IP Library Granted Patent US 12,252,540
Granted Patent B2
US 12,252,540 · App. 17/332,578 · Granted Mar 18, 2025

Nucleic acid molecules encoding binding proteins for gastric inhibitory peptide receptor (GIPR)

Inventors: Junming Yie (Warren, NJ); Donghui Shi (Thousand Oaks, CA); David J. Lloyd (Thousand Oaks, CA); Jinghong Wang (Palo Alto, CA); Glenn N. Sivits, Jr. (Newbury Park, CA); Murielle M. Veniant-Ellison (Thousand Oaks, CA); Renee Komorowski (Ventura, CA); Neeraj Agrawal (Thousand Oaks, CA); Darren L. Bates (Oak Park, CA); Brandon C. P. Clavette (Coquitlam, CA); Ian N. Foltz (Burnaby, CA); Shu-yin Ho (Thousand Oaks, CA); Christopher Murawsky (Roberts Creek, CA); Xiaoshan Min (Burlingame, CA); Zhulun Wang (Palo Alto, CA)
Assignee: Amgen Inc.
C07K16/2869A61K9/0019A61K38/1703A61K38/26A61K39/3955A61K2039/505A61K2039/54C07K2299/00C07K2317/21C07K2317/32C07K2317/33C07K2317/41C07K2317/52C07K2317/71C07K2317/76C07K2317/92
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Quick Facts
Patent No.
US 12,252,540
App. No.
17/332,578
Granted
Mar 18, 2025
Kind
B2
Abstract

Methods of treating metabolic diseases and disorders using an antigen binding protein specific for the GIPR polypeptide are provided. In various embodiments the metabolic disease or disorder is type 2 diabetes, obesity, dyslipidemia, elevated glucose levels, elevated insulin levels and diabetic nephropathy. In certain embodiments the antigen binding protein is administered in combination with a GLP-1 receptor agonist.

Claims (8)

1. A nucleic acid molecule encoding an antibody selected from the group consisting of:

a) an antibody comprising a CDRL1, a CDRL2, a CDRL3, a CDRH1, a CDRH2, and a CDRH3, wherein said CDRL1 comprises SEQ ID NO: 702; said CDRL2 comprises SEQ ID NO: 859; said CDRL3 comprises SEQ ID NO: 1016; said CDRH1 comprises SEQ ID NO: 1173; said CDRH2 comprises SEQ ID NO: 1330; and said CDRH3 comprises SEQ ID NO: 1487;

b) an antibody comprising a light chain variable region comprising SEQ ID NO: 74 and a heavy chain variable region comprising SEQ ID NO: 231; and

c) an antibody comprising a light chain comprising SEQ ID NO: 388 and a heavy chain comprising SEQ ID NO: 545.

2. The nucleic acid molecule according to claim 1 , wherein said nucleic acid molecule is operably linked to a control sequence.

3. A vector comprising a nucleic acid molecule according to claim 2 .

4. A host cell comprising the nucleic acid molecule according to claim 3 .

5. A method of making the antibody, comprising the step of preparing said antibody from a host cell of claim 4 .

Assignments (1)
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Oct 6, 2022
From: YIE, JUMMING; SHI, DONGHUI; LLOYD, DAVID J.; WANG, JINGHONG; SIVITS, GLENN N., JR.; VENIANT-ELLISON, MURIELLE M.; KOMOROWSKI, RENEE; AGRAWAL, NEERAJ; BATES, DARREN L; CLAVETTE, BRANDON C. P.; FOLTZ, IAN N.; HO, SHU-YIN; MURAWSKY, CHRISTOPHER; MIN, XIAOSHAN; WANG, ZHULUN
To: AMGEN INC.
Reel/Frame 061334/0365 →
Continuity (6)
Division 16285118 · Feb 25, 2019
Division 15387542 · Dec 21, 2016
Provisional Application 62420415 · Nov 10, 2016
Provisional Application 62337799 · May 17, 2016
Provisional Application 62387486 · Dec 23, 2015
Related Publication 20220025059A1 · Jan 27, 2022
References Cited (400)
US 3773919A · Boswell et al. · 1973 [cited by applicant]
US 4399216A · Axel et al. · 1983 [cited by applicant]
US 4619794A · Hauser · 1986 [cited by applicant]
US 4740461A · Kaufman · 1988 [cited by applicant]
US 4816567A · Cabilly et al. · 1989 [cited by applicant]
US 4912040A · Kaufman et al. · 1990 [cited by applicant]
US 4946778A · Ladner et al. · 1990 [cited by applicant]
US 4959455A · Clark et al. · 1990 [cited by applicant]
US 4965195A · Namen et al. · 1990 [cited by applicant]
US 4968607A · Dower et al. · 1990 [cited by applicant]
US 5011912A · Hopp et al. · 1991 [cited by applicant]
US 5260203A · Ladner et al. · 1993 [cited by applicant]
US 5292658A · Cormier et al. · 1994 [cited by applicant]
US 5418155A · Cormier et al. · 1995 [cited by applicant]
US 5470582A · Supersaxo et al. · 1995 [cited by applicant]
US 5530101A · Queen et al. · 1996 [cited by applicant]
US 5545618A · Buckley et al. · 1996 [cited by applicant]
US 5545806A · Lonberg et al. · 1996 [cited by applicant]
US 5545807A · Surami et al. · 1996 [cited by applicant]
US 5569825A · Lonberg et al. · 1996 [cited by applicant]
US 5585089A · Queen et al. · 1996 [cited by applicant]
US 5625126A · Lonberg et al. · 1997 [cited by applicant]
US 5633425A · Lonberg et al. · 1997 [cited by applicant]
US 5661016A · Lonberg et al. · 1997 [cited by applicant]
US 5683888A · Campbell · 1997 [cited by applicant]
US 5693761A · Queen et al. · 1997 [cited by applicant]
US 5693762A · Queen et al. · 1997 [cited by applicant]
US 5741668A · Ward et al. · 1998 [cited by applicant]
US 5770429A · Lonberg et al. · 1998 [cited by applicant]
US 5777079A · Tsien et al. · 1998 [cited by applicant]
US 5789650A · Lonberg et al. · 1998 [cited by applicant]
US 5804387A · Cormack et al. · 1998 [cited by applicant]
US 5814318A · Lonberg et al. · 1998 [cited by applicant]
US 5874299A · Lonberg et al. · 1999 [cited by applicant]
US 5874304A · Zolotukhin et al. · 1999 [cited by applicant]
US 5876995A · Bryan · 1999 [cited by applicant]
US 5877397A · Lonberg et al. · 1999 [cited by applicant]
US 5925558A · Tsien et al. · 1999 [cited by applicant]
US 6114598A · Kucherlapati et al. · 2000 [cited by applicant]
US 6162963A · Kucherlapati et al. · 2000 [cited by applicant]
US 6180370B1 · Queen et al. · 2001 [cited by applicant]
US 6255458B1 · Lonberg et al. · 2001 [cited by applicant]
US 6270964B1 · Michnick et al. · 2001 [cited by applicant]
US 6300129B1 · Lonberg et al. · 2001 [cited by applicant]
US 6506724B1 · Hiles et al. · 2003 [cited by applicant]
US 6565841B1 · Niven et al. · 2003 [cited by applicant]
US 6673986B1 · Kucherlapati et al. · 2004 [cited by applicant]
US 6703359B1 · Young et al. · 2004 [cited by applicant]
US 6713610B1 · Kucherlapati et al. · 2004 [cited by applicant]
US 6753165B1 · Cox et al. · 2004 [cited by applicant]
US 6833268B1 · Green et al. · 2004 [cited by applicant]
US 6858576B1 · Young et al. · 2005 [cited by applicant]
US 6872700B1 · Young et al. · 2005 [cited by applicant]
US 6902744B1 · Emmot · 2005 [cited by applicant]
US 6956026B2 · Beeley et al. · 2005 [cited by applicant]
US 7045337B2 · Schultz et al. · 2006 [cited by applicant]
US 7049426B2 · Green et al. · 2006 [cited by applicant]
US 7064244B2 · Jakobovits et al. · 2006 [cited by applicant]
US 7081473B2 · Tsubamoto et al. · 2006 [cited by applicant]
US 7091183B1 · Wolfe et al. · 2006 [cited by applicant]
US 7157555B1 · Beeley et al. · 2007 [cited by applicant]
US 7220721B1 · Beeley et al. · 2007 [cited by applicant]
US 7223725B1 · Beeley et al. · 2007 [cited by applicant]
US 7368427B1 · Dong et al. · 2008 [cited by applicant]
US 7456254B2 · Wright et al. · 2008 [cited by applicant]
US 7521423B2 · Young et al. · 2009 [cited by applicant]
US 7572451B2 · Bachmann et al. · 2009 [cited by applicant]
US 7666838B2 · O'Harte et al. · 2010 [cited by applicant]
US 7875587B2 · Gault et al. · 2011 [cited by applicant]
US 7959924B2 · Bachmann et al. · 2011 [cited by applicant]
US 8263545B2 · Levy et al. · 2012 [cited by applicant]
US 8999940B2 · Dong · 2015 [cited by applicant]
US 10294303B2 · Yie et al. · 2019 [cited by applicant]
US 10905772B2 · Cheng et al. · 2021 [cited by applicant]
US 11046774B2 · Yie et al. · 2021 [cited by applicant]
US 20030036504A1 · Kolterman et al. · 2003 [cited by applicant]
US 20030157107A1 · Miyawaki et al. · 2003 [cited by applicant]
US 20040029805A1 · Wolfe et al. · 2004 [cited by applicant]
US 20040106547A1 · Larsen et al. · 2004 [cited by applicant]
US 20050159379A1 · McSwiggen et al. · 2005 [cited by applicant]
US 20060068910A1 · Schmidt et al. · 2006 [cited by applicant]
US 20060094652A1 · Levy et al. · 2006 [cited by applicant]
US 20060125763A1 · Akai et al. · 2006 [cited by applicant]
US 20060275288A1 · Grihalde et al. · 2006 [cited by applicant]
US 20080125371A1 · Wolfe et al. · 2008 [cited by applicant]
US 20080182795A1 · Wolfe et al. · 2008 [cited by applicant]
US 20080312098A1 · Kozian et al. · 2008 [cited by applicant]
US 20080312157A1 · Levy et al. · 2008 [cited by applicant]
US 20090036364A1 · Levy et al. · 2009 [cited by applicant]
US 20090042922A1 · Romo et al. · 2009 [cited by applicant]
US 20090074769A1 · Glaesner et al. · 2009 [cited by applicant]
US 20090186817A1 · Ghosh et al. · 2009 [cited by applicant]
US 20090209469A1 · Kim et al. · 2009 [cited by applicant]
US 20100143392A1 · Bachmann et al. · 2010 [cited by applicant]
US 20110136737A1 · Levy et al. · 2011 [cited by applicant]
US 20120101037A1 · Danho et al. · 2012 [cited by applicant]
US 20120157379A1 · Hsu · 2012 [cited by applicant]
US 20120238493A1 · DiMarchi et al. · 2012 [cited by applicant]
US 20120322725A1 · DiMarchi et al. · 2012 [cited by applicant]
US 20130344524A1 · Miyachi et al. · 2013 [cited by applicant]
US 20160194371A1 · Boscheinen et al. · 2016 [cited by applicant]
US 20160297883A1 · Gallo et al. · 2016 [cited by applicant]
US 20170114115A1 · Alsina-Fernandez et al. · 2017 [cited by applicant]
US 20170275370A1 · Yie et al. · 2017 [cited by applicant]
US 20180311372A1 · Cheng et al. · 2018 [cited by applicant]
US 20190276546A1 · Yie et al. · 2019 [cited by applicant]
US 20200384119A1 · Walker et al. · 2020 [cited by applicant]
US 20210087286A1 · Bates et al. · 2021 [cited by applicant]
US 20210154318A1 · Cheng et al. · 2021 [cited by applicant]
AU 3139984A · 1984 [cited by applicant]
CL 2018001695A1 · 2018 [cited by applicant]
CL 2019001963A1 · 2020 [cited by applicant]
CN 101044162B · 2010 [cited by applicant]
CN 109715662A · 2019 [cited by applicant]
EP 0036676A1 · 1981 [cited by applicant]
EP 0058481A1 · 1982 [cited by applicant]
EP 0088046A2 · 1983 [cited by applicant]
EP 0133988A2 · 1985 [cited by applicant]
EP 0143949A1 · 1985 [cited by applicant]
EP 0367566A1 · 1990 [cited by applicant]
EP 0367566B1 · 1990 [cited by applicant]
EP 0460846A1 · 1991 [cited by applicant]
EP 0460846B1 · 1991 [cited by applicant]
EP 0546073A4 · 1997 [cited by applicant]
EP 0546073B1 · 1997 [cited by applicant]
EP 1119625A1 · 2001 [cited by applicant]
EP 1283058A1 · 2003 [cited by applicant]
JP 2010514835A · 2010 [cited by applicant]
JP 2011511753A · 2011 [cited by applicant]
KR 20090096498A · 2009 [cited by applicant]
MX 0395677 · 2022 [cited by applicant]
PE 0012080 · 2016 [cited by applicant]
WO 8801649A1 · 1988 [cited by applicant]
WO 9004036A1 · 1990 [cited by applicant]
WO 9110741A1 · 1991 [cited by applicant]
WO 9203918A1 · 1992 [cited by applicant]
WO 9215673A1 · 1992 [cited by applicant]
WO 9222646A1 · 1992 [cited by applicant]
WO 9301227A1 · 1993 [cited by applicant]
WO 9315722A1 · 1993 [cited by applicant]
WO 9402602A1 · 1994 [cited by applicant]
WO 9420069A1 · 1994 [cited by applicant]
WO 9507463A1 · 1995 [cited by applicant]
WO 9633735A1 · 1996 [cited by applicant]
WO 9805351A1 · 1998 [cited by applicant]
WO 9814605A1 · 1998 [cited by applicant]
WO 9824464A1 · 1998 [cited by applicant]
WO 9824893A2 · 1998 [cited by applicant]
WO 9826277A2 · 1998 [cited by applicant]
WO 9907404A1 · 1999 [cited by applicant]
WO 9910494A2 · 1999 [cited by applicant]
WO 9925727A2 · 1999 [cited by applicant]
WO 9925728A1 · 1999 [cited by applicant]
WO 9940788A1 · 1999 [cited by applicant]
WO 9949019A2 · 1999 [cited by applicant]
WO 0020592A1 · 2000 [cited by applicant]
WO 2000037098A1 · 2000 [cited by applicant]
WO 0041546A2 · 2000 [cited by applicant]
WO 0041548A2 · 2000 [cited by applicant]
WO 0073331A2 · 2000 [cited by applicant]
WO 0151078A1 · 2001 [cited by applicant]
WO 01055213A2 · 2001 [cited by applicant]
WO 0187341A1 · 2001 [cited by applicant]
WO 200355914A2 · 2003 [cited by applicant]
WO 03072195A2 · 2003 [cited by applicant]
WO 03097031A1 · 2003 [cited by applicant]
WO 03099314A1 · 2003 [cited by applicant]
WO 2004083211A1 · 2004 [cited by applicant]
WO 2005000892A2 · 2005 [cited by applicant]
WO 2005021022A2 · 2005 [cited by applicant]
WO 2005102293A1 · 2005 [cited by applicant]
WO 2006045796A2 · 2006 [cited by applicant]
WO 2006068910A1 · 2006 [cited by applicant]
WO 2006086769A2 · 2006 [cited by applicant]
WO 2006086769A3 · 2006 [cited by applicant]
WO 2006125763A1 · 2006 [cited by applicant]
WO 2007028633A2 · 2007 [cited by applicant]
WO 2008021560A2 · 2008 [cited by applicant]
WO 2008021560A3 · 2008 [cited by applicant]
WO 2008081418A1 · 2008 [cited by applicant]
WO 2008101017A2 · 2008 [cited by applicant]
WO 2009042922A2 · 2009 [cited by applicant]
WO 2009068910A1 · 2009 [cited by applicant]
WO 2009042922A3 · 2009 [cited by applicant]
WO 2010012495A1 · 2010 [cited by applicant]
WO 2010016935A2 · 2010 [cited by applicant]
WO 2010016936A1 · 2010 [cited by applicant]
WO 2010016938A2 · 2010 [cited by applicant]
WO 2010016940A2 · 2010 [cited by applicant]
WO 2010016944A2 · 2010 [cited by applicant]
WO 2011014680A2 · 2011 [cited by applicant]
WO 2011094337A1 · 2011 [cited by applicant]
WO 2012055770A1 · 2012 [cited by applicant]
WO 2012088116A2 · 2012 [cited by applicant]
WO 2012167744A1 · 2012 [cited by applicant]
WO 2015022420A1 · 2015 [cited by applicant]
WO 2015086853A1 · 2015 [cited by applicant]
WO 2015095354A2 · 2015 [cited by applicant]
WO 2015185640A1 · 2015 [cited by applicant]
WO 2016209707A1 · 2016 [cited by applicant]
WO 2017074714A1 · 2017 [cited by applicant]
WO 2017112824A2 · 2017 [cited by applicant]
WO 2018136440A1 · 2018 [cited by applicant]
WO 2018237095A1 · 2018 [cited by applicant]
WO 2018237097A1 · 2018 [cited by applicant]
Almind, K. et al., “Discovery of amino acid variants in the human glucose-dependent insulinotropic polypeptide (GIP) receptor: the impact on the pancreatic beta cell responses and functional expression studies in Chines… [cited by applicant]
Al-Sabah, Suleiman, “Molecular Pharmacology of the Incretin Receptors,” Medical Principles and Practice, 25(1):15-21 (2016). [cited by applicant]
Althage, M. C. et al., “Targeted Ablation of Glucose-dependent Insulinotropic Polypeptide-producing Cells in Transgenic Mice Reduces Obesity and Insulin Resistance Induced by a High Fat Diet,” The Journal of Biological … [cited by applicant]
American Diabetes Association, Standards of Medical Care in Diabetes—2010, American Diabetes Association, Diabetes Care, 33(1):S11-S61 (2010). [cited by applicant]
Asmar, M. et al., “Glucose-Dependent Insulinotropic Polypeptide May Enhance Fatty Acid Re-esterification in Subcutaneous Abdominal Adipose Tissue in Lean Humans,” Diabetes, 59:2160-2163 (2010). [cited by applicant]
Ausubel, F. M. et al., eds., “Hybridization with Radioactive Probes, Using DNA Fragments as Probes,” Current Protocols in Molecular Biology, John Wiley & Sons, Inc., NY, Section II, Supplements Unit 6.3, pp. 6.3.1-6.3.6… [cited by applicant]
Ausubel, F. M. et al., eds., Brown, Terry, Contributor, “Hybridization Analysis of DNA Blots” Current Protocols in Molecular Biology, John Wiley and Sons, Inc., Chapter 2, Section IV, Supplements 21, 35, 29, 26, and 42,… [cited by applicant]
Ausubel, F. M. et al., eds., Duby, Allan, Jacobs, Kenneth A., Celeste, Anthony, Contributors, “Hybridization With Radioactive Probes, Using Synthetic Oligonucleotides as Probes,” Current Protocols in Molecular Biology, … [cited by applicant]
Ausubel, F. M. et al., eds., Short Protocols in Molecular Biology, 2nd Edition, A Compendium of Methods from Current Protocols In Molecular Biology, Greene Publishing Associates and John Wiley and Sons, New York Chiches… [cited by applicant]
Ausubel, F. M. et al., eds., Strauss, William M., Contributor, “Hybridization With Radioactive Probes, Using DNA Fragments as Probes,” Current Protocols in Molecular Biology, John Wiley and Sons, Inc., Chapter 6, Sectio… [cited by applicant]
Baggio, L. L. et al., “Chronic exposure to G1P-1R agonists promotes homologous GLP-1 receptor desensitization in vitro but does not attenuate GLP-1R-dependent glucose homeostasis in vivo,” Diabetes, 53(3):S205-S214 (200… [cited by applicant]
Beck, B. et al., “Direct metabolic effects of gastric inhibitory polypeptide (GIP): dissociation at physiological levels of effects on insulin-stimulated fatty acid and glucose incorporation in rat adipose tissue,” Diab… [cited by applicant]
Beck, B. et al., “Hypersensitivity of Adipose Tissue to Gastric Inhibitory Polypeptide Action in the Obese Zucker Rat,” Cellular and Molecular Biology, 33(5):555-562 (1987). [cited by applicant]
Behrens, C. R. et al., “Methods for Site-Specific Drug Conjugation to Antibodies,” mAbs, 6(1):46-53 (2014) (Downloaded by EPO Aug. 3, 2016). [cited by applicant]
Berndt, S. I. et al., “Genome-wide meta-analysis identifies 11 new loci for anthropometric traits and provides insights into genetic architecture,” Nature Genetics, 45(5):501-512 (2013). [cited by applicant]
Bhatnagar, P. K. et al., “Structure—Activity Relationships of Novel Hematoregulatory Peptides,” J. Med. Chem., 39:3814-3819 (1996). [cited by applicant]
Bianchi, A. A. and McGrew, J. T., “High-Level Expression of Full-Length Antibodies Using Trans-Complementing Expression Vectors,” Biotech Biotechnol. Bioeng., 84:439-444 (2003). [cited by applicant]
Bong, et al., “Chemoselective Pd(0)-catelyzed peptide coupling in water,” Organic Letters, 3(16):2509-2511 (2001). [cited by applicant]
Bootcov, M. R. et al., “MIC-1, a novel macrophage inhibitory cytokind, is a divergent member of the TGF-β superfamily,” Proc. Natl. Acad. Sci. USA, 94:11514-11519 (1997). [cited by applicant]
Bowie, J. U. et al., “A Method to Identify Protein Sequences That Fold into a Known Three-Dimensional Structure,” Science, 253:164-170 (1991). [cited by applicant]
Boylan, M. O. et al., “Gastric inhibitory polypeptide immunoneutralization attenuates development of obesity in mice,” Am J Physiol Endocrinol Metab, 309 :E1008-E1018 (2015). [cited by applicant]
Branden, C. and Tooze, J., eds., Introduction to Protein Structure, Garland Publishing, Inc. New York and London (1991) (Table of Contents Only). [cited by applicant]
Brenner, S. E. et al., “Population statistics of protein structures: lessons from structural classifications,” Curr. Op. Struct. Biol., 7:369-376 (1997). [cited by applicant]
Brons, C. et al., “Impact of short-term high-fat feeding on glucose and insulin metabolism in young healthy men,” The Journal of Physiology, 587:2387-2397 (2009). [cited by applicant]
Bruggermann, M. et al., “Design Mice: The Production of Human Antibody Repertoires in Transgenic Animals,” Year in Immunol., 7:33-40 (1993). [cited by applicant]
Campbell, J. E. et al., “TCF1 links GIPR signaling to the control of beta cell function and survival,” Nature Medicine, 22(1):84-90 (2016). [cited by applicant]
Carrillo, H. et al., “The Multiple Sequence Alignment Problem in Biology,” Siam J. Applied Math, Society for Industrial and Applied Mathematics, 48(5):1073-1082 (1988). [cited by applicant]
Chalfie, M. et al., “Green Fluorescent Protein as a Marker for Gene Expression,” Science, 263:802-805 (1994). [cited by applicant]
Chamow, S. M. and Ashkenazi, A., “Immunoadhesins: principles and applications,” Tibtech 14: 52-60 (1996). [cited by applicant]
Chen, J. et al., “Immunoglobulin gene rearrangement in B cell deficient mice generated by targeted deletion of the JH locus, ” International Immunology, 5(6):647-656 (1993). [cited by applicant]
Cheung, R. C. et al., “Epitope-Specific Antibody Response to the Surface Antigen of Duck Hepatitis B Virus in Infected Ducks,” Virology, 176:546-552 (1990). [cited by applicant]
Chia, C. W. et al., “Exogenous Glucose-Dependent Insulinotropic Polypeptide Worsens Postprandial Hyperglycemia in Type 2 Diabetes,” Diabetes, 58:1342-1349 (2009). [cited by applicant]
Chothia & Lesk, “Canonical Structures for the Hypervariable Regions of Immunoglobulins,” J. Mol. Biol., 196:901-917 (1987). [cited by applicant]
Chothia, C. et al., “Conformations of immunoglobulin hypervariable regions,” Nature, 342:877-883 (1989). [cited by applicant]
Chou, P. Y. et al., “Conformational Parameters for Amino Acids in Helical, β-Sheet, and Random Coil Regions Calculated from Proteins,” Biochemistry, 13(2):211-222 (1974). [cited by applicant]
Chou, P. Y. et al., “Empirical Predictions of Protein Conformation,” Ann. Rev. Biochem., 47:251-276 (1978). [cited by applicant]
Chou, P. Y. et al., “Prediction of Protein Conformation,” Biochem., 13(2):222-245 (1974). [cited by applicant]
Chou, P. Y. et al., “Prediction of the Secondary Structure of Proteins From Their Amino Acid Sequence,” Adv. Enzymol. Relat. Areas Mol. Biol., 47:45-148 (1978). [cited by applicant]
Chou, P. Y. et al., “Prediction of β-Turns,” Biophys. J., 26:367-384 (1979). [cited by applicant]
Cinti, S. et al., “Adipocyte death defines macrophage localization and function in adipose tissue of obese mice and humans,” Journal of Lipid Research, 46:2347-2355 (2005). [cited by applicant]
Coligan, J. E., ed., Current Protocols in Immunology, New York: John Wiley & Sons, Inc. (1993) (Table of Contents Only). [cited by applicant]
Cosman, D. et al., “Cloning, sequence and expression of human interleukin-2 receptor,” Nature, 312:768-771 (1984). [cited by applicant]
Creighton, T. E., Ed., Proteins: Structures and Molecular Principles, 2nd ed., W. H. Freeman and Company, New York (1984) (Table of Contents Only). [cited by applicant]
Creighton, T. E., Ed., Proteins: Structures and Molecular Principles, W. H. Freeman and Company, San Francisco, CA, Section About: Hydroxylation of Pro and Lys, pp. 70-86 (1983). [cited by applicant]
Dayhoff, M. O. et al., Atlas of Protein Sequence and Structure, Chapter 22, A Model of Evolutionary Change in Proteins, 5(3):345-352 (1978). [cited by applicant]
Devasher, R. B. et al., “Aqueous-phase, palladium-catelyzed cros-coupling of aryl bromides under mid conditions, using water-soluble, sterically demanding alkylphosphines,” J. Org. Chem., 69:7919-7927 (2004). [cited by applicant]
Devereux, J. et al., “A comprehensive set of sequence analysis programs for the VAX.” Nucl. Acid Res., Laboratory of Genetics, University of Wisconsin, Madison, WI, 12(1):387-395 (1984). [cited by applicant]
Dibowski, H. et al., Bioconjugation of peptides by palladium-catalyzed C-C cross-coupling in water, Angew. Chem. Int. Ed., 37(4):476-478 (1998). [cited by applicant]
Dillon, J. S. et al., “Cloning and functional expression of the human glucagon-like peptide-1 (GLP-1) receptor,” Endocrinology, 133(4):1907-1910 (1993). [cited by applicant]
Drucker, D. J., “Enhancing incretin action for the treatment of type 2 diabetes,” Diabetes Care, 26(10):2929-2940 (2003). [cited by applicant]
Eng et al., “Purification and Structure of Exendin-3, a New Pancreatic Secretagogue Isolated from Heloderma horridum Venom,” The Journal of Biological Chemistry, 265(33):20259-202262 (1990). [cited by applicant]
Eppstein, D. A. et al., “Biological activity of liposomes-encapsulated murine interferon γ is mediated by a cell membrane receptor,” Proc. Natl. Acad. Sci. USA 82:3688-3692 (1985). [cited by applicant]
Evans, B. E. et al., “Design of Nonpeptidal Ligands for a Peptide Receptor: Cholecystokinin Antagonists,” J. Med. Chem., 30:1229-1239 (1987). [cited by applicant]
Fairlie, W. D., “Expression of a TGF-β superfamily protein, macrophage inhibitory cytokine-1, in the yeast Pichia pastoris,” Gene, 254:67-76 (2000). [cited by applicant]
Falko, J. M. et al., “Gastric Inhibitory Polypeptide (GIP) Stimulated by Fat Ingestion in Man,” JCE&M, 41(2):260-265 (1975). [cited by applicant]
Fauchere, J-L., “Elements for the Rational Design of Peptide Drugs,” Adv. Drug Res., 15:29-69 (1986). [cited by applicant]
Fehmann, H. et al. “Cell and Molecular Biology of the Incretin Hormones Glucagon-Like Peptide-I and Glucose-Dependent Insulin Releasing Polypeptide,” Endocrine Reviews, 16(3):390-410 (1995). [cited by applicant]
Finan, B. et al., “Emerging Opportunities for the Treatment of Metabolic Diseases: Glucagon-Like Peptide-1 Based Multi-Agonists,” Molecular and Cellular Endocrinology, 418: 42-54 (2015). [cited by applicant]
Finan, B. et al., “Unimolecular Dual Incretins Maximize Metabolic Benefits in Rodents, Monkeys, and Humans,” Science-Translational Medicine, 5(209):209ra151 (2013). [cited by applicant]
Fishwild, D. M. et al., “High-avidity human IgGk monoclonal antibodies from a novel strain of minilocus transgenic mice,” Nature Biotechnology, 14:845-851 (1996). [cited by applicant]
Fulurija, A. et al., “Vaccination against GIP for the Treatment of Obesity,” PloS One, 3(9):e3163 (2008). [cited by applicant]
Gault, V. A. et al., “Characterization of the Cellular and Metabolic Effects of a Novel Enzyme-Resistant Antagonist of Glucose-Dependent Insulinotropic Polypeptide,” Biochemical and Biophysical Research Communications, … [cited by applicant]
Genbank Accession No. U55762, “Cloning vector pEGFP-N1, complete sequence, enhanced green fluorescent protein (egfp) and neomycin phosphotransferase genes, complete cds,” CLONTECH Labs, Inc., Kitts, P. A., (2003). [cited by applicant]
Gennaro, A. R., Remington's Pharmaceutical Sciences, 18th Edition, Mack Publishing Co., Easton, PA (1990) (Table of Contents Only). [cited by applicant]
Gerhard, D. S. et al., “The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC),” Genome Research, 14:2121-2127 (2004). [cited by applicant]
Getty-Kaushik, L. et al., “Glucose-Dependent Insulinotropic Polypeptide Modulates Adipocyte Lipolysis and Reesterification,” Obesity, 14(7):1124-1131 (2006). [cited by applicant]
Goding, Production of Monoclonal Antibodies, Monoclonal antibodies: principles and practice: production and application of monoclonal antibodies in cell biology, biochemistry, and immunology, pp. 59-103 (1986). [cited by applicant]
Goeddel, D. V., ed., Methods Enzymol., Gene Expression Technology, vol. 185, New York: Academic Press (1990) (Table of Contents Only). [cited by applicant]
Green, L. L. and Jakobovits, Aya, “Regulation of B Cell Development by Variable Gene Complexity in Mice Reconstituted with Human Immunoglobulin Yeast Artificial Chromosomes,” J. Exp. Med., 188(3):483-495 (1998). [cited by applicant]
Green, L. L., et al., “Antigen-specific human monoclonal antibodies from mice engineered with human Ig heavy and light chain YACs,” Nature Genetics, 7:13-21 (1994). [cited by applicant]
Gremlich, S. et al., “Cloning, Functional Expression, and Chromosomal Localization of the Human Pancreatic Islet Glucose-Dependent Insulinotropic Polypeptide Receptor,” Diabetes, 44:1202-1208, (1995). [cited by applicant]
Gribskov, M. and Devereux, J., eds., Sequence Analysis Primer, New York: M. Stockton Press, (1991) (Table of Contents Only). [cited by applicant]
Gribskov, M. et al., “Profile Analysis, Searching Databases,” Meth. Enzym., Chapter 9, 183:146-159 (1990). [cited by applicant]
Gribskov, M. et al., “Profile analysis: Detection of distantly related proteins,” Proc. Nat. Acad. Sci. USA, 84:4355-4358 (1987). [cited by applicant]
Griffin, A. M. and Griffin, H. G., eds., Computer Analysis of Sequence Data, Part I, Humana Press, Totowa, New Jersey (1994) (Table of Contents Only). [cited by applicant]
Gupta, D. et al., “Physiologic and Pharmacologic Modulation of Glucose-Dependent Insulinotropic Polypeptide (GIP) Receptor Expression in β-Cells by Peroxisome Proliferator- Activated Receptor (PPAR)-γ Signaling: Possibl… [cited by applicant]
Harding, F. A. and Lonberg, N., “Class Switching in Human Immunoglobulin Transgenic Mice,” Ann. NY Acad. Sci., 765:536-546 (1995). [cited by applicant]
Hargrove, D. M. et al., “Biological activity of AC3174, a peptide analog of exendin-4,” Regulatory Peptides, 141:113-119 (2007). [cited by applicant]
Harlow, E. and Lane, D., Antibodies: A Laboratory Manual, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY (1988). [cited by applicant]
Harlow, E. and Lane, D., Antibodies: A Laboratory Manual, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY (1988) (Ed. 1991 and Periodic Supplements) (Table of Contents Only). [cited by applicant]
Haugland, R. P., Molecular Probes Handbook, A Guide to Fluorescent Probes and Labeling Technologies, 11th Ed. Invitrogen by ThermoFisher Scientific (2010) (Table of Contents Only). [cited by applicant]
Hauner, H. et al., “Effects of Gastric Inhibitory Polypeptide on Glucose and Lipid Metabolism of Isolated Rat Adipocytes,” Ann. Nutr. Metab., 32:282-288 (1988). [cited by applicant]
Heim, R. et al., “Engineering green fluorescent protein for improved brightness, longer wavelengths and fluorescence resonance energy transfer,” Current Biology, 6:178-182 (1996). [cited by applicant]
Henikoff, S. et al., “Amino acid substitution matrices from protein blocks,” Proc. Natl. Acad. Sci. USA, 89:10915-10919 (1992). [cited by applicant]
Hinke, S. A. et al., Identification of a bioactive domain in the amino-terminus of glucose-dependent insulinotropic polypeptide (GIP), Biochimica et Biophysica Acta, 1547(1):143-155 (2001). [cited by applicant]
Højberg, P. V. et al., “Four weeks of near-normalisation or blood glucose improves the insulin response to glucagon-like peptide-1 and glucose-dependent insulinotropic polypeptide in patients with type 2 diabetes,” Diab… [cited by applicant]
Holm, L. et al., “Protein folds and families: sequence and structure alignments,” Nucleic Acid Research, 27(1):244-247 (1999). [cited by applicant]
Hoogenboom et al., “By-passing Immunisation Human Antibodies from Synthetic Repertoires of Germline VH Gene Segments Rearranged in Vitro,” J. Mol. Biol., 227:381-388 (1991). [cited by applicant]
Hopp, T. P. et al., “A Short Polypeptide Marker Sequence Useful for Recombinant Protein Identification and Purification,” Bio/Technology, 6:1204-1210 (1988). [cited by applicant]
Ichiki, T. et al., “Regulation of the expression of human C epsilon germline transcript. Identification of a novel IL-4 responsive element,” The Journal of Immunology, 150:5408-5417 (1993). [cited by applicant]
Inagaki, N. et al., “Gastric Inhibitory Polypeptide: Structure and Chromosomal Localization of the Human Gene,” Molecular Endocrinology 3(6):1014-1021 (1989). [cited by applicant]
Jakobovits, A. et al., “Analysis of homozygous mutant chimeric mice: deletion of the immunoglobulin heavy-chain joining region blocks B-cell development and antibody production,” Proc. Natl. Acad. Sci. USA, 90:2551-2555… [cited by applicant]
Jakobovits, A. et al., “Germ-line transmission and expression of a human-derived yeast artificial chromosome,” Nature, 362:255-258 (1993). [cited by applicant]
Jalkanen, M. et al., “Cell Surface Proteoglycan of Mouse Mammary Epithelial Cells is Shed by Cleavage of Its Matrix-binding Ectodomain from Its Membrane-associated Domain,” The Journal of Cell Biology, 105(6)(2):3087-30… [cited by applicant]
Jalkanen, M. et al., “Heparan Sulfate Proteoglycans from Mouse Mammary Epithelial Cells: Localization on the Cell Surface with a Monoclonal Antibody,” The Journal of Cell Biology, 101:976-984 (1985). [cited by applicant]
Jones, D. T. et al., “Progress in protein structure prediction,” Current Opinion in Structural Biology, 7:377-387 (1997). [cited by applicant]
Jones, P. T. et al., “Replacing the complementarity-determining regions in a human antibody with those from a mouse,” Nature, 321:522-525 (1986). [cited by applicant]
Joo, E. et al., “Inhibition of Gastric Inhibitory Polypeptide Receptor Signaling in Adipose Tissue Reduces Insulin Resistance and Hepatic Steatosis in High-Fat Diet-Fed Mice,” Diabetes, 66:868-879 (2017). [cited by applicant]
Kabat, E. A. et al., Sequences of Proteins of Immunological Interest, 5th ed., U.S. Dept. of Health and Human Services, PHS, NIH, Bethesda, MD (1987 and 1991) (Table of Contents Only). [cited by applicant]
Kabat, E. A. et al., Sequences of Proteins of Immunological Interest, 5th ed., U.S. Dept. of Health and Human Services, PHS, NIH, NIH Publication No. 91-3242, Bethesda, MD (1991) (Table of Contents Only). [cited by applicant]
Kellerman, S. and Green, L. L., “Antibody discovery: the use of transgenic mice to generate human monoclonal antibodies for therapeutics,” Current Opinion in Biotechnology, 13:593-597 (2002). [cited by applicant]
Kennett, R. H. et al., eds., Monoclonal Antibodies, Hybridomas: A New Dimension in Biological Analyses, Plenum Press, New York (1980) (Table of Contents Only). [cited by applicant]
Kilpatrick, K. E. et al., “Rapid development of affinity matured monoclonal antibodies using RIMMS,” Hybridoma, 16(4):381-389 (1997). [cited by applicant]
Kim, S. J. et al., “Activation of Lipoprotein Lipase by Glucose-dependent Insulinotropic Polypeptide in Adipocytes: A Role for a Protein Kinase B, LKB1, and AMP-Activated Protein Kinase Cascade,” The Journal of Biologic… [cited by applicant]
Kim, S. J. et al., “GIP-Overexpressing Mice Demonstrate Reduced Diet-Induced Obesity and Steatosis, and Improved Glucose Homeostasis,” PloS One, 7(7):e40156 (2012). [cited by applicant]
Kirkland,T. N. et al., “Analysis of the Fine Specificity and Cross-Reactivity of Monoclonal Anti-Lipid A Antibodies,” The Journal of Immunology, 137(11):3614-3619 (1986). [cited by applicant]
Knapper, J. M. et al., “Investigations into the Actions of Glucose-Dependent Insulinotropic Polypeptide and Glucagon-Like Peptide-1(7-36)amide on Lipoprotein Lipase Activity in Explants of Rat Adipose Tissue,” The Journ… [cited by applicant]
Kostelny, S. A. et al., “Formation of a Bispecific Antibody by the Use of Leucine Zippers,” The Journal of Immunology, 148(5):1547-1553 (1992). [cited by applicant]
Kyte, J. et al., “A Simple Method for Displaying the Hydropathic Character of a Protein,” J. Mol. Biol., 157:105-132 (1982). [cited by applicant]
Langer, R. et al., “Biocompatibility of polymeric delivery systems for macromolecules,” Journal of Biomedical Materials. Research, 15:267-277 (1981). [cited by applicant]
Langer, R. et al., “Controlled release of macromolecules,” Chem. Tech., 12:98-105 (1982). [cited by applicant]
Lesk, A. M., ed., Computational Molecular Biology, Sources and Methods for Sequence Analysis, New York: Oxford University Press, Oxford New York Tokyo (1988) (Table of Contents Only). [cited by applicant]
Lewis, J. T. et al. “Glucose-dependent insulinotropic polypeptide confers early phase insulin release to oral glucose in rats: demonstration by a receptor antagonist”, Endocrinology, 141(10): 3710-3716 (2000). [cited by applicant]
Link, A. J. et al., “Non-canonical amino acids in protein engineering,” Current Opinion in Biotechnology, 14(6):603-609 (2003). [cited by applicant]
Lonberg, N. and Huszar, D., “Human Antibodies from Transgenic Mice,” Intern. Rev. Immunol., 13:65-93 (1995). [cited by applicant]
Lonberg, N. et al., “Antigen-specific human antibodies from mice comprising four distinct genetic modifications,” Nature, 368:856-859 (1994). [cited by applicant]
Lonberg, N. et al., The Pharmacology of Monoclonal Antibodies—Chapter 3: “Transgenic Approaches to Human Monoclonal Antibodies,” Handbook of Exp. Pharmacology, 113:49-101 (1994). [cited by applicant]
Lorenz, M. et al., “Recent progress and future options in the development of GLP-1 receptor agonists for the treatment of diabesity,” Bioorg Med Chem Lett, 23(14):4011-4018 (2013). [cited by applicant]
Lund, A. et al., “The separate and combined impact of the intestinal hormones, GIP, GLP-1, and GLP-2, on glucagon secretion in type 2 diabetes,” Am J Physiol Endocrinol Metab, 300:E1038-E1046 (2011). [cited by applicant]
Manandhar, B. and Ahn, J., “Glucagon-like Peptide 1 (GLP-1) Analogs: Recent Advances, New Possibilities, and Therapeutic Implications,” J. Med. Chem., 58(3):1020-1037 (2015). [cited by applicant]
Maniatis et al., “Regulation of Inducible and Tissue-Specific Gene Expression,” Science, 236:1237-1244 (1987). [cited by applicant]
Marks, J. D. et al., “By-passing Immunization: Human Antibodies and V-gene Libraries Displayed on Phage,” J. Mol. Biol., 222:581-597 (1991). [cited by applicant]
Mcclean, P. L. et al., “GIP receptor antagonism reverses obesity, insulin resistance, and associated metabolic disturbances induced in mice by prolonged consumption of high-fat diet,” American Journal of Physiology: End… [cited by applicant]
Meier, J. J. et al., “Gastric inhibitory polypeptide (GIP) dose-dependently stimulates glucagon secretion in healthy human subjects at euglycaemia,” Diabetologia, 46:798-801 (2003). [cited by applicant]
Mendez et al., “Functional transplant of megabase human immunoglobulin loci recapitulates human antibody response in mice,” Nature Genetics, 15:146-156 (1997). [cited by applicant]
Miyawaki, K. et al., “Inhibition of gastric inhibitory polypeptide signaling prevents obesity,” Nature Medicine, 8(7):738-742 (2002). [cited by applicant]
Mohammad, S. et al., “A Naturally Occurring GIP Receptor Variant Undergoes Enhanced Agonist-Induced Desensitization, Which Impairs GIP Control of Adipose Insulin Sensitivity,” Molecular and Cellular Biology, 34(19):3618… [cited by applicant]
Moldenhauer, G. et al., “Identity of HML-1 Antigen on Intestinal Intraepithelial T Cells and of B-ly7 Antigen on Hairy Cell Leukaemia,” Scand. J. Immunol., 32:77-82 (1990). [cited by applicant]
Montgomery, I. A. et al., “Active immunization against (Pro(3))GIP improves metabolic status in high-fat-fed mice,” Diabetes, Obesity & Metabolism, pp. 744-751 (2010). [cited by applicant]
Morel et al., “Monoclonal Antibodies to Bovine Serum Albumin: Affinity and Specificity Determinations,” Molecular Immunology, 25(1):7-15 (1988). [cited by applicant]
Morrison, S. L. et al., “Chimeric human antibody molecules: Mouse antigen-binding domains with human constant region domains,” Proc. Natl. Acad. Sci. USA, 81:6851-6855 (1984). [cited by applicant]
Moult, J. et al., “The current state of the art in protein structure prediction,” Current Opinion in Biotechnology, 7:422-427 (1996). [cited by applicant]
Murphy, M. C. et al., “Postprandial lipid and hormone responses to meals of varying fat contents: modulatory role of lipoprotein lipase?,” European Journal of Clinical Nutrition, 49:579-588 (1995). [cited by applicant]
Nasteska, D. et al., “Chronic Reduction of GIP Secretion Alleviates Obesity and Insulin Resistance Under High-Fat Diet Conditions,” Diabetes, 63:2332-2343 (2014). [cited by applicant]
Nauck, M. A. et al., “Preserved Incretin Activity of Glucagon-like Peptide 1 [7-36 Amide] but Not of Synthetic Human Gastric Inhibitory Polypeptide in Patients with Type-2 Diabetes Mellitus,” J. Clinic. Invest., 91:301-… [cited by applicant]
NCBI Reference Sequence: AAI20674, https://www.ncbi.nlm.nih.gov/sviewer/viewer.fcgi?db=nuccore&val=AAI20674&report=genbank, (downloaded Nov. 28, 2017). [cited by applicant]
NCBI Reference Sequence: NM_000164, https://www.ncbi.nlm.nih.gov/sviewer/viewer.fcgi?noredirect=1&db=nuccore&val=NM_000164.1, (downloaded Nov. 28, 2017). [cited by applicant]
NCBI Reference Sequence: NM_001080815, https://www.ncbi.nlm.nih.gov/sviewer/viewer.fcgi?db=protein&val=NM_001080815&report=genbank, (downloaded Nov. 28, 2017). [cited by applicant]
NCBI Reference Sequence: NP_000155, https://www.ncbi.nlm.nih.gov/protein/NP_000155.1 (downloaded Aug. 16, 2018). [cited by applicant]
NCBI Reference Sequence: NP_001074284, https://www.ncbi.nlm.nih.gov/sviewer/viewer.fcgi?db=protein&val=NP_001074284+&report=genbank, (downloaded Nov. 28, 2017). [cited by applicant]
NCBI Reference Sequence: XP_005258790, https://www.ncbi.nlm.nih.gov/sviewer/viewer.fcgi?db=nuccore&val=XP_005258790&report=genbank, (downloaded Nov. 28, 2017). [cited by applicant]
Needleman, S. B. et al., Algorithm, “A General Method Applicable to the Search for Similarities in the Amino Acid Sequence of Two Proteins,” J. Mol. Biol., 48:443-453 (1970). [cited by applicant]
Nielsen, L. L. et al., “Pharmacology of exenatide (synthetic exendin-4) for the treatment of type 2 diabetes,” Current Opinion in Investigational Drugs, 4(4):401-405 (2003). [cited by applicant]
Nolan, G. P. et al., “Flourescence-activated cell analysis and sorting of viable mammalian cells based on beta-D-galactosidase activity after transduction of [cited by applicant]
Okada, Y. et al., “Common variants at CDKALI and KLF9 are associated with body mass index in east Asian populations,” Nature Genetics, 44(3):302-306 (2012). [cited by applicant]
Paul, W. E. et al., Fundamental Immunology, 2nd ed., Chapter 7: Evolution of the Immune System, pp. 139-165, Raven Press, New York (1989). [cited by applicant]
Prasad-Reddy, L. et al., “A clinical review of GLP-1 receptor agonists: efficacy and safety in diabetes and beyond, ” Drugs in Context, 4:212283 (2015). [cited by applicant]
Prescher, J. A., and Bertozzi, C. R., Chemistry in living systems, Nature Chemical Biology, 1(1):13-21 (2005). [cited by applicant]
Raufman, J. P. et al., “Truncated Glucagon-like Peptide-1 Interacts with Exendin Receptors on Dispersed Acini from Guinea Pig Pancreas,” The Journal of Biological Chemistry, 265(30):21432-21437 (1992). [cited by applicant]
Ravn, P. et al., “Structural and Pharmacological Characterization of Novel Potent and Selective Monoclonal Antibody Antagonists of Glucose-dependent Insulinotropic Polypeptide Receptor,” The Journal of Biological Chemis… [cited by applicant]
Riechmann, L.et al., “Reshaping human antibodies for therapy,” Nature, 332(24):323-327 (1988). [cited by applicant]
Rizo, J. and Gierasch, L. M., “Constrained Peptides: Models of Bioactive Peptides and Protein Substructures,” Annual Rev. Biochem., 61:387-418 (1992). [cited by applicant]
Rudikoff, S. et al., “Single amino acid substitution altering antigen-binding specificity,” Proc. Natl. Acad. Sci., 79:1979-1983 (1982). [cited by applicant]
Sambrook, J. et al., Molecular Cloning: A Laboratory Manual, 2nd ed., Cold Spring Harbor Laboratory Press (1989) (Table of Contents Only). [cited by applicant]
Sambrook, J. et al., Molecular Cloning: A Laboratory Manual, 3rd ed., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY (2001) (Table of Contents Only). [cited by applicant]
Saxena, R. et al., “Genetic variation in GIPR influences the glucose and insulin responses to an oral glucose challenge,” Nature Genetics, 42(2):142-148 (2010). [cited by applicant]
Schumacher, D. et al., “Current Status: Site-Specific Antibody Drug Conjugates,” Journal of Clinical Immunology, 36(1):100-107 (2016). [cited by applicant]
Shinmi, D. et al., “One-Step Conjugation Method for Site-Specific Antibody-Drug Conjugates through Reactive Cysteine-Engineered Antibodies,” Bioconjugate Chem, 27(5):1324-1331 (2016). [cited by applicant]
Sidman, K. R. et al., “Controlled Release of Macromolecules and Pharmaceuticals from Synthetic Polypeptides Based on Glutamic Acid,” Biopolymers, 22:547-556 (1983). [cited by applicant]
Sippl, Manfred J. et al., “Threading thrills and threats,” Structure, 4:15-19 (1996). [cited by applicant]
Smith, D. W., ed., Biocomputing Informatics and Genome Projects, New York: Academic Press (1994) (Table of Contents Only). [cited by applicant]
Songsivilai, S. and Lachmann, P. J., “Bispecific antibody: a tool for diagnosis and treatment of disease,” Clin. Exp. Immunol., 79:315-321 (1990). [cited by applicant]
Speliotes, E. K. et al., “Association analyses of 249,796 individuals reveal 18 new loci associated with body mass index,” Nature Genetics, 42(11):937-948 (2010). [cited by applicant]
Stahli, C. et al., “Distinction of Epitopes by Monoclonal Antibodies,” Methods in Enzymology, 92:242-253 (1983). [cited by applicant]
Stauber, R. H., “Developments and Applications of Enhanced Green Fluorescent Protein Mutants,” BioTechniques, 24(3):462-471 (1998). [cited by applicant]
Strissel, K. J. et al., “Adipocyte Death, Adipose Tissue Remodeling, and Obesity Complications,” Diabetes, 56:2910-2918 (2007). [cited by applicant]
Suzuki, K. et al., “Transcriptional Regulatory Factor X6 (Rfx6) Increases Gastric Inhibitory Polypeptide (GIP) Expression in Enteroendocrine K-cells and Is Involved in GIP Hypersection in High Fat Diet-induced Obesity,”… [cited by applicant]
Taylor, L. D. et al., “A Transgenic mouse that expresses a diversity of human sequence heavy and light chain immunoglobulins,” Nucleic Acids Research, 20(23):6287-6295 (1992). [cited by applicant]
Taylor, L. D. et al., “Human immunoglobulin transgenes undergo rearrangement, somatic mutation and class switching in mice that lack endogenous IgM,” International Immunology, 6(4):579-591 (1994). [cited by applicant]
Third Report of the National Cholesterol Education Program (NCEP) Expert Panel on Detection, Evaluation, and Treatment of the High Blood Cholesterol in Adults (adult Treatment Panel III) Final Report, National Institute… [cited by applicant]
Thornton, J. M. et al., “Prediction of progress at last,” Nature, 354:105-106 (1991). [cited by applicant]
Tijssen, Practice and Theory of Enzyme Immunoassays, R. H. Burdon and P. H. van Knippenberg, Eds, Elsevier, Amsterdam, vol. 15 (1993) (Table of Contents Only). [cited by applicant]
Trumper, A. et al., “Glucose-Dependent Insulinotropic Polypeptide Is a Growth Factor for β (INS-1) Cells by Pleiotropic Signaling,” Molecular Endocrinology, 15(9):1559-1570 (2001). [cited by applicant]
Tseng, C. C. et al., “Regulation of glucose-dependent insulinotropic peptide gene expression by a glucose meal,” Am J Physiol, 266(5)(1):G887-891 (1994). [cited by applicant]
Tsubamoto, Y. et al., “A novel low-molecular-weight antagonist of glucose-dependent insulinotropic polypeptide receptor SKL-14959, prevents obesity and insulin resistance,” Diabetologia, 51:S373 (2008). [cited by applicant]
Tuaillon et al., “Biased utilization of DHQ52 and JH4 gene segments in a human Ig transgenic minilocus is independent of antigenic selection,” The Journal of Immunology, 152:2912-2920 (1994). [cited by applicant]
UniProtKB Sequence Identifier: P48546-2, http://www.uniprot.org/uniprot/P48546-2.fasta, downloaded Nov. 30, 2017. [cited by applicant]
UniprotKB/Swiss-Prot Q0P543-1, http://www.uniprot.org/uniprot/Q0P543.fasta, downloaded Dec. 4, 2017. [cited by applicant]
Usdin, T. B. et al., “Gastric Inhibitory Polypeptide Receptor, a Member or the Secretin-Vasoactive Intestinal Peptide Receptor Family, Is Widely Distributed in Peripheral Organs and the Brain,” Endocrinology, 133(6):286… [cited by applicant]
Van Heeke, G. & Schuster, S. M., “Expression of Human Asparagine Synthetase in [cited by applicant]
Vassilatis et al., “The G Protein-coupled receptor repertoires of human and mouse,” PNAS USA, 100(8):4903-4908 (2003). [cited by applicant]
Veber, D. F. and Freidinger, R. M., “The design of metabolically-stable peptide analogs,” TINS, p. 392-396 (1985). [cited by applicant]
Verhoeyen, M. et al., “Reshaping Human Antibodies: Grafting an Antilysozyme Activity,” Science, 239:1534-1536 (1988). [cited by applicant]
Vilsboll, T. et al., “Incretin Secretion in Relation to Meal Size and Body Weight in Healthy Subjects and People with Type 1 and Type 2 Diabetes Mellitus,” The Journal of Clinical Endocrinology & Metabolism, 88(6):2706-… [cited by applicant]
Volz, A. et al., “Molecular cloning, functional expression, and signal transduction of the GIP-receptor cloned from a human insulinoma,” FEBS Letters, 373:23-29 (1995). [cited by applicant]
Von Heinje, G., Sequence Analysis in Molecular Biology, Academic Press, Inc., New York (1987) (Table of Contents Only). [cited by applicant]
Voss, S. D. et al., “The role of enhancers in the regulation of cell-type-specific transcriptional control,” TIBS, 11:287 (1986). [cited by applicant]
Wang, Y. et al., “Multifunctional Antibody Agonists Targeting Glucagon-like Peptide-1, Glucagon, and Glucose-Dependent Insulinotropic Polypeptide Receptors,” Angewandte Chemie International Edition, 55(40): 12475-12478 … [cited by applicant]
Wang, Y. J. and Hanson, M. A. et al., “Parenteral Formulations of Proteins and Peptides: Stability and Stabilizers,” Journal of Parenteral Science and Technology, Technical Report No. 10, 42(2S): S4-S26 (1988). [cited by applicant]
Wen, W. et al., “Meta-analysis identifies common variants associated with body mass index in east Asians,” Nature Genetics, 44(3):307-311 (2012). [cited by applicant]
Western, E. C. (Including Shaugnessy, K. H. as shown in specification) et al., “Efficient One-Step Suzuki Arylation of Unprotected Halonucleosides, Using Water-Soluble Palladium Catalysts,” J. Org. Chem., 68:6767-6774 (… [cited by applicant]
Yamada, Y. et al., “Pancreatic and Extrapancreatic Effects of Gastric Inhibitory polypeptide,” Diabetes, 55(2):S86-S91 (2006). [cited by applicant]
Yip, R. G. et al., “Functional GIP Receptors are Present on Adipocytes,” Endocrinology, 139(9):4004-4007 (1998). [cited by applicant]
Yutaka, S. et al., “Glucose-dependent insulinotropic polypeptide and glucagon-like peptide-1: Incretin actions beyond the pancreas”, Journal of Diabetes Investigation, 4(2):108-130 (2013). [cited by applicant]
Zola, H., Monoclonal Antibodies: A Manual of Techniques, “Using Monoclonal Antibodies: Soluble Antigens,” CRC Press, Inc., Chapter 6, pp. 147-181 (1987). [cited by applicant]