]
Israeli Patent Application No. 238481, Office Action dated Nov. 6, 2017—English Translation available.
[cited by applicant]
Iversen et al., “Cell Kinetics of African Cases of Burkitt Lymphoma. A Preliminary Report,” European Journal of Cancer, Jun. 1972, vol. 8 (3), pp. 305-308.
[cited by applicant]
Jackson et al., “N-Terminal Mutations Activate the Leukemogenic Potential of the Myristoylated form ofc-abl,” The EMBO Journal, Feb. 1989, vol. 8 (2), pp. 449-456.
[cited by applicant]
Jaffe, “The 2008 WHO Classification of Lymphomas: Implications for Clinical Practice and Translational Research,” Hematology-American Society of Hematology Education Program, 2009, pp. 523-531.
[cited by applicant]
Jakobi., “Subcellular Targeting Regulates the Function of Caspase-Activated Protein Kinases in Apoptosis,” Drug Resistance Updates, Feb. 2004, vol. 7 (1), pp. 11-17.
[cited by applicant]
Japanese Patent Application No. 2014-520475, Notice of Allowance dated Dec. 4, 2017—English Translation Available.
[cited by applicant]
Japanese Patent Application No. 2014-520475, Office Action dated Apr. 10, 2017—English Translation available.
[cited by applicant]
Japanese Patent Application No. 2014-520475, Office Action dated May 09, 2016—English Translation available.
[cited by applicant]
Japanese Patent Application No. 2015-0538225, Office Action dated Jul. 10, 2017—with English Translation.
[cited by applicant]
Japanese Patent Application No. 2015-0538225, Office Action dated May 21, 2018—English Translation Available.
[cited by applicant]
Japanese Patent Application No. 2018-502095, Office Action dated Jul. 6, 2020—English Translation Available.
[cited by applicant]
Japanese Patent Application No. 2018-502095, Office Action dated Jun. 21, 2021—English Translation Available.
[cited by applicant]
Japanese Patent Application No. 20210176651, Office Action dated Nov. 7, 2022—English Translation Available.
[cited by applicant]
Juo et al., “Essential Requirement for Caspase-8/FLICE in the Initiation of the Fas-Induced Apoptotic Cascade,” Current Biology, Sep. 1998, vol. 8 (18), pp. 1001-1008.
[cited by applicant]
Kaelin., “The Concept of Synthetic Lethality in the Context of Anticancer Therapy,” Nature Reviews Cancer, Sep. 2005, vol. 5 (9), pp. 689-698.
[cited by applicant]
Kagawa et al., “Deficiency of Caspase-3 in MCF7 Cells Blocks Bax-mediated Nuclear Fragmentation but not Cell Death,” Clinical Cancer Research, May 2001, vol. 7 (5), pp. 1474-1480.
[cited by applicant]
Kamps et al., “Mutation of NH2-Terminal Glycine of p60src Prevents Both Myristoylation and Morphological Transformation,” Proceedings of the National Academy of Sciences, Jul. 1985, vol. 82 (14), pp. 4625-4628.
[cited by applicant]
Kasahara et al., “Rapid Trafficking of C-Src, a Non-Palmitoylated Src-Family Kinase, Between the Plasma Membrane and Late Endosomes/Lysosomes,” Experimental Cell Research, Jul. 2007, vol. 313 (12), pp. 2651-2666.
[cited by applicant]
Kay et al., “Tris (Dibenzylideneacetone) Dipalladium a Small-Molecule Palladium Complex is Effective in the Induction of Apoptosis for B-Chronic Lymphocytic Leukemia B-Cells,” Blood, Dec. 2011, vol. 118, pp. 2851. [retr…
[cited by applicant]
Kelly et al., “Burkitt Lymphoma: Revisiting the Pathogenesis of a Virus-Associated Malignancy,” Hematology American Society of Hematology Education Program, 2007, vol. 1, pp. 277-284.
[cited by applicant]
Kenkre et al., “Burkitt Lymphoma/Leukemia: Improving Prognosis,” Clinical Lymphoma, Myeloma & Leukemia Supplement, 2009, vol. 9 Suppl 3, pp. 3231-3238.
[cited by applicant]
Kim et al., “Src Kinases as Therapeutic Targets for Cancer,” Nature Reviews Clinical Oncology, Oct. 2009, vol. 6 (10), pp. 587-595.
[cited by applicant]
King et al., “Demonstration of Multiple Forms of Bovine Brain Myristoyl Coa:Protein N-Myristoyl Transferase,” Molecular and Cellular Biochemistry, Jul. 1992, vol. 113 (1), pp. 77-81.
[cited by applicant]
King et al., “Identification, Purification and Characterization of a Membrane-Associated N-Myristoyltransferase Inhibitor Protein from Bovine Brain,” Biochemical Journal, Apr. 1993, vol. 291 (Pt 2), pp. 635-639.
[cited by applicant]
King et al., “N-Myristoyl Transferase Assay Using Phosphocellulose Paper Binding,” Analytical Biochemistry, Dec. 1991, vol. 199 (2), pp. 149-153.
[cited by applicant]
Kishore et al., “The Substrate Specificity of
[cited by applicant]
Kojima et al., “Ghrelin is a Growth-Hormone-Releasing Acylated Peptide from Stomach,” Nature, Dec. 1999, vol. 402 (6762), pp. 656-660.
[cited by applicant]
Kon et al., “Chaperone-Mediated Autophagy in Health and Disease,” FEBS Letters, Apr. 2010, vol. 584 (7), pp. 1399-1404.
[cited by applicant]
Korean Patent Application No. 10-2014-7004635, Office Action dated May 27, 2019 English Translation Available.
[cited by applicant]
Korean Patent Application No. 10-2014-7004635, Office Action dated Oct. 16, 2018—English Translation Available.
[cited by applicant]
Korean Patent Application No. 10-2014-7004635, Office Action dated Sep. 6, 2019—English Translation Available.
[cited by applicant]
Korean Patent Application No. 10-2015-7014547, Notice of Grant dated Jan. 20, 2023—English Translation Not Available.
[cited by applicant]
Korean Patent Application No. 10-2015-7014547, Office Action dated Apr. 19, 2022—English Translation Available.
[cited by applicant]
Korean Patent Application No. 10-2015-7014547, Office Action dated Dec. 20, 2021—English Translation Available.
[cited by applicant]
Enari et al., “A Caspase-Activated Dnase That Degrades DNA During Apoptosis, and Its Inhibitor ICAD,” Nature, Jan. 1998, vol. 391 (6662), pp. 43-50.
[cited by applicant]
European Patent Application No. 12817041, Extended European Search Report dated Dec. 12, 2014.
[cited by applicant]
European Patent Application No. 12817041, Supplementary European Search Report dated Feb. 26, 2015.
[cited by applicant]
European Patent Application No. 12817041.2, European office action dated Jun. 2, 2022.
[cited by applicant]
European Patent Application No. 12817041.2, Office Action dated Dec. 20, 2017.
[cited by applicant]
European Patent Application No. 13852049, Extended European Search Report dated Jun. 28, 2016.
[cited by applicant]
European Patent Application No. 13852049, Partial European Search Report dated Feb. 25, 2016.
[cited by applicant]
European Patent Application No. 13852049.9, Communication pursuant to Article 94(3) EPC dated Oct. 6, 2017.
[cited by applicant]
European Patent Application No. 13852049.9, Office Action dated Nov. 20, 2018.
[cited by applicant]
European Patent Application No. 16826961.1, Communication pursuant to Article 94(3) EPC dated Dec. 4, 2019.
[cited by applicant]
European Patent Application No. 16826961.1, Communication pursuant to Article 94(3) EPC dated Feb. 23, 2021.
[cited by applicant]
European Patent Application No. 16826961.1, Extended European Search Report dated Dec. 5, 2018.
[cited by applicant]
European Patent Application No. 20213908.5, Extended European Search Report dated Jun. 9, 2021.
[cited by applicant]
Fadeel et al., “Apoptosis: a Basic Biological Phenomenon With Wide-Rnging Implications in Human Disease,” Journal of Internal Medicine, Dec. 2005, vol. 258 (6), pp. 479-517.
[cited by applicant]
Falkenberg et al., “Histone Deacetylases and Their Inhibitors in Cancer, Neurological Diseases and Immune Disorders,” Nature Reviews Drug Discovery, Sep. 2014, vol. 13 (9), pp. 673-691.
[cited by applicant]
Farazi et al., “The Biology and Enzymology of Protein N-Myristoylation,” The Journal of Biological Chemistry, Oct. 2001, vol. 276 (43), pp. 39501-39504.
[cited by applicant]
Farmer et al., “Targeting the Dna Repair Defect in Brca Mutant Cells as a Therapeutic Strategy,” Nature, Apr. 2005, vol. 434 (7035), pp. 917-921.
[cited by applicant]
FDA, Guidance for Industry and FDA Staff: Interpretation of the Term “Chemical Action” in the Definition of Device Under Section 201 (h) of the Federal Food, Drug, and Cosmetic Act. Accessed online at https://www.fda.go…
[cited by applicant]
FDA, Information for Consumers (Biosimilars). Accessed online at https://www.fda.gov/Drugs/DevelopmentApprovaiProcess/HowDrugsareDevelopedandApproved/ApprovaiApplications/TherapeuticBiologicApplications/Biosimilars/ucm2…
[cited by applicant]
Federal Register, 2001, vol. 66 (4), pp. 1099-1111.
[cited by applicant]
Feinberg et al., “The History of Cancer Epigenetics,” Nature Reviews Cancer, Feb. 2004, vol. 4 (2), pp. 143-153.
[cited by applicant]
Felsted et al., “Protein N-Myristoylation as a Chemotherapeutic Target for Cancer,” Journal of the National Cancer Institute, Nov. 1995, vol. 87 (211), pp. 1571-1573.
[cited by applicant]
Ferrara et al., “Cost-effectiveness Analysis of the Addition of Rituximab to CHOP in Young Patients With Good-prognosis Diffuse Large-B-cell Lymphoma,” Clinical Drug Investigation, 2008, vol. 28 (1), pp. 55-65.
[cited by applicant]
Fong et al., “Inhibition of Poly(ADP-Ribose) Polymerase in Tumors From BRCA Mutation Carriers,” The New England Journal of Medicine, Jul. 2009, vol. 361 (2), pp. 123-134.
[cited by applicant]
Foon et al., “Novel Therapies for Aggressive B-cell Lymphoma,” Advances in Hematology, 2012, vol. 2012, pp. 22.
[cited by applicant]
Frearson et al., “N-Myristoyltransferase Inhibitors as New Leads to Treat Sleeping Sickness,” Nature, Apr. 2010, vol. 464 (7289), pp. 728-732.
[cited by applicant]
French et al., “Cyclohexyl-Octahydro-Pyrrolo[1,2-a]Pyrazine-Based Inhibitors of Human N-Myristoyltransferase-1,” Journal of Pharmacology and Experimental Therapeutics, Apr. 2004, vol. 309 (1), pp. 340-347.
[cited by applicant]
Frottin et al., “The Proteomics of N-terminal Methionine Cleavage,” Molecular Cellular Proteomics, Dec. 2006, vol. 5 (12), pp. 2336-2349.
[cited by applicant]
Fukata et al., “Protein Palmitoylation in Neuronal Development and Synaptic Plasticity,” Nature Reviews Neuroscience, Mar. 2010, vol. 11 (3), pp. 161-175.
[cited by applicant]
Gamper et al., “Gene Expression Profile of Bladder Tissue of Patients with Ulcerative Interstitial Cystitis,” BMC Genomics, Apr. 28, 2009, vol. 10 (199), pp. 1-17.
[cited by applicant]
Gatto et al., “The Germinal Center Reaction,” The Journal of Allergy and Clinical Immunology, Nov. 2010, vol. 126 (5), pp. 898-907, quiz 908-9.
[cited by applicant]
Gebhart et al., “Genomic Imbalances in T-cell Acute Lymphoblastic Leukemia Cell Lines,” International Journal of Oncology, Apr. 2002, vol. 21 (4), pp. 887-894.
[cited by applicant]
Giang et al., “A Second Mammalian N-Myristoyltransferase,” The Journal of Biological Chemistry, Mar. 1998, vol. 273 (12), pp. 6595-6598.
[cited by applicant]
Glover et al., “Human N-Myristoyltransferase Amino-terminal Domain Involved in Targeting the Enzyme to the Ribosomal Subcellular Fraction,” The Journal of Biological Chemistry, Nov. 1997, vol. 272 (45), pp. 28680-28689.
[cited by applicant]
Goncalves et al., “A Fluorescence-Based Assay for N-Myristoyltransferase Activity,” Analytical Biochemistry, Feb. 2012, vol. 421 (1), pp. 342-344.
[cited by applicant]
Goncalves et al., “Discovery of Plasmodium Vivax N-myristoyltransferase Inhibitors: Screening, Synthesis, and Structural Characterization of their Binding Mode,” Journal of Medicinal Chemistry, Apr. 2012, vol. 55(7), pp…
[cited by applicant]
Greaves et al., “DHHC Palmitoyl Transferases: Substrate Interactions and (Patho) Physiology,” Trends in Biochemical Sciences, May 2011, vol. 36 (5), pp. 245-253.
[cited by applicant]
Griffin et al., “A Study of Rituximab and Ifosfamide, Carboplatin, and Etoposide Chemotherapy in Children with Recurrent/Refractory B-cell (CD20+) Non-Hodgkin Lymphoma and Mature B-Cell Acute Lymphoblastic Leukemia: A R…
[cited by applicant]
Gsselbrecht et al., “Salvage Regimens with Autologous Transplantation for Relapsed Large B-Cell Lymphoma in : he Rituximab Era,” Journal of Clinical Oncology, Sep. 2010, vol. 28 (27), pp. 4184-4190.
[cited by applicant]
Gui et al., “Histone Deacetylase (HDAC) Inhibitor Activation of p21WAF1 Involves Changes in Promoter Associated Proteins, Including HDAC1,” Proceedings of the National Academy of Sciences of the United States of America…
[cited by applicant]
Gutkowska et al., “Structure, Regulation and Cellular Functions of Rab Geranylgeranyl Transferase and is Cellular Partner Rab Escort Protein,” Molecular Membrane Biology, Nov. 2012, vol. 29 (7), pp. 243-256.
[cited by applicant]
Hancock et al., “All Ras Proteins are Polyisoprenylated but Only Some are Palmitoylated,” Cell, Jun. 1989, vol. 57 (7), pp. 1167-1177.
[cited by applicant]
Hang et al., “Chemical probes for the rapid detection of Fatty-acylated proteins in Mammalian cells.,” Journal of the American Chemical Society, Mar. 2007, vol. 129 (10), pp. 2744-2745.
[cited by applicant]
Hang et al., “Exploring Protein Lipidation With Chemical Biology,” Chemical Reviews, Oct. 2011, vol. 111 (10), pp. 6341-6358.
[cited by applicant]
Hannoush et al., “Imaging the Lipidome: omega-Alkynyl Fatty Acids for Detection and Cellular Visualization of Lipid-Modified Proteins,” ACS Chemical Biology, Jul. 2009, vol. 4 (7), pp. 581-587.
[cited by applicant]
Hannoush et al., “The Chemical Toolbox for Monitoring Protein Fatty Acylation and Prenylation,” Nature Chemical Biology, Jul. 2010, vol. 6 (7), pp. 498-506.
[cited by applicant]
Hantschel et al., “A Myristoyl/Phosphotyrosine Switch Regulates c-Abl,” Cell, Mar. 2003, vol. 112 (6), pp. 845-857.
[cited by applicant]
Harper et al., “Inhibition of Varicella-Zoster Virus Replication by an Inhibitor of Protein Myristoylation,” The Journal of General Virology, Jun. 1993, vol. 74 (Pt 6), pp. 1181-1184.
[cited by applicant]
Heal et al., “Bioorthogonal Chemical Tagging of Protein Cholesterylation in Living Cells,” Chemical Communications, Apr. 2011, vol. 47 (14), pp. 4081-4083.
[cited by applicant]
Hedo et al., “Myristyl and Palmityl Acylation of the Insulin Receptor,” The Journal of Biological Chemistry, Jan. 1987, vol. 262 (3), pp. 954-957.
[cited by applicant]
Sperandio et al., “An Alternative, Nonapoptotic form of Programmed Cell Death,” Proceedings of the National Academy of Sciences of the United States of America, Dec. 2000, vol. 97 (26), pp. 14376-14381.
[cited by applicant]
Stevenson et al., “Myristyl Acylation of the Tumor Necrosis Factor alpha Precursor on Specific Lysine Residues,” The Journal of Experimental Medicine, Oct. 1992, vol. 176 (4), pp. 1053-1062.
[cited by applicant]
Stevenson et al., “The 31-Kda Precursor of Interleukin 1 Alpha is Myristoylated on Specific Lysines Within the 16-Kda 4-Terminal Propiece,” Proceedings of the National Academy of Sciences of the United States of America…
[cited by applicant]
Sugii et al., “Performance Improvement in Protein N-Myristoyl Classification by BONSAI with Insignificant Indexing Symbol,” Genome Informatics, 2007, vol. 18, pp. 277-286.
[cited by applicant]
Suzuki and Bird., “DNA Methylation Landscapes: Provocative Insights From Epigenomics,” Nature Reviews Genetics, Jun. 2008, vol. 9, pp. 465-476.
[cited by applicant]
Suzuki et al., “Strategy for Comprehensive Identification of Human N-Myristoylated Proteins Using an Insect Cell-Free Protein Synthesis System,” Proteomics, May 2010, vol. 10 (9), pp. 1780-1793.
[cited by applicant]
Swerdlow, Who classification of tumours of haematopoietic and lymphoid tissues. Lyon: International Agency for Research on Cancer; GLOBOCAN 2012. Accessed Apr. 9, 2016 (5 pages) [online]. Retrieved from the Internet: UR…
[cited by applicant]
Takada et al., “Monounsaturated Fatty Acid Modification of Wnt Protein: Its Role in Wnt Secretion,” Development Cell, Dec. 2006, vol. 11 (6), pp. 791-801.
[cited by applicant]
Takamune et al., “Suppression of Human Immunodeficiency Virus Type-1 Production by Coexpression of Catalytic-Region-Deleted N-Myristoyltransferase Mutants,” Biological and Pharmaceutical Bulletin, 2010, vol. 33 (12), pp…
[cited by applicant]
Tate et al., “N-Myristoyltransferase as a Potential Drug Target in Malaria and Leishmaniasis,” Parasitology, Jan. 2014, vol. 141 (1), pp. 37-49.
[cited by applicant]
The Affordable Care Act. The Leukemia and Lymphoma Society. accessed on Oct. 30, 2013. The Affordable Care Act (2 pages) [online]. Retrieved from the Internet: URL: http://www.11s.org. search.
[cited by applicant]
Thinon et al., “Global Profiling of Co- and Post-Translationally N-Myristoylated Proteomes in Human Cells,” Nature Communications, Sep. 2014, vol. 5, 13 pages.
[cited by applicant]
Tomatis et al., “Acyl-Protein Thioesterase 2 Catalizes the Deacylation of Peripheral Membrane-Associated GAP-43,” PLoS One, Nov. 2010, vol. 5 (11), pp. e15045.
[cited by applicant]
Toska et al., “Repression of Transcription by WT1-BASP1 Requires the Myristoylation of BASP1 and the PIP2-Dependent Recruitment of Histone Deacetylase,” Cell Reports, Sep. 2012, vol. 2 (3), pp. 462-469.
[cited by applicant]
Towler et al., “Amino-Terminal Processing of Proteins by N-myristoylation. Substrate Specificity of N-myristoyl transferase,” The Journal of Biological Chemistry, Jan. 1987, vol. 262 (3), pp. 1030-1036.
[cited by applicant]
Towler et al., “Protein Fatty Acid Acylation: Enzymatic Synthesis of an N-Myristoylglycyl Peptide,” Proceedings of the National Academy of Sciences of the United States of America, May 1986, vol. 83 (9), pp. 2812-2816.
[cited by applicant]
Towler et al., “Purification and Characterization of Yeast Myristoyl CoA:Protein N-Myristoyltransferase,” Proceedings of the National Academy of Sciences of the United States of America, May 1987, vol. 84 (9), pp. 2708-…
[cited by applicant]
Traverso et al., “High-Throughput Profiling of N-Myristoylation Substrate Specificity Across Species Including Pathogens,” Proteomics, Jan. 2013, vol. 13 (1), pp. 25-36.
[cited by applicant]
Tsai et al., “Chemical Biology of Glycosylphosphatidylinositol Anchors,” Angewandte Chemie International Edition in English, Nov. 2012, vol. 51 (46), pp. 11438-11456.
[cited by applicant]
Turnay et al., “Structure-function Relationship in Annexin A13, the Founder Member of the Vertebrate Family of Annexins,” The Biochemical Journal, Aug. 2005, vol. 389 (Pt 3), pp. 899-911.
[cited by applicant]
Uniprot, NMT2_HUMAN: Protein Glycylpeptide N-tetradecanoyltransferase 2; Gene NMT2. Accessed online at http://www.uniprot.org/uniprot/060551 on Mar. 10, 2017, 11 pages.
[cited by applicant]
U.S. Appl. No. 14/234,312, Final Office Action dated Aug. 24, 2016.
[cited by applicant]
U.S. Appl. No. 14/234,312, Final Office Action dated Jan. 12, 2018.
[cited by applicant]
U.S. Appl. No. 14/234,312, Non-Final Office Action dated Mar. 31, 2017.
[cited by applicant]
U.S. Appl. No. 14/438,594, Final Office Action dated Oct. 2, 2017.
[cited by applicant]
U.S. Appl. No. 14/438,594, Non-Final Office Action dated Mar. 22, 2017.
[cited by applicant]
U.S. Appl. No. 15/745,578, Final Office Action dated Sep. 29, 2021.
[cited by applicant]
U.S. Appl. No. 15/745,578, Non Final office Action dated Oct. 4, 2022.
[cited by applicant]
U.S. Appl. No. 15/745,578, Non-Final Office Action dated Dec. 28, 2020.
[cited by applicant]
U.S. Appl. No. 15/943,068, Final office Action dated Dec. 20, 2021.
[cited by applicant]
U.S. Appl. No. 15/943,068, Non-Final Office Action dated May 17, 2021.
[cited by applicant]
U.S. Appl. No. 16/025,835, Non-Final Office Action dated May 31, 2019.
[cited by applicant]
U.S. Appl. No. 16/025,835, Notice of Allowance dated Aug. 27, 2021.
[cited by applicant]
U.S. Appl. No. 16/025,835, Notice of Allowance dated Feb. 5, 2021.
[cited by applicant]
U.S. Appl. No. 16/025,835, Notice of Allowance dated Jun. 9, 2021.
[cited by applicant]
U.S. Appl. No. 15/943,068, Final Office Action dated Oct. 30, 2020.
[cited by applicant]
U.S. Appl. No. 15/943,068, Non-Final Office Action dated Apr. 22, 2020.
[cited by applicant]
U.S. Appl. No. 16/025,835, Final Office Action dated Mar. 20, 2020.
[cited by applicant]
U.S. Appl. No. 15/745,578, Restriction Requirement dated Aug. 23, 2019.
[cited by applicant]
Uno et al., “Myristoylation of the Fus1 Protein is Required for Tumor Suppression in Human Lung Cancer Cells,” Cancer Research, May 2004, vol. 64 (9), pp. 2969-2976.
[cited by applicant]
Utsumi et al., “C-Terminal 15 kDa Fragment of Cytoskeletal Actin is Posttranslationally N-Myristoylated Upon Caspase-Mediated Cleavage and Targeted to Mitochondria,” FEBS Letters, Mar. 2003, vol. 539 (1-3), pp. 37-44.
[cited by applicant]
Utsumi et al., “Vertical-Scanning Mutagenesis of Amino Acids in a Model N-Myristoylation Motif Reveals the Major Amino-Terminal Sequence Requirements for Protein N-Myristoylation,” European Journal of Biochemistry, Feb.…
[cited by applicant]
Veer et al., “Enabling Personalized Cancer Medicine Through Analysis of Gene-Expression Patterns,” Nature, Apr. 2008, vol. 452 (7187), pp. 564-570.
[cited by applicant]
Vilas et al., “Posttranslational Myristoylation of Caspase'activated P21-Activated Protein Kinase 2 (PAK2) Potentiates Late Apoptotic Events,” Proceedings of the National Academy of Sciences of the United States of Amer…
[cited by applicant]
Wahlstrom et al., “Rce1 Deficiency Accelerates the Development of K-RAS-induced Myeloproliferative Disease,” Blood, Jan. 2007, vol. 109 (2), pp. 763-768.
[cited by applicant]
Walsh et al., “Executioner Caspase-3 and Caspase-7 are Functionally Distinct Proteases,” Proceedings of the National Academy of Sciences of the United States of America, Sep. 2008, vol. 105 (35), pp. 12815-12819.
[cited by applicant]
Wang et al., “Bioconjugation by Copper(I)-Catalyzed Azide-Alkyne [3 + 2] Cycloaddition,” Journal of the American Chemical Society, Mar. 2003, vol. 125 (11), pp. 3192-3193.
[cited by applicant]
Webb et al., “Inhibition of Protein Palmitoylation, Raft Localization, and T Cell Signaling by 2-bromopalmitate and Polyunsaturated Fatty Acids,” The Journal of Biological Chemistry, Jan. 2000, vol. 275 (1), pp. 261-270.
[cited by applicant]
Weinberg et al., “Genetic Studies Reveal that MyristoylCoA:protein N-Myristoyltransferase is an Essential Enzyme in Candida Albicans,” Molecular Microbiology, Apr. 1995, vol. 16 (2), pp. 241-250.
[cited by applicant]
Weston et al., “Crystal Structure of the Anti-Fungal Target N-Myristoyl Transferase,” Nature Structural Biology, Mar. 1998, vol. 5 (3), pp. 213-221.
[cited by applicant]
Decision to Grant for European Patent Application No. 16826961.1, mailed Aug. 3, 2023 (2 pages).
[cited by applicant]
Office Action for Japanese Patent Application No. 2021-176651, mailed Jul. 24, 2023 (with English Translation, 4 pages).
[cited by applicant]
European Patent Application No. 20213908.5, European Office Action dated Mar. 19, 2024 (5 pages).
[cited by applicant]
International Patent Application No. PCT/CA2016/050846, International Preliminary Report on Patentability dated Jan. 23, 2018 (8 pages).
[cited by applicant]
Japanese Patent Application No. 2018-502095, Office Action dated Apr. 24, 2023—incl English Lang Translation. (13 pages total).
[cited by applicant]
Notice of Intention to Grant for European Application No. 16826961.1, dated Mar. 13, 2023 (69 pages).
[cited by applicant]
Resh, M.D., “Regulation of Cellular Signalling by Fatty Acid Acylation and Prenylation of Signal Transduction Proteins,” Cell Signal. Sep. 1996;8(6):403-412.
[cited by applicant]
U.S. Appl. No. 15/745,578, Notice of Allowance dated May 24, 2023. (7 pages).
[cited by applicant]
U.S. Appl. No. 15/745,578, Notice of Allowance dated Sep. 6, 2023. (2 pages).
[cited by applicant]
U.S. Appl. No. 15/745,578, Notice of Allowance dated Aug. 10, 2023. (2 pages).
[cited by applicant]
Raju et al., “N-Myristoyltransferase Overexpression in Human Colorectal Adenocarcinomas,” Experimental Cell Research, Aug. 1997, vol. 235 (1), pp. 145-154.
[cited by applicant]
Raju et al., “Preparation and Assay of Myristoyl-CoA:Protein N-Myristoyltransferase,” Methods in Molecular Biology, 1999, vol. 116, pp. 193-211.
[cited by applicant]
Rasti et al., “Circulating Epstein-Barr Virus in Children Living in Malaria-Endemic Areas,” Scandinavian Journal of Immunology, May 2005, vol. 61 (5), pp. 461-465.
[cited by applicant]
Resh, “Fatty Acylation of Proteins: New Insights into Membrane Targeting of Myristoylated and Palmitoylated Proteins,” Biochimica et Biophysica Acta, Aug. 1999, vol. 1451 (1), pp. 1-16.
[cited by applicant]
Resh, “Myristylation and Palmitylation of Src Family Members: The Fats of the Matter,” Cell, Feb. 1994, vol. 76 (3), pp. 411-413.
[cited by applicant]
Resh, “Palmitoylation of Ligands, Receptors, and Intracellular Signaling Molecules,” Science's STKE : Signal Transduction Knowledge Environment, Oct. 2006, vol. 2006 (359), pp. re14.
[cited by applicant]
Resh, “Trafficking and Signaling by Fatty-Acylated and Prenylated Proteins,” Nature Chemical Biology, Nov. 2006, vol. 2 (11), pp. 584-590.
[cited by applicant]
Richter-Larrea et al., “Reversion of Epigenetically Mediated BIM Silencing Overcomes Chemoresistance in Burkit Ymphoma,” Blood, Oct. 2010, vol. 116 (14), pp. 2531-2542.
[cited by applicant]
Rioux et al., “Identification and Characterization of Recombinant and Native Rat Myristoyl-coa: Protein N-Myristoyltransferases,” Molecular and Cellular Biochemistry, Jun. 2006, vol. 286 (1-2), pp. 161-170.
[cited by applicant]
Rocks et al., “An Acylation Cycle Regulates Localization and Activity of Palmitoylated Ras Isoforms,” Science, Mar. 2005, vol. 307 (5716), pp. 1746-1752.
[cited by applicant]
Rocque et al., “A Comparative Analysis of the Kinetic Mechanism and Peptide Substrate Specificity of Human and
[cited by applicant]
Roskoski, “Protein Prenylation: A Pivotal Posttranslational Process,” Biochemical and Biophysical Research Communications, Mar. 2003, vol. 303 (1), pp. 1-7.
[cited by applicant]
Rostovtsev et al., “A Stepwise Huisgen Cycloaddition Process: Copper(I)-Catalyzed Regioselective Ligation of Azides and Terminal Alkynes,” Angewandte Chemie (International ed. in English), Jul. 2002, vol. 41 (14), pp. 2…
[cited by applicant]
Rouleau et al., “PARP Inhibition: PARP1 and Beyond,” Nature Reviews Cancer, Apr. 2010, vol. 10 (4), pp. 293-301.
[cited by applicant]
Rudel et al., “Membrane and Morphological Changes in Apoptotic Cells Regulated by Caspase-mediated Activation pf PAK2,” Science, 1997, vol. 276 (5318), pp. 1571-1574.
[cited by applicant]
Rudnick et al., “Analogs of Palmitoyl-CoA That are Substrates for Myristoyl-coa:protein N-Myristoyltransferase,” Proceedings of the National Academy of Sciences of the United States of America, Nov. 1992, vol. 89 (21), …
[cited by applicant]
Rudnick et al., “Kinetic and Structural Evidence for a Sequential Ordered Bi Bi Mechanism of Catalysis by
[cited by applicant]
Rudnick et al., “Studies of the Catalytic Activities and Substrate Specificities of
[cited by applicant]
Russian Patent Application No. 2014101787, Office Action dated Apr. 28, 2016—English Translation available.
[cited by applicant]
Russian Patent Application No. 2014101787, Office Action dated Aug. 30, 2016—English Translation available.
[cited by applicant]
Russian Patent Application No. 2014101787, Office Action dated Dec. 21, 2017—English Translation Available.
[cited by applicant]
Russian Patent Application No. 2014101787, Office Action dated Jun. 27, 2018—English Translation Available.
[cited by applicant]
Russian Patent Application No. 2015118294, Notice of Allowancedated Oct. 23, 2018—English Translation Available.
[cited by applicant]
Russian Patent Application No. RU2015118294, Office Action dated Jul. 7, 2017 with English Translation.
[cited by applicant]
Ryan et al., “Hedgehog Secretion and Signal Transduction in Vertebrates,” The Journal of Biological Chemistry, May 2012, vol. 287 (22), pp. 17905-17913.
[cited by applicant]
Saini et al., “Rituximab in Hodgkin Lymphoma: Is the Target Always a Hit?,” Cancer Treatment Reviews, Aug. 2011, vol. 37 (5), pp. 385-390.
[cited by applicant]
Sakurai et al., “Posttranslational N-myristoylation is Required for the Anti-apoptotic Activity of Human Tgelsolin, the C-terminal Caspase Cleavage Product of Human Gelsolin,” The Journal of Biological Chemistry, May 20…
[cited by applicant]
Sato et al., “Differential Trafficking of Src, Lyn, Yes and Fyn is Specified by the State of Palmitoylation in the SH4 Domain,” Journal of cell science, Apr. 2009, vol. 122 (Pt 7), pp. 965-975.
[cited by applicant]
Schey et al., “Novel Fatty Acid Acylation of Lens Integral Membrane Protein Aquaporin-0,” Biochemistry, 2010, vol. 49 (45), pp. 9858-9865.
[cited by applicant]
Schmidt-Supprian et al., “Excision of the Frt-flanked Neor Cassette From the CD19cre Knock-in Transgene Reduces 2, Re-Mediated Recombination,” Transgenic Research, Oct. 2007, vol. 16 (5), pp. 657-660.
[cited by applicant]
Seaton et al., “N-Myristoyltransferase Isozymes Exhibit Differential Specificity for Human Immunodeficiency Virus Type 1 Gag and Nef,” The Journal of General Virology, Jan. 2008, vol. 89 (Pt 1), pp. 288-296.
[cited by applicant]
SEER Cancer Statistics Review 1975-2010, [online]. URL: http://seer.cancer.govicsr/ 1975_2010/results_single/sect_01_table.01_pdf, 86 pages.
[cited by applicant]
Sehn et al., “Treatment of Aggressive Non-hodgkin's Lymphoma: A North American Perspective,” Oncology, Apr. 2005, vol. 19 (4 Suppl 1), pp. 26-34.
[cited by applicant]
Selvakumar et al., “N-myristoyltransferase 2 Expression in Human Colon Cancer: Cross-Talk Between the Calpain and Caspase System,” FEBS Letters, Apr. 2006, vol. 580 (8), pp. 2021-2026.
[cited by applicant]
Selvakumar et al., “Potential Role of N-Myristoyltransferase in Cancer,” Progress in Lipid Research, Jan. 2007, vol. 46 (1), pp. 1-36. Retrieved from Internet:[https://www.sciencedirect.com/science/article/abs/pii/S0163…
[cited by applicant]
Shawgo et al., “Caspase-9 Activation by the Apoptosome is Not Required for Fas-mediated Apoptosis in Type II Jurkat Cells,” The Journal of Biological Chemistry, Nov. 2009, vol. 284 (48), pp. 33447-33455.
[cited by applicant]
Sheng et al., “Homology Modeling and Molecular Dynamics Simulation of N-Myristoyltransferase From Protozoan Parasites: Active Site Characterization and Insights Into Rational Inhibitor Design,” Journal of Computer-Aided…
[cited by applicant]
Shrivastav et al., “Overexpression of Akt/PKB Modulates N-myristoyltransferase Activity in Cancer Cells,” The Journal of Pathology, Jul. 2009, vol. 218 (3), pp. 391-398.
[cited by applicant]
Shrivastav et al., “Potent Inhibitor of N-myristoylation: a Novel Molecular Target for Cancer,” Cancer Research, Nov. 2003, vol. 63 (22), pp. 7975-7978.
[cited by applicant]
Shrivastav et al., “Regulation of N-Myristoyltransferase by Novel Inhibitor Proteins,” Cell Biochemistry and Biophysics, Jan. 2005, vol. 43 (1), pp. 189-202. XP055143026. Retrieved from Internet:[ http://dx.doi.org/10.1…
[cited by applicant]
Sigal et al., “Amino-terminal Basic Residues of Src Mediate Membrane Binding Through Electrostatic Interaction With Acidic Phospholipids,” Proceedings of the National Academy of Sciences of the United States of America,…
[cited by applicant]
Sikorski et al., “Selective Peptidic and Peptidomimetic Inhibitors of Candida albicans MyristoylCoA: Protein N-Mlyristoyltransferase: A New Approach to Antifungal Therapy,” Biopolymers, 1997, vol. 43 (1), pp. 43-71.
[cited by applicant]
Silverman et al., “Lysine Residues Form an Integral Component of a Novel NH2-Terminal Membrane Targeting Motif for Myristylated pp60v-src,” The Journal of Cell Biology, Oct. 1992, vol. 119 (2), pp. 415-425.
[cited by applicant]
Singapore Patent Application No. SG10201703505V, Search Report and Written Opinion dated Jan. 6, 2023.
[cited by applicant]
Singapore Patent Application No. SG10201703505V, Search Report and Written Opinion dated Mar. 22, 2021.
[cited by applicant]
Singapore Patent Application No. SG20161005814Q, Notice of Allowance dated Dec. 1, 2022.
[cited by applicant]
Singh et al., “Autophagy Regulates Lipid Metabolism,” Nature, Apr. 2009, vol. 458 (7242), pp. 1131-1135.
[cited by applicant]
Sjogren et al., “Inactivating GGTase-I Reduces Disease Phenotypes in a Mouse Model of K-RAS-Induced Myeloproliferative Disease,” Leukemia, Jan. 2011, vol. 25 (1), pp. 186-189.
[cited by applicant]
Smotrys et al., “Palmitoylation of Intracellular Signaling Proteins: Regulation and Function,” Annual Review of Biochemistry, 2004, vol. 73, pp. 559-587.
[cited by applicant]
Solary et al., “Proteases, Proteolysis, and Apoptosis,” Cell Biology and Toxicology, Mar. 1998, vol. 14 (2), pp. 121-132.
[cited by applicant]
McIlhinney et al., “Purification and Partial Sequencing of Myristoyl-CoA: Protein N-Myristoyltransferase from Bovine Drain,” Biochemical Journal, Mar. 1993, vol. 290 (Pt 2), pp. 405-410.
[cited by applicant]
McLaughlin et al., “The Myristoyl-Electrostatic Switch: A Modulator of Reversible Protein-Membrane Nteractions,” Trends in Biochemical Sciences, Jul. 1995, vol. 20 (7), pp. 272-276.
[cited by applicant]
McTaggart, “Isoprenylated Proteins,” Cellular and Molecular Life Sciences, Feb. 2006, vol. 63 (3), pp. 255-267.
[cited by applicant]
Merck Manual, 18th Edition, Japanese Edition, Nikkei BP, Apr. 25, 2007, pp. 1177-1186—English Translation available.
[cited by applicant]
Mexican Patent Application No. 20140000661, Office Action dated Mar. 8, 2017.
[cited by applicant]
Mexican Patent Application No. MX/a/2014/000661, Office Action dated Aug. 7, 2018—English Translation Not Available.
[cited by applicant]
Mexican Patent Application No. MX/a/2014/000661, Office Action dated Nov. 6, 2017—With Unofficial English Translation.
[cited by applicant]
Mexican Patent Application No. MX/a/2015/005441, Office Action dated Dec. 7, 2018—English Translation Not Available.
[cited by applicant]
Miles et al., “Risk Factors and Treatment of Childhood and Adolescent Burkitt Lymphoma/Leukaemia,” British Journal of Haematology, Mar. 2012, vol. 156 (6), pp. 730-743.
[cited by applicant]
Mishkind, “Morbid Myristoylation,” Trends in Cell Biology, May 2001, vol. 11 (5), pp. 191.
[cited by applicant]
Mitchell et al., “Protein Palmitoylation by a Family of Dhhc Protein S-Acyltransferases,” Journal of Lipid Research, Jun. 2006, vol. 47 (6), pp. 1118-1127.
[cited by applicant]
Moffitt et al., “From Sentencing to Execution—The Processes of Apoptosis,” The Journal of Pharmacy and Pharmacology, May 2010, vol. 62 (5), pp. 547-562.
[cited by applicant]
Molyneux et al., “Burkitt's Lymphoma,” Lancet (London, England), Mar. 2012, vol. 379 (9822), pp. 1234-1244.
[cited by applicant]
Moore et al., “DNA Methylation and Its Basic Function,” Neuropsychopharmacology, 2013, vol. 38, pp. 23-38.
[cited by applicant]
Morgan et al., “Modulation of Anthracycline-Induced Cytotoxicity by Targeting the Prenylated Proteome in Myeloid Eukemia Cells,” Journal of Molecular Medicine (Berlin, Germany), Feb. 2012, vol. 90 (2), pp. 149-161.
[cited by applicant]
Nagata, “Apoptotic DNA Fragmentation,” Experimental Cell Research, Apr. 2000, vol. 256 (1), pp. 12-18.
[cited by applicant]
New Zealand Patent Application No. 620167, First Examination Report dated Nov. 24, 2014.
[cited by applicant]
New Zealand Patent Application No. 707090, Examination Report dated Mar. 20, 2018.
[cited by applicant]
New Zealand Patent Application No. 707090, Office Action dated Nov. 13, 2018.
[cited by applicant]
New Zealand Patent Application No. 720441, First Examination Report dated May 25, 2016.
[cited by applicant]
New Zealand Patent Application No. 737605, Examination Report dated Apr. 12, 2018.
[cited by applicant]
New Zealand Patent Application No. 737605, Examination Report dated Jul. 28, 2022.
[cited by applicant]
New Zealand Patent Application No. 737605, Notice of Acceptance dated Nov. 15, 2022.
[cited by applicant]
New Zealand Patent Application No. 794388, Examination Report dated Nov. 15, 2022.
[cited by applicant]
Nimchuk et al., “Eukaryotic Fatty Acylation Drives Plasma Membrane Targeting and Enhances Function of Several Type Iii Effector Proteins From Pseudomonas Syringae,” Cell, May 2000, vol. 101 (4), pp. 353-363.
[cited by applicant]
Novelli et al., “Protein Farnesylation and Disease,” Journal of Inherited Metabolic Disease, Sep. 2012, vol. 35 (5), pp. 917-926.
[cited by applicant]
Ntwasa et al., “
[cited by applicant]
Ntwasa et al., “Sequence and Expression of
[cited by applicant]
Ohno et al., “Intracellular Localization and Tissue-Specific Distribution of Human and Yeast DHHC Cysteine-Rich Domain-Containing Proteins,” Biochimica et Biophysica Acta, Apr. 2006, vol. 1761 (4), pp. 474-483.
[cited by applicant]
Olsson et al., “Caspases and Cancer,” Cell Death and Differentiation, Sep. 2011, vol. 18 (9), pp. 1441-1449.
[cited by applicant]
Paige et al., “Metabolic Activation of 2-Substituted Derivatives of Myristic Acid to Form Potent Inhibitors of Myristoyl CoA:Protein N-Myristoyltransferase,” Biochemistry, Nov. 1990, vol. 29 (46), pp. 10566-10573.
[cited by applicant]
Panethymitaki et al., “Characterization and Selective Inhibition of Myristoyl-CoA:protein N-myristoyltransferase From Trypanosoma Brucei and Leishmania Major,” The Biochemical Journal, Jun. 2006, vol. 396 (2), pp. 277-2…
[cited by applicant]
Parekh et al, “Therapeutic Targeting of the BCL6 Oncogene for Diffuse Large B-cell Lymphomas,” Leukemia and Lymphoma, May 2008, vol. 49 (5), pp. 874-882.
[cited by applicant]
Patwardhan et al., “Myristoylation and Membrane Binding Regulate c-Src Stability and Kinase Activity,” Molecular and Cellular Biology, Sep. 2010, vol. 30 (17), pp. 4094-4107.
[cited by applicant]
Paulick et al., “The Glycosylphosphatidylinositol Anchor: A Complex Membrane-Anchoring Structure for Proteins,” Biochemistry, Jul. 2008, vol. 47 (27), pp. 6991-7000.
[cited by applicant]
Pegram et al., “Rational Combinations of Trastuzumab With Chemotherapeutic Drugs Used in the Treatment of Breast Cancer,” Journal of the National Cancer Institute, May 2004, vol. 96 (10), pp. 739-749.
[cited by applicant]
Peitzsch et al., “Binding of Acylated Peptides and Fatty Acids to Phospholipid Vesicles: Pertinence to Vlyristoylated Proteins,” Biochemistry, Oct. 1993, vol. 32 (39), pp. 10436-10443.
[cited by applicant]
Perinpanayagam et al., “Regulation of Co- and Post-Translational Myristoylation of Proteins During Apoptosis: Nterplay of N-Myristoyltransferases and Caspases,” The FASEB Journal, Feb. 2013, vol. 27 (2), pp. 811-821.
[cited by applicant]
Perkins et al., “Burkitt Lymphoma in Adults,” Hematology American Society of Hematology Education Program, 2008, pp. 341-348.
[cited by applicant]
Peseckis et al., “Fatty Acyl Transfer by Human N-Myristyl Transferase is Dependent Upon Conserved Cysteine and Histidine Residues,” The Journal of Biological Chemistry, Dec. 1994, vol. 269 (49), pp. 30888-30892.
[cited by applicant]
Peseckis et al., “Iodinated Fatty Acids as Probes for Myristate Processing and Function. Incorporation into pp60v-src.1,” The Journal of Biological Chemistry, Mar. 1993, vol. 268 (7), pp. 5107-5114.
[cited by applicant]
Phan et al., “The BCL6 Proto-Oncogene Suppresses P53 Expression in Germinal-Centre B Cells,” Nature, Dec. 2004, vol. 432 (7017), pp. 635-639.
[cited by applicant]
Podell, “Predicting N-Terminal Myristoylation Sites in Plant Proteins,” BMC Genomics. Jun. 2004, 17 (51): 37.
[cited by applicant]
Porter et al., “Cholesterol Modification of Hedgehog Signaling Proteins in Animal Development,” Science, Oct. 1996, vol. 274 (5285), pp. 255-259.
[cited by applicant]
Prasad et al., “N-Myristoyltransferase: A Novel Target,” Mini-Reviews in Medicinal Chemistry, Feb. 2008, vol. 8 (2), pp. 142-149.
[cited by applicant]
Price et al., “Myristoyl-CoA:Protein N-Myristoyltransferase, an Essential Enzyme and Potential Drug Target in Kinetoplastid Parasites,” The Journal of Biological Chemistry, Feb. 2003, vol. 278 (9), pp. 7206-7214.
[cited by applicant]
De La Puente et al., “Tris DBA Palladium Overcomes Hypoxia Mediated Drug Resistance in Multiple Myeloma,” Journal of Blood, 2015, p. 2978.
[cited by applicant]
Rackham et al., “Discovery of Novel and Ligand-Efficient Inhibitors of Plasmodium Falciparum and Plasmodium Vivax N-myristoyltransferase,” Journal of Medicinal Chemistry, Jan. 2013, vol. 56(1), pp. 371-375.
[cited by applicant]
Rajala et al., “Increased Expression of N-Myristoyltransferase in Gallbladder Carcinomas,” Cancer, May 2000, vol. 38 (9), pp. 1992-1999.
[cited by applicant]
Raju et al., “Molecular Cloning and Biochemical Characterization of Bovine Spleen Myristoyl CoA:Protein N-Vlyristoyltransferase,” Archives Biochemistry Biophysics, Dec. 1997, vol. 348 (1), pp. 134-142.
[cited by applicant]
Wikipedia, Definition: Small molecule. Accessed online at https://en.wikipedia.org/wiki/Small_molecule on Mar. 10, 2017, 4 pages.
[cited by applicant]
Wilcox et al., “Acylation of Proteins With Myristic Acid Occurs Cotranslationally,” Science, Nov. 1987, vol. 238 (4831), pp. 1275-1278.
[cited by applicant]
Willert et al., “Wnt Proteins are Lipid-Modified and can Act as Stem Cell Growth Factors,” Nature, May 2003, vol. 423 (6938), pp. 448-452.
[cited by applicant]
Wright et al., “Protein Myristoylation in Health and Disease,” Journal of Chemical Biology, Mar. 2010, vol. 3 (1), pp. 19-35.
[cited by applicant]
Wright et al., “Validation of N-myristoyltransferase as an Antimalarial Drug Target Using an Integrated Chemical Biology Approach,” Nature Chemistry, Feb. 2014, vol. 6(2), pp. 112-121.
[cited by applicant]
Written Opinion for Application No. PCT/CA2012/000696, mailed on Nov. 7, 2012, 7 pages.
[cited by applicant]
Written Opinion for Application No. PCT/CA2013/050821, mailed on Feb. 5, 2014, 8 pages.
[cited by applicant]
Wu et al., “Crystal Structures of
[cited by applicant]
Wu et al., “Necroptosis: An Emerging Form of Programmed Cell Death,” Critical Reviews in Oncology/hematology, Jun. 2012, vol. 82 (3), pp. 249-258.
[cited by applicant]
Yang et al., “Identification of the Acyltransferase that Octanoylates Ghrelin, an Appetite-Stimulating Peptide Hormone,” Cell, Feb. 2008, vol. 132 (3), pp. 387-396.
[cited by applicant]
Yang et al., “N-Myristoyltransferase 1 is Essential in Early Mouse Development,” The Journal of Biological Chemistry, May 2005, vol. 280 (19), pp. 18990-18995.
[cited by applicant]
Yap et al., “Rapid and Selective Detection of Fatty Acylated Proteins Using Omega-Alkynyl-Fatty Acids and Click Chemistry,” Clinical Cancer Research, Jun. 2010, vol. 51 (6), pp. 1566-1580.
[cited by applicant]
Youle et al., “The BCL-2 Protein Family: Opposing Activities that Mediate Cell Death,” Nature Reviews Molecular Cell Biology, Jan. 2008, vol. 9 (1), pp. 47-59.
[cited by applicant]
Yustein et al., “Biology and Treatment of Burkitt's Lymphoma,” Current Opinion in Hematology, Jul. 2007, vol. 14 (4), pp. 375-381.
[cited by applicant]
Zha, “Posttranslational N-Myristoylation of BID as a Molecular Switch for Targeting Mitochondria and Apoptosis,” Science, Dec. 2000, vol. 290 (5497), pp. 1761-1765.
[cited by applicant]
Zhang et al., “Down-Regulation of NKD1 Increases the Invasive Potential of Non-Small-Cell Lung Cancer and Correlates with a Poor Prognosis,” BMC Cancer, May 2011, vol. 11, pp. 186.
[cited by applicant]
Zhang et al., “Protein Prenylation: Molecular Mechanisms and Functional Consequences,” Annual Review of Biochemistry, 1996, vol. 65, pp. 241-269.
[cited by applicant]
Zhao et al., “Palmitoylation of Apolipoprotein B is Required for Proper Intracellular Sorting and Transport of Cholesteroyl Esters and Triglycerides,” Molecular Biology of the Cell, Feb. 2000, vol. 11 (2), pp. 721-734.
[cited by applicant]
Zverina et al., “Recent Advances in Protein Prenyltransferases: Substrate Identification, Regulation, and Disease—Interventions,” Current Opinion in Chemical Biology, Dec. 2012, vol. 16 (5-6), pp. 544-552.
[cited by applicant]
Korean Patent Application No. 10-2015-7014547, Office Action dated Feb. 22, 2021—English Translation Available.
[cited by applicant]
Korean Patent Application No. 10-2015-7014547, Office Action dated Mar. 6, 2020—English Translation Available.
[cited by applicant]
Korean Patent Application No. 10-2022-7009175, Office Action dated Jul. 7, 2022—English Translation Available.
[cited by applicant]
Korycka et al., “Human DHHC Proteins: A Spotlight on the Hidden Player of Palmitoylation,” The European Journal of Cell Biology, Feb. 2012, vol. 91 (2), pp. 107-117.
[cited by applicant]
Kosciuk et al., “N-Myristoyltransferase as a Glycine and Lysine Myristoyltransferase in Cancer, Immunity, and Infections,” ACS Chemical Biology, Jul. 2020, vol. 15 (7), pp. 1747-1758.
[cited by applicant]
Kostiuk et al., “Identification of Palmitoylated Mitochondrial Proteins Using a Bio-orthogonal Azido-palmitate Analogue,” FASEB Journal, Mar. 2008, vol. 22 (3), pp. 721-732.
[cited by applicant]
Kovalchuk et al., “Burkitt Lymphoma in the Mouse,” The Journal of Experimental Medicine, Oct. 2000, vol. 192 (8), pp. 1183-1190.
[cited by applicant]
Kuang et al., “Genome-wide Identification of Aberrantly Methylated Promoter Associated 1-3 and 32-81 Cpg Islands in Acute Lymphocytic Leukemia,” Leukemia, Aug. 2008, vol. 22 (8), pp. 1529-1538.
[cited by applicant]
Kumar et al., “The Potential Use of N-Myristoyltransferase as a Biomarker in the Early Diagnosis of Colon Cancer,” Cancers (Basel), Mar. 2011, vol. 3 (1), pp. 1372-1382.
[cited by applicant]
Kuppers, “Mechanisms of B-cell Lymphoma Pathogenesis,” Nature Reviews Cancer, Apr. 2005, vol. 5 (4), pp. 251-262.
[cited by applicant]
Laemmli, “Cleavage of Structural Proteins During the Assembly of the Head of Bacteriophage T4,” Nature, Aug. 1970, vol. 227 (5259), pp. 680-685.
[cited by applicant]
Lane et al., “Histone Deacetylase Inhibitors in Cancer Therapy,” Journal of Clinical Oncology, Nov. 2009, vol. 27 (32), pp. 5459-5468.
[cited by applicant]
Leatherbarrow, “Grafit User's Guide (Version 6),” Erithacus Software Ltd., Horley, United Kingdom. 2009, pp. 1-294.
[cited by applicant]
Lee , “A Capacitance-Based Method for Experimental Determination of Metallurgical Channel Length of Submicron LDD MOSFET's,” IEEE Transactions on Electron Devices, Mar. 1994, vol. 41 (3), pp. 403-412.
[cited by applicant]
Lee et al., “Costs Associated with Diffuse Large B-Cell Lymphoma Patient Treatment in a Canadian Integrated Cancer are Center,” Value Health , Mar.-Apr. 2008 , vol. 11 (2) , pp. 221-230.
[cited by applicant]
Lee et al., “Prognosis of Chronic Lymphocytic Leukemia: a Multivariate Regression Analysis of 325 Untreated Patients,” Blood, Mar. 1987, vol. 69 (3), pp. 929-936.
[cited by applicant]
Lenz et al., “Aggressive Lymphomas,” The New England Journal of Medicine, Apr. 2010, vol. 362 (15), pp. 1417-1429.
[cited by applicant]
Leuenroth et al., “The Loss of Mcl-1 Expression in Human Polymorphonuclear Leukocytes Promotes Apoptosis,” Journal of Leukocyte Biology, Jul. 2000, vol. 68 (1), pp. 158-166.
[cited by applicant]
Liang et al., “Mass Spectrometric Analysis of GAP-43/neuromodulin Reveals the Presence of a Variety of Fatty Acylated Species,” The Journal of Biological Chemistry, Sep. 2002, vol. 277 (36), pp. 33032-33040.
[cited by applicant]
Liang et al., “The N-Terminal SH4 Region of the Src Family Kinase Fyn is Modified by Methylation and Heterogeneous Fatty Acylation: Role in Membrane Targeting, Cell Adhesion, and Spreading,” The Journal of Biological Ch…
[cited by applicant]
Lim et al., (Abstract) P004:Understanding the roles of NMT1 and NMT2 cancers. Accessed online at https://www.biochemistry.org/Portals/O/Conferences/Abstracts/SA164/SA164P004.pdf on Mar. 10, 2017, 1 page.
[cited by applicant]
Lin et al., “Protein Lysine Acylation and Cysteine Succination by Intermediates of Energy Metabolism,” ACS Chemical Biology, Jun. 2012, vol. 7 (6), pp. 947-960.
[cited by applicant]
Liston et al., “The Inhibitors of Apoptosis: There is More to Life Than Bcl2,” Oncogene, Nov. 2003, vol. 22 (53), pp. 8568-8580.
[cited by applicant]
Liu et al., “Targeting the Protein Prenyltransferases Efficiently Reduces Tumor Development in Mice With K-RAS-Induced Lung Cancer,” Proceedings of the National Academy of Sciences of the United States of America, Apr. …
[cited by applicant]
Lobo et al., “Identification of a Ras Palmitoyltransferase in
[cited by applicant]
Lodge et al., “Comparison of Myristoyl-CoAProtein N-Myristoyltransferases from Three Pathogenic Fungi: Cryptococcus Neoformans,” The Journal of Biological Chemistry, Jan. 1994, vol. 269 (4), pp. 2996-3009.
[cited by applicant]
Lodge et al., “Targeted Gene Replacement Demonstrates That Myristoyl-CoA: Protein N-myristoyltransferase is Essential for Viability of Cryptococcus Neoformans,” Proceedings of the National Academy of Sciences of the Uni…
[cited by applicant]
Love et al., “The Genetic Landscape of Mutations in Burkitt Lymphoma,” Nature Genetics, Dec. 2012, vol. 44 (12), pp. 1321-1325.
[cited by applicant]
Lu et al., “Expression of N-myristoyltransferase in Human Brain Tumors,” Neurochemical Research, Jan. 2005, vol. 30 (1), pp. 9-13. Retrieved from Internet:[ http:https://www.ncbi.nlm.nih.gov/pubmed?term=((%22Neurochemic…
[cited by applicant]
Luciano et al., “Phosphorylation of Bim-el by Erk1/2 on Serine 69 Promotes Its Degradation via the Proteasome Pathway and Regulates Its Proapoptotic Function,” Oncogene, Oct. 2003, vol. 22 (43), pp. 6785-6793.
[cited by applicant]
Lueg et al., “N-myristoyltransferase Inhibition Is Synthetic Lethal in MYC-Deregulated Cancers,” BioRxiv, Mar. 20, 2021, 25 pages, Retrieved from [URL:https://doi.org/10.1101/2021.03.20.436222].
[cited by applicant]
Mackey et al., “N-Myristoyltransferase Proteins in Breast Cancer: Prognostic Relevance and Validation as a New Drug Target,” Breast Cancer Research and Treatment, Jan. 2021, 7 pages.
[cited by applicant]
Magee et al., “Fatty Acylation and Prenylation of Proteins: What's Hot in Fat,” Current Opinion in Cell Biology, Apr. 2005, vol. 17 (2), pp. 190-196.
[cited by applicant]
Magnuson et al., “Increased N-Myristoyltransferase Activity Observed in Rat and Human Colonic Tumors,” Journal of the National Cancer Institute, Nov. 1995, vol. 87 (21), pp. 1630-1635.
[cited by applicant]
Mahrus et al., “Global Sequencing of Proteolytic Cleavage Sites in Apoptosis by Specific Labeling of Protein N Termini,” Cell, Sep. 2008, vol. 134 (5), pp. 866-876.
[cited by applicant]
Mann et al., “Novel Lipid Modifications of Secreted Protein Signals,” Annual Review of Biochemistry, 2004, vol. 73, pp. 891-923.
[cited by applicant]
Martin et al., “Large-Scale Profiling of Protein Palmitoylation in Mammalian Cells,” Nature Methods, Feb. 2009, vol. 6 (2), pp. 135-138.
[cited by applicant]
Martin et al., “Post-Translational Myristoylation: Fat Matters in Cellular Life and Death,” Biochimie, Jan. 2011, vol. 93 (1), pp. 18-31.
[cited by applicant]
Martin et al., “Rapid Detection, Discovery, and Identification of Post-translationally Myristoylated Proteins During Apoptosis Using a Bio-orthogonal Azidomyristate Analog,” FASEB Journal, Mar. 2008, vol. 22 (3), pp. 79…
[cited by applicant]
Martin et al., “Tandem Reporter Assay for Myristoylated Proteins Post-translationally (TRAMPP) Identifies Novel Substrates for Post-Translational Myristoylation: PKCK, a Case Study,” FASEB Journal, Jan. 2012, vol. 26 (1…
[cited by applicant]
Massadi et al., “Ghrelin Acylation and Metabolic Control,” Peptides, Nov. 2011, vol. 32 (11), pp. 2301-2308.
[cited by applicant]
Matheson et al., “The Conservation of Amino Acids in the N-Terminal Position of Ribosomal and Cytosol Proteins from
[cited by applicant]
Maurer-Stroh et al., “N-Terminal N-Myristoylation of Proteins: Prediction of Substrate Proteins from Amino Acid Sequence,” Journal of Molecular Biology, Apr. 2002, vol. 317 (4), pp. 541-557.
[cited by applicant]
Maurer-Stroh et al., “N-Terminal N-Myristoylation of Proteins: Refinement of the Sequence Motif and its Taxon-Specific Differences,” Journal of Molecular Biology, Apr. 2002, vol. 317 (4), pp. 523-540.
[cited by applicant]
Maurer-Stroh et al., “Refinement and Prediction of Protein Prenylation Motifs,” Genome Biology, 2005, vol. 6 (6), pp. R55.
[cited by applicant]
Mayor et al., “Sorting GPI-Anchored Proteins,” Sorting GPI-Anchored Proteins, Feb. 2004, vol. 5 (2), pp. 110-120.
[cited by applicant]
McCabe et al., “Functional Roles for Fatty Acylated Amino-terminal Domains in Subcellular Localization,” Molecular Biology of the Cell, Nov. 1999, vol. 10 (11), pp. 3771-3786.
[cited by applicant]
McCabe et al., “N-Terminal Protein Acylation Confers Localization to Cholesterol, Sphingolipid-enriched Vlembranes But Not to Lipid Raffs/Caveolae,” Molecular Biology of the Cell, Nov. 2001, vol. 12 (11), pp. 3601-3617.
[cited by applicant]
McIlhinney et al., “Characterization and Cellular Localization of Human Myristoyl-Coa: Protein N-Myristoyltransferase,” Biochemical Society Transactions, Aug. 1995, vol. 23 (3), pp. 549-553.
[cited by applicant]
McIlhinney et al., “Immunocytochemical Characterization and Subcellular Localization of Human Vlyristoyl-CoA: Protein N-Myristoyltransferase in HeLa Cells.,” Experimental Cell Research, Mar. 1996, vol. 223 (2), pp. 348-…
[cited by applicant]
Canadian Patent Application No. 2,842,443, Office Action dated May 9, 2018.
[cited by applicant]
Canadian Patent Application No. 2,842,443, Office Action dated Nov. 15, 2019.
[cited by applicant]