IP Library › Granted Patent US 12,252,504
Granted Patent B2
US 12,252,504 · App. 17/671,249 · Granted Mar 18, 2025

Oligosaccharide-protein conjugates

Inventors: Luis Z. Avila (Arlington, MA); Clark Q. Pan (Sudbury, MA); Patrick Finn (Weymouth, MA); John Harrahy (Medway, MA); Qun Zhou (Ashland, MA); Yunxiang Zhu (Wayland, MA); Paul A. Konowicz (Maynard, MA); Duncan E. Paterson (Zurich, CH); Andreas Peer (Basel, CH); Joseph P. Kutzko (Southborough, MA); Michael R. Reardon (North Attleboro, MA); James E. Stefano (Hopkinton, MA); Xiaoyang Zheng (Newton, MA); Robert J. Miller (E. Bridgewater, MA); Lauren Young (Hampton, NH)
Assignee: Genzyme Corporation
C07H15/04A61K47/61A61K38/46
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Quick Facts
Patent No.
US 12,252,504
App. No.
17/671,249
Granted
Mar 18, 2025
Kind
B2
Abstract

Provided herein are conjugates comprising a protein and an oligosaccharide of one of Formulae I-VI. Also provided herein are pharmaceutical compositions comprising such conjugates. Further provided herein are methods of treating a lysosomal storage disorder in a mammal by administration of an oligosaccharide-glycoprotein conjugate.

Claims (6)

1. A pharmaceutical composition comprising an oligosaccharide-protein conjugate and an excipient comprising about 10 mM histidine pH 6.5, about 2% glycine, about 2% mannitol and about 0.01% polysorbate 80, wherein the oligosaccharide-protein conjugate comprises: (1) a protein, wherein the protein is acid a-glucosidase, and (2) an oligosaccharide of Formula A:

2. The pharmaceutical composition of claim 1 , wherein the oligosaccharide-protein conjugate further comprises a linker between the protein and the oligosaccharide of Formula A.

3. The pharmaceutical composition of claim 2 , wherein the linker comprises a reactive group for conjugation of the linker to the protein, wherein the reactive group is an aminooxy, hydrazide, or thiol group.

4. The pharmaceutical composition of claim 1 , wherein the oligosaccharide-protein conjugate comprises an oligosaccharide-linker having the structure of:

wherein the protein is conjugated to the linker through the aminooxy group of the linker.

5. The pharmaceutical composition of claim 1 , wherein the pharmaceutical composition has been reconstituted from a lyophilized powder.

Assignments (1)
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Mar 3, 2022
From: MILLER, ROBERT J.; AVILA, LUIZ Z.; PAN, CLARK Q.; FINN, PATRICK; HARRAHY, JOHN; ZHOU, QUN; ZHU, YUNXIANG; KONOWICZ, PAUL A.; KUTZKO, JOSEPH P.; REARDON, MICHAEL R.; STEFANO, JAMES E.; ZHENG, XIAOYANG; PATERSON, DUNCAN E; PEER, ANDREAS; YOUNG, LAUREN
To: GENZYME CORPORATION
Reel/Frame 059159/0232 →
Continuity (6)
Continuation 16581148 · Sep 24, 2019
Division 15288486 · Oct 7, 2016
Continuation 14445941 · Jul 29, 2014
Continuation 13140272
Provisional Application 61122851 · Dec 16, 2008
Related Publication 20220242899A1 · Aug 4, 2022
References Cited (400)
US 4671958A · Rodwell et al. · 1987 [cited by applicant]
US 4701521A · Ryser et al. · 1987 [cited by applicant]
US 4749570A · Poznansky · 1988 [cited by applicant]
US 4867973A · Goers et al. · 1989 [cited by applicant]
US 5153312A · Porro · 1992 [cited by applicant]
US 5179023A · Calhoun et al. · 1993 [cited by applicant]
US 5206370A · Schwartz et al. · 1993 [cited by applicant]
US 5212298A · Rademacher et al. · 1993 [cited by applicant]
US 5236838A · Rasmussen et al. · 1993 [cited by applicant]
US 5280113A · Rademacher et al. · 1994 [cited by applicant]
US 5306492A · Porro · 1994 [cited by applicant]
US 5312903A · Lina et al. · 1994 [cited by applicant]
US 5324663A · Lowe · 1994 [cited by applicant]
US 5420285A · Schwartz et al. · 1995 [cited by applicant]
US 5521290A · Sivam et al. · 1996 [cited by applicant]
US 5549892A · Friedman et al. · 1996 [cited by applicant]
US 5650096A · Harris et al. · 1997 [cited by applicant]
US 5658567A · Calhoun et al. · 1997 [cited by applicant]
US 5670488A · Gregory et al. · 1997 [cited by applicant]
US 5691154A · Callstrom et al. · 1997 [cited by applicant]
US 5719131A · Harris et al. · 1998 [cited by applicant]
US 5747471A · Siegel et al. · 1998 [cited by applicant]
US 5753520A · Schwartz et al. · 1998 [cited by applicant]
US 5767099A · Harris et al. · 1998 [cited by applicant]
US 5783565A · Lee et al. · 1998 [cited by applicant]
US 5834266A · Crabtree et al. · 1998 [cited by applicant]
US 5840702A · Bedwell · 1998 [cited by applicant]
US 5840710A · Lee et al. · 1998 [cited by applicant]
US 5846728A · Haralambidis et al. · 1998 [cited by applicant]
US 5851991A · Lee et al. · 1998 [cited by applicant]
US 5863990A · Papisov · 1999 [cited by applicant]
US 5910487A · Yew et al. · 1999 [cited by applicant]
US 5912239A · Siegel et al. · 1999 [cited by applicant]
US 5916911A · Shayman et al. · 1999 [cited by applicant]
US 5925628A · Lee et al. · 1999 [cited by applicant]
US 5935936A · Fasbender et al. · 1999 [cited by applicant]
US 5939401A · Marshall et al. · 1999 [cited by applicant]
US 5942634A · Siegel et al. · 1999 [cited by applicant]
US 5945442A · Shayman et al. · 1999 [cited by applicant]
US 5948767A · Scheule et al. · 1999 [cited by applicant]
US 5948925A · Keynes et al. · 1999 [cited by applicant]
US 5952370A · Shayman et al. · 1999 [cited by applicant]
US 5968502A · Treco et al. · 1999 [cited by applicant]
US 6022874A · Wheeler · 2000 [cited by applicant]
US 6030995A · Shayman et al. · 2000 [cited by applicant]
US 6040332A · Shayman et al. · 2000 [cited by applicant]
US 6051598A · Shayman et al. · 2000 [cited by applicant]
US 6066626A · Yew et al. · 2000 [cited by applicant]
US 6071890A · Scheule et al. · 2000 [cited by applicant]
US 6118045A · Reuser et al. · 2000 [cited by applicant]
US 6156547A · Roth · 2000 [cited by applicant]
US 6251858B1 · Monsigny et al. · 2001 [cited by applicant]
US 6287857B1 · O'Riordan et al. · 2001 [cited by applicant]
US 6399575B1 · Smith et al. · 2002 [cited by applicant]
US 6461609B1 · Calhoun et al. · 2002 [cited by applicant]
US 6465488B1 · Butter et al. · 2002 [cited by applicant]
US 6472506B1 · Moreau et al. · 2002 [cited by applicant]
US 6492332B1 · Demopulos et al. · 2002 [cited by applicant]
US 6495570B2 · Jacob et al. · 2002 [cited by applicant]
US 6534300B1 · Canfield · 2003 [cited by applicant]
US 6537785B1 · Canfield · 2003 [cited by applicant]
US 6541669B1 · Moran et al. · 2003 [cited by applicant]
US 6562316B1 · Edwards et al. · 2003 [cited by applicant]
US 6569451B1 · Li et al. · 2003 [cited by applicant]
US 6573337B1 · Toth et al. · 2003 [cited by applicant]
US 6610703B1 · Jacob et al. · 2003 [cited by applicant]
US 6642038B1 · Canfield · 2003 [cited by applicant]
US 6660749B2 · Butters et al. · 2003 [cited by applicant]
US 6670165B2 · Canfield · 2003 [cited by applicant]
US 6676963B1 · Lanza et al. · 2004 [cited by applicant]
US 6696059B2 · Jacob et al. · 2004 [cited by applicant]
US 6703488B1 · Burton et al. · 2004 [cited by applicant]
US 6723843B2 · Toth et al. · 2004 [cited by applicant]
US 6749865B2 · Calias et al. · 2004 [cited by applicant]
US 6770468B1 · Canfield · 2004 [cited by applicant]
US 6800273B2 · Rajopadhye et al. · 2004 [cited by applicant]
US 6800472B2 · Canfield et al. · 2004 [cited by applicant]
US 6828135B2 · Canfield · 2004 [cited by applicant]
US 6861242B2 · Canfield · 2005 [cited by applicant]
US 6905856B2 · Canfield et al. · 2005 [cited by applicant]
US 7001994B2 · Zhu · 2006 [cited by applicant]
US 7011831B2 · Calhoun et al. · 2006 [cited by applicant]
US 7019131B2 · Wong et al. · 2006 [cited by applicant]
US 7067127B2 · Canfield · 2006 [cited by applicant]
US 7141676B1 · Wilbur et al. · 2006 [cited by applicant]
US 7160517B2 · Seeberger et al. · 2007 [cited by applicant]
US 7176185B2 · Hilfinger et al. · 2007 [cited by applicant]
US 7232805B2 · Weinshenker et al. · 2007 [cited by applicant]
US 7312324B2 · Souza et al. · 2007 [cited by applicant]
US 7341720B2 · Stefano · 2008 [cited by applicant]
US 7723296B2 · Zhu · 2010 [cited by applicant]
US 7786277B2 · Zhu · 2010 [cited by applicant]
US 7910545B2 · Meeker et al. · 2011 [cited by applicant]
US 8124073B2 · Stefano · 2012 [cited by applicant]
US 8168587B2 · Meeker et al. · 2012 [cited by applicant]
US 8835614B2 · Avila et al. · 2014 [cited by applicant]
US 9493498B2 · Avila et al. · 2016 [cited by applicant]
US 10363291B2 · Zhu · 2019 [cited by applicant]
US 10792342B2 · Zhu · 2020 [cited by applicant]
US 10907142B2 · Zhu · 2021 [cited by applicant]
US 10973887B2 · Zhu · 2021 [cited by applicant]
US 11279725B2 · Roberts et al. · 2022 [cited by applicant]
US 20010031741A1 · Ziegler et al. · 2001 [cited by applicant]
US 20010044453A1 · Jacob et al. · 2001 [cited by applicant]
US 20020025550A1 · Canfield · 2002 [cited by applicant]
US 20020095135A1 · Meeker et al. · 2002 [cited by applicant]
US 20020127213A1 · Jacob et al. · 2002 [cited by applicant]
US 20020137125A1 · Zhu · 2002 [cited by applicant]
US 20020142985A1 · Dwek et al. · 2002 [cited by applicant]
US 20030017139A1 · Souza et al. · 2003 [cited by applicant]
US 20030050299A1 · Hirth et al. · 2003 [cited by applicant]
US 20030082176A1 · Lebowitz et al. · 2003 [cited by applicant]
US 20030087868A1 · Yew et al. · 2003 [cited by applicant]
US 20030119088A1 · Canfield et al. · 2003 [cited by applicant]
US 20030153768A1 · Hirth · 2003 [cited by applicant]
US 20040006008A1 · Lebowitz et al. · 2004 [cited by applicant]
US 20040014652A1 · Trouet et al. · 2004 [cited by applicant]
US 20040132640A1 · Defrees et al. · 2004 [cited by applicant]
US 20040204379A1 · Cheng et al. · 2004 [cited by applicant]
US 20050003486A1 · Canfield et al. · 2005 [cited by applicant]
US 20050026823A1 · Zankel et al. · 2005 [cited by applicant]
US 20050048047A1 · Kakkis · 2005 [cited by applicant]
US 20050058634A1 · Zhu · 2005 [cited by applicant]
US 20050075305A1 · Dwek et al. · 2005 [cited by applicant]
US 20050169941A1 · Lees · 2005 [cited by applicant]
US 20050169968A1 · Elmaleh et al. · 2005 [cited by applicant]
US 20050222244A1 · Siegel et al. · 2005 [cited by applicant]
US 20050267094A1 · Shayman et al. · 2005 [cited by applicant]
US 20050281805A1 · Lebowitz et al. · 2005 [cited by applicant]
US 20060051317A1 · Batrakova et al. · 2006 [cited by applicant]
US 20060074107A1 · Butters et al. · 2006 [cited by applicant]
US 20060281145A1 · Zhu · 2006 [cited by applicant]
US 20070178081A1 · Fan · 2007 [cited by applicant]
US 20080226658A1 · Stefano · 2008 [cited by applicant]
US 20100047225A1 · Zhu et al. · 2010 [cited by applicant]
US 20100173385A1 · Zhu · 2010 [cited by applicant]
US 20110142818A1 · Meeker et al. · 2011 [cited by applicant]
US 20120141507A1 · Stefano · 2012 [cited by applicant]
US 20120183502A1 · Meeker et al. · 2012 [cited by applicant]
US 20170014520A1 · Zhu et al. · 2017 [cited by applicant]
US 20170042979A1 · Stefano et al. · 2017 [cited by applicant]
US 20180002365A1 · Avila et al. · 2018 [cited by applicant]
US 20180085436A1 · Zhu et al. · 2018 [cited by applicant]
US 20190054154A1 · Stefano · 2019 [cited by applicant]
US 20200010825A1 · Zhu et al. · 2020 [cited by applicant]
US 20200147184A1 · Zhu et al. · 2020 [cited by applicant]
US 20220204963A1 · Zhu et al. · 2022 [cited by applicant]
EP 0384769A2 · 1990 [cited by applicant]
EP 1197222A2 · 2002 [cited by examiner]
EP 1171128B1 · 2003 [cited by applicant]
EP 2889043A2 · 2015 [cited by applicant]
JP S5936691A · 1984 [cited by applicant]
JP 2005535280A · 2005 [cited by applicant]
JP 2010516257A · 2010 [cited by applicant]
JP 2012512313A · 2012 [cited by applicant]
JP 2019112444A · 2019 [cited by applicant]
WO WO9216555A1 · 1992 [cited by applicant]
WO WO9709441A2 · 1997 [cited by applicant]
WO WO9734623A1 · 1997 [cited by applicant]
WO WO9811206A2 · 1998 [cited by applicant]
WO WO9941399A1 · 1999 [cited by applicant]
WO WO9941400A1 · 1999 [cited by applicant]
WO WO9957296A1 · 1999 [cited by applicant]
WO WO0062779A1 · 2000 [cited by applicant]
WO WO0062780A1 · 2000 [cited by applicant]
WO WO0160412A2 · 2001 [cited by applicant]
WO WO0190139A2 · 2001 [cited by applicant]
WO WO0207671A2 · 2002 [cited by applicant]
WO WO02057445A1 · 2002 [cited by applicant]
WO WO03031464A2 · 2003 [cited by applicant]
WO 2003046150A2 · 2003 [cited by applicant]
WO WO03057179A2 · 2003 [cited by applicant]
WO WO2005002515A2 · 2005 [cited by applicant]
WO WO2005014035A2 · 2005 [cited by applicant]
WO WO2005016973A1 · 2005 [cited by applicant]
WO WO2005034909A2 · 2005 [cited by applicant]
WO WO2005077093A2 · 2005 [cited by applicant]
WO WO2005094874A1 · 2005 [cited by applicant]
WO 2007084737A2 · 2007 [cited by applicant]
WO WO2008029281A2 · 2008 [cited by applicant]
WO WO2008089339A2 · 2008 [cited by applicant]
WO WO2008089339A3 · 2008 [cited by applicant]
WO WO2008089403A2 · 2008 [cited by applicant]
WO WO2008089403A3 · 2008 [cited by applicant]
WO WO2010075010A2 · 2010 [cited by applicant]
WO WO2010075010A3 · 2010 [cited by applicant]
JP 2007224052A ,machine translation, published Sep. 6, 2007. (Year: 2007). [cited by examiner]
A Guide to IUPAC Nomenclature of Organic Compounds (Recommendations 1993). “Specific Classes of Compounds R-5,6,6 Nitrogenous derivatives of carbonyl compounds” Blackwell scientific publications, (online), (retrieved on… [cited by applicant]
Abe et al. (Feb. 2000). “Glycosphingolipid depletion in fabry disease lymphoblasts with potent inhibitors of glucosylceramide synthase,” Kidney Intl. 57:446-454. [cited by applicant]
Abe et al. (Jun. 1, 2000). “Reduction of globotriaosylceramide in Fabry disease mice by substrate deprivation,” J. Clin. Invest. 105(11):1563-1571. [cited by applicant]
Abraham et al. (1993). “Heparin-binding EGF-like growth factor: characterization of rat and mouse cDNA clones, protein domain conservation across species, and transcript expression in tissues,” Biochem. Biophys. Res. Co… [cited by applicant]
Advanced Drug Delivery Reviews. Table of Contents, vol. 53, Iss. 2 (Dec. 17, 2001). [cited by applicant]
Advanced Drug Delivery Reviews. Table of Contents, vol. 54, Iss. 4 (Jun. 17, 2002). [cited by applicant]
Advanced Drug Delivery Reviews. Table of Contents, vol. 55, Iss. 2 (Feb. 10, 2003). [cited by applicant]
Advanced Drug Delivery Reviews. Table of Contents, vol. 56, Iss. 4 (Mar. 3, 2004). [cited by applicant]
Advanced Drug Delivery Reviews. Table of Contents, vol. 57, Iss. 4 (Feb. 28, 2005). [cited by applicant]
Amalfitano et al. (Aug. 1999). “Systemic correction of the muscle disorder glycogen storage disease type II after hepatic targeting of a modified adenovirus vector encoding human acid-alpha-glucosidase,” PNAS 96:8861-88… [cited by applicant]
Andersson et al. (2000). “N-butyldeoxygalactonojirimycin: a more selective inhibitor of glycosphingolipid biosynthesis than N-butyldeoxynojirimycin, in vitro and in vivo,” Biochem. Pharmacol. 59:821-829. [cited by applicant]
Arakatsu et al. (1966). “Immunochemical studies on dextrans. V. Specificity and cross-reactivity with dextrans of the antibodies formed in rabbits to isomaltonic and isomaltotrionic acids coupled to bovine serum albumin… [cited by applicant]
Ashwell et al. (1982). “Carbohydrate-specific receptors of the liver,” Ann. Rev. Biochem. 51:531-534. [cited by applicant]
Ashwell et al. (1972). “Carbohydrate Antigens: coupling of carbohydrates to proteins by a mixed anhydride reaction,” Meth. in Enzymology, vol. XXVII, Complete Carbohydrates, Part B, pp. 219-222. [cited by applicant]
Avigad et al. (1962). “The D-galactose oxidase of Polyporus circinatus,” J. Biol. Chem. 237:2736-2743. [cited by applicant]
Baba et al. (1988). “Preparation and application of a pentamannosyl monophosphate-bovine serum albumin conjugate,” Carbohydr. Res. 177:163-172. [cited by applicant]
Balaji et al. (Aug. 1994). “Molecular dynamics simulations of high-mannose oligosaccharides,” Glycobiology 4(4):497-515. [cited by applicant]
Barbon et al. (Sep. 2005). “AAV8-mediated hepatic expression of acid sphingomyelinase corrects the metabolic defect in the visceral organs of a mouse model of Niemann-Pick disease,” Mol. Ther. 12(3):431-440. [cited by applicant]
Barton et al. (1991). “Replacement therapy for inherited enzyme deficiency—macrophage-targeted glucocerebrosidase for Gaucher's disease,” N. Engl. J. Med. 324:1464-1470. [cited by applicant]
Bayer et al. (1987). “Enzyme-based detection of glycoproteins on blot transfers using avidin-biotin technology,” Anal. Biochem. 161:123-131. [cited by applicant]
Bayer et al. (1988). “Biocytin hydrazide—a selective label for sialic acids, galactose, and other sugars in glycoconjugates using avidin-biotin technology,” Anal. Biochem. 170:271-281. [cited by applicant]
Beesley et al. (2001). “Mutational analysis of 85 mucopolysaccharidosis type I families: frequency of known mutations, identification of 17 novel mutations and in vitro expression of missense mutations,” Hum. Genet. 109… [cited by applicant]
Berge et al. (1977). “Pharmaceutical salts,” J. Pharm. Sci. 66:1-19. [cited by applicant]
Bernstein et al. (1980). “A general synthesis of model glycoproteins: coupling of alkenyl glycosides to proteins, using reductive ozonolysis followed by reductive amination with sodium cyanoborohydride,” Carb. Res. 78:C… [cited by applicant]
Beutler et al. (1996). “Gaucher disease: four families with previously undescribed mutations,” Proc. Assoc. Am. Physicians 108:179-184. [cited by applicant]
Bielicki et al. (1999). “Advantages of using same species enzyme for replacement therapy in a feline model of mucopolysaccharidosis type VI,” J. Biol. Chem. 274(51):36335-36343. [cited by applicant]
Bijvoet et al. (1998). “Generalized glycogen storage and cardiomegaly in a knockout mouse model of Pompe disease,” Hum. Mol. Genet. 7(1):53-62. [cited by applicant]
Bijvoet et al. (1999). “Human acid α-glucosidase from rabbit milk has therapeutic effect in mice with glycogen storage disease type II,” Hum. Mol. Genet. 8(12):2145-2153. [cited by applicant]
Bodamer et al. (1997). “Dietary treatment in late-onset acid maltase deficiency,” Eur. J. Pediatr. 156(Suppl. 1):S39-S42. [cited by applicant]
Bond et al. (1997). “Structure of a human lysosomal sulfatase,” Structure 15:277-289. [cited by applicant]
Bongiorno et al. (2003). “Fabry disease: enzyme replacement therapy,” J. Eur. Acad. Dermatol. Venereol. 17:676-679. [cited by applicant]
Bou-Gharios et al. (1993). “Lysosomal storage diseases: mechanisms of enzyme replacement therapy,” Histochem. 25(9):593-605. [cited by applicant]
Bowie et al. (1990). “Deciphering the message in protein sequences: tolerance to amino acid substitutions,” Science 247:1306-1310. [cited by applicant]
Brady et al. (2001). “Enzyme replacement therapy in Fabry disease,” J. Inherit. Metab. Dis. 24(Suppl. 2):18-24. [cited by applicant]
Branco et al. (1999). “Selective deletion of antigen-specific, activated T cells by a humanized MAB to CD2 (MEDI-507) is mediated by NK cells,” Transpl. 68(10):1588-1596. [cited by applicant]
Branden et al. (1999). Introduction to Protein Structure, 2nd edition, Garland Publishing, Inc., New York: 1999; pp. 358-366. [cited by applicant]
Braslawsky et al. (1991). “Adriamycin(hydrazone)-antibody conjugates require internalization and intracellular acid hydrolysis for antitumor activity,” Cancer Immunol. Immunother. 33(6):367-374. [cited by applicant]
Bretthauer et al. (1973). “Characterization of a phosphorylated pentasaccharide isolated from Hansenula holstii NRRL Y-2448 phosphomannan,” Biochem. 12(7):1251-1256. [cited by applicant]
Brooks et al. (2001). “Glycosidase active site mutations in human alpha-L-iduronidase,” Glycobiol. 11(9):741-750. [cited by applicant]
Brooks et al. (1999). “Immune response to enzyme replacement therapy in lysosomal storage disorder patients and animal models,” Mol. Genet. Metabol. 68:268-275. [cited by applicant]
Brooks et al. (1991). “A specific fluorogenic assay for N-acetylgalactosamine-4-sulphatase activity using immunoads,” J. Inher. Metab. Dis. 14:5-12. [cited by applicant]
Buechner et al. (2008). “Central nervous system involvement in Anderson-Fabry disease: a clinical and MRI retrospective study,” J. Neurol. Neurosurg. Psychiatry 79(11):1249-1254. [cited by applicant]
Byers et al. (1997). “Effect of enzyme replacement therapy on bone formation in a feline model of mucopolysaccharidosis type VI,” Bone 21(5):425-431. [cited by applicant]
Caliceti et al. (2003). “Pharmacokinetic and biodistribution properties of poly(ethylene glycol)-protein conjugates,” Adv. Drug Deliv. Rev. 55(10):1261-1277. [cited by applicant]
Casares et al. (2001). “Antigen-specific downregulation of T cells by doxorubicin delivered through a recombinant MHC II-peptide chimera,” Nat. Biotechnol. 19:142-147. [cited by applicant]
Cavallaro et al. (2004). “Glycosylated macromolecular conjugates of antiviral drugs with a polyaspartamide,” J. Drug. Targeting 12(9-10):593-605. [cited by applicant]
Chaudhari et al. (1972). “Coupling of amino acids and amino sugars with cyanuric chloride (2,4,6-trichloro-s-triazine),” Can. J. Chem. 50(13):1987-1991. [cited by applicant]
Chen et al. (2000). “Purification and characterization of human α-galactosidase a expressed in insect cells using a baculovirus vector,” Protein Expr. Purif. 20:228-236. [cited by applicant]
Chen et al. (2000). “Towards a molecular therapy for glycogen storage disease type II (Pompe disease),” Mol. Med. Today 6(6):245-251. [cited by applicant]
Chen (1998). “Glycogen storage diseases,” in Harrison's principles of internal medicine, Fauci et al. (eds.); McGraw-Hill, 14 edition, pp. 2176-2182. [cited by applicant]
Christensen, M.K. et al. (1994). “Synthesis of Glycosylated Peptide Templates Containing 6′-O-Phosphorylated Mannose Disaccharides and Their Binding to the Cation-Independent Mannose 6-Phosphate Receptor,” Journal of th… [cited by applicant]
Civallero et al. (2006). “Twelve different enzyme assays on dried-blood filter paper samples for detection of patients with selected inherited lysosomal storage diseases,” Clin. Chim. Acta 372:98-102. [cited by applicant]
Cleary et al. (1995). “The presenting features of mucopolysaccharidosis type IH (Hurler syndrome),” Acta Paediatr. 84:337-339. [cited by applicant]
Colville et al. (1996). “Early presentation in the mucopolysaccharide disorders,” Child care, Health and Development 22(1):31-36. [cited by applicant]
Cox et al. (Apr. 2000). “Novel oral treatment of Gaucher's disease with N-butyldeoxynojirimycin (OGT 918) to decrease substrate biosynthesis,” Lancet 355:1481-1485. [cited by applicant]
Crawley et al. (1996). “Enzyme replacement therapy in a feline model of Maroteaux-Lamy syndrome,” J. Clin. Invest. 97(8):1864-1873. [cited by applicant]
Crich et al. (1998). “Direct chemical synthesis of β-mannopyranosides and other glycosides via glycosyl trillates,” Tetrahedron 54:8321-8348. [cited by applicant]
Czartoryska et al. (2000). “Changes in serum chitotriosidase activity with cessation of replacement enzyme (cerebrosidase) administration in Gaucher disease,” Clin. Biochem. 33(2):147-149. [cited by applicant]
Czartoryska et al. (1998). “Serum chitotriosidase activity in Gaucher patients on enzyme replacement therapy (ERT),” Clin. Biochem. 31(5):417-420. [cited by applicant]
Daniele et al. (2002). “Uptake of recombinant iduronate-2-sulfatase into neuronal and glial cells in vitro,” Biochim. Biophys. Acta 1588:203-209. [cited by applicant]
Davis et al. (1999). “Glycoprotein synthesis: from glycobiological tools to tailor-made catalysts,” Synlett 9:1495-1507. [cited by applicant]
Davis (1999). “Recent developments in glycoconjugates,” J. Chem. Soc. Perkin Trans. 1 1:3215-3237. [cited by applicant]
Davis (2002). “Synthesis of glycoproteins,” Chem. Rev. 102:579-601. [cited by applicant]
Day et al. (2003). “Induction of antigen-specific CTL responses using antigens conjugated to short peptide vectors,” J. Immunol. 170:1498-1503. [cited by applicant]
Demeule et al. (2002). “High transcytosis of melanotransferrin (P97) across the blood-brain barrier,” J. Neurochem. 83:924-933. [cited by applicant]
Den Tandt et al. (1996). “Marked increase of methylumbelliferyl-tetra-N-acetylchitotetraoside hydrolase activity in plasma from Gaucher disease patients,” J. Inherit. Metab. Dis. 19:344-350. [cited by applicant]
Deonarain (1998). “Ligand-targeted receptor mediated vectors for gene delivery,” Exp. Opin. Ther. Patents 8(1):53-69. [cited by applicant]
Derossi et al. (1998). “Trojan peptides: the penetratin system for intracellular delivery,” Trends Cell Biol. 8:84-87. [cited by applicant]
Desnick et al. (1979). “Enzyme therapy in Fabry disease: differential in vivo plasma clearance and metabolic effectiveness of plasma and splenic α-galactosidase A isozymes,” PNAS 76(10):5326-5330. [cited by applicant]
Desnick et al. (2003). “Fabry disease, an under-recognized multisystemic disorder: expert recommendations for diagnosis, management, and enzyme replacement therapy,” Ann. Int. Med. 138:338-346. [cited by applicant]
Desnick (1995). α-galactosidase A deficiency: Fabry disease in the metabolic and molecular bases of inherited disease, 7th edition, Scriver et al. (eds.), McGraw-Hill, New York, pp. 2741-2784. [cited by applicant]
Di Francesco et al. (1997). “In vitro correction of iduronate-2-sulfatase deficiency by adenovirus-mediated gene transfer,” Gene Ther. 4(5):442-448. [cited by applicant]
Distler et al. (1991). “The binding specificity of high and low molecular weight phosphomannosyl receptors from bovine testes: Inhibition studies with chemically synthesized 6-O-phosphorylated oligomannosides,” J. Biol.… [cited by applicant]
Dodelson De Kremer et al. (1997). “Actividad de la chitotriosidasa plasmatica en pacientes Argentinos con enfermedad de Gaucher Diversas lisosomopatias y en otras metabolopaties geneticas,” Medicina (Buenos Aires) 57:67… [cited by applicant]
Downing et al. (2006). “Synthesis of enzymatically active human alpha-L-iduronidase in [cited by applicant]
Dubowchik et al. (2002). “Cathepsin B-labile dipeptide linkers for lysosomal release of doxorubicin from internalizing immunoconjugates: model studies of enzymatic drug release and antigen-specific in vitro anticancer a… [cited by applicant]
Duffels et al. (2000). “Synthesis of high-mannose type neoglycolipids: active targeting of liposomes to macrophages in gene therapy,” Chem. Eur. J. 6(8):1416-1430. [cited by applicant]
Duncan et al. (1983). “A new reagent which may be used to introduce sulfhydryl groups into proteins, and its use in the preparation of conjugates for immunoassay,” Anal. Biochem. 132:68-73. [cited by applicant]
Durand et al. (1997). “Active-site motifs of lysosomal acid hydrolases: invariant features of clan GH-A glycosyl hydrolases deduced from hydrophobic cluster analysis,” Glycobiology 7(2)277-284. [cited by applicant]
Dvir et al. (2003). “X-ray structure of human acid-β-glucosidase, the defective enzyme in Gaucher disease,” EMBO Reports 4(7):1-6. [cited by applicant]
El Sayed, H. et al. (Jul. 1, 1982). “Stereoselective Syntheses of 1,2-cis- and 1,2-trans-D-mannopyranosides,” [cited by applicant]
Elliot et al. (1997). “Intercellular trafficking and protein delivery by a herpesvirus structural protein,” Cell 88:223-233. [cited by applicant]
Elstein et al. (Oct. 2007). “Oral maintenance clinical trial with miglustat for type I Gaucher disease: switch from or combination with intravenous enzyme replacement,” Blood 110(7):2296-2301. [cited by applicant]
Eng et al. (Jul. 2001). “Safety and efficacy of recombinant human alpha-galactosidase A-replacement therapy in Fabry's disease,” N. Engl. J. Med. 345(1):9-16. [cited by applicant]
Eto et al. (2004). “Treatment of lysosomal storage disorders: cell therapy and gene therapy,” J. Inherit. Metab. Dis. 27:411-415. [cited by applicant]
Etrych et al. (2001). “New HPMA copolymers containing doxorubicin bound via pH-sensitive linkage: synthesis and preliminary in vitro and in vivo biological properties,” J. Controlled Release 73:89-102. [cited by applicant]
European Patent Application No. 06740572.0 Summons to attend oral proceeding at the European Patent Office, dated Mar. 30, 2011. [cited by applicant]
Fawell et al. (Jan. 1994). “Tat-mediated delivery of heterologous proteins into cells,” PNAS 91:664-668. [cited by applicant]
Felice et al. (1995). “Clinical variability in adult-onset acid maltase deficiency: report of affected sibs and review of the literature,” Medicine (Baltimore) 74(3):131-135. [cited by applicant]
Fellgiebel et al. (Sep. 2006). “CNS manifestations of Fabry's disease,” Lancet Neurol. 5(9):791-795. [cited by applicant]
Fielder et al. (1970). “An immunogenic polysaccharide-protein conju-gate,” J. Immunol. 105(1):265-267. [cited by applicant]
Final Office Action mailed on Jun. 9, 2017, for U.S. Appl. No. 13/433,822, filed Mar. 29, 2012, 14 pages. [cited by applicant]
Final Office Action mailed on May 5, 2016, for U.S. Appl. No. 13/433,822, filed Mar. 29, 2012, 15 pages. [cited by applicant]
Final Office Action mailed on Jul. 8, 2014, for U.S. Appl. No. 13/433,822, filed Mar. 29, 2012, 12 pages. [cited by applicant]
Final Office Action mailed on Jan. 26, 2016, for U.S. Appl. No. 14/272,960, filed May 8, 2014, 6 pages. [cited by applicant]
Final Office Action mailed on Oct. 23, 2012, for U.S. Appl. No. 12/523,631, filed Aug. 20, 2009, 14 pages. [cited by applicant]
Final Office Action mailed on Jul. 19, 2016, for U.S. Appl. No. 14/463,955, filed Aug. 20, 2014, 5 pages. [cited by applicant]
Flomen et al. (Jan. 1993). “Determination of the organisation of coding sequences within the iduronate sulphate sulphatase (IDS) gene,” Hum. Mol. Genet. 2(1):5-10. [cited by applicant]
Freireich et al. (1966). “Quantitative comparison of toxicity of anticancer agents in mouse, rat, hamster, dog, monkey, and man,” Cancer Chemother. Rep. 50(4):219-244. [cited by applicant]
Friden et al. (1996). “Characterization, receptor mapping and blood-brain barrier transcytosis of antibodies to the human transferrin receptor,” J. Pharmacol. Exp. Ther. 278(3):1491-1498. [cited by applicant]
Fujita et al. (1992). “Targeted delivery of human recombinant superoxide dismutase by chemical modification with mono- and polysaccharide derivatives,” J. Pharmacol. Exp. Ther. 263(3):971-978. [cited by applicant]
Funhoff et al. (2005). “PEG shielded polymeric double-layered micelles for gene delivery,” J. Control Release 102(3):711-724. [cited by applicant]
Furbish et al. (1981). “Uptake and distribution of placental glucocerebrosidase in rat hepatic cells and effects of sequential deglycosylation,” Biochim. Biophys. Acta 673:425-434. [cited by applicant]
Gahmberg et al. (1992). “Cell surface carbohydrate in cell adhesion. Sperm cells and leukocytes bind to their target cells through specific oligosaccharide ligands,” APMIS Suppl 27:39-52. [cited by applicant]
Gahmberg et al. (1994). “Nonmetabolic radiolabeling and tagging of glycoconjugates,” Methods Enzymol. 230:32-44. [cited by applicant]
Gaillard et al. (2005). “Targeted delivery across the blood-brain barrier,” Expert Opin. Drug Deliv. 2(2):299-309. [cited by applicant]
Garman et al. (Sep.-Oct. 2002). “Structural basis of Fabry disease,” Mol. Genet. Metab. 77(1-2):3-11. [cited by applicant]
Garman et al. (2004). “The molecular defect leading to Fabry disease: structure of human α-galactosidase,” J. Mol. Biol. 337:319-335. [cited by applicant]
Gaziev et al. (2000). “Chronic graft-versus-host disease: is there an alternative to the conventional treatment?” Bone Marrow Transplant 25(7):689-696. [cited by applicant]
GenBank Accession No. AI587087, tr53e08.x1 NCI_CGAP_Pan1 [cited by applicant]
GenBank Accession No. NM_000152, “ [cited by applicant]
GenBank Accession No. X05790, “Human mRNA for alpha-galactosidase A (EC 3.2.1-22)” (1987). [cited by applicant]
Genzyme Corp. Prescribing information for Fabrazyme® (Nov. 2006) (available online at http://www.fabrazyme.com/hcp/pi/fz_us_hc_pi_pdf). [cited by applicant]
Geoghegan et al. (1992). “Site-directed conjugation of nonpeptide groups to peptides and proteins via periodate oxidation of a 2-amino alcohol. Application to modification at N-terminal serine,” Bioconjugate Chem. 3:138… [cited by applicant]
Ghose et al. (1983). “Preparation of antibody-linked cytotoxic agents,” Meth. Enzymol. 93:280-333. [cited by applicant]
Giugliani et al. (2007). “Management guidelines for mucopolysaccharidosis VI,” Pediatrics 120(2):405-418. [cited by applicant]
Gottschalk et al. (1994). “Folate receptor mediated DNA delivery into tumor cells: potosomal disruption results in enhanced gene expression,” Gene Ther. 1(3):185-191. [cited by applicant]
Grabowski et al. (1995). “Enzyme therapy in type 1 Gaucher disease: comparative efficacy of mannose-terminated glucocerebrosidase from natural and recombinant sources,” Ann. Intern. Med. 122(1):33-39. [cited by applicant]
Grady (Saturday, May 27, 2000). “Cell transplamts offer hope for severe cases of diabetes,” The New York Times, pp. A1 and A11. [cited by applicant]
Gray (1974). “The direct coupling of oligosaccharides to proteins and derivatized gels,” Arch. Biochem. Biophys. 163(1):426-428. [cited by applicant]
Gregoriadis et al. (Jan. 1993). “Polysialic acids: potential in drug delivery,” FEBS 315(3):271-276. [cited by applicant]
Gregoriadis et al. (1999). “Polysialylated proteins. An approach to improving enzyme stability and half-life in the blood circulation,” S.T.P. Pharma Sci. 9(1):61-66. [cited by applicant]
Grewal (1994). “Stroke in Fabry's disease,” J. Neurol. 241:153-156. [cited by applicant]
Grindley, B.T. (1998). “Applications of tin-containing intermediates to carbohydrate chemistry”, Advances in Carbohydrate Chem. & Biochem. 53:17-142. [cited by applicant]
Guffon et al. (1998). “Follow-up of nine patients with Hurler syndrome after bone marrow transplantation,” J. Pediatr. 133(1):119-125. [cited by applicant]
Gullingsrud et al. (1998). “Ocular abnormalities in the mucopolysaccharidoses after bone marrow transplantation. Longer follow-up,” Ophthalmology 105(6):1099-1105. [cited by applicant]
Gummert et al. (1999). “Newer immunosuppressive drugs: a review,” 10:1366-1380. [cited by applicant]
Guo et al. (1995). “Elevated plasma chitotriosidase activity in various lysosomal storage disorders,” J. Inherit Metab. Dis. 18:717-722. [cited by applicant]
Hagihara et al. (2006). “Exploration of oligosaccharide-protein interactions in glycoprotein quality control by synthetic approaches,” Chem. Rec. 6(6):290-302. [cited by applicant]
Hamann et al. (2002). “An anti-CD33 antibody-calicheamicin conjugate for treatment of acute myeloid leukemia. Choice of linker,” Bioconjug. Chem. 13:40-46. [cited by applicant]
Hara et al. (1994). “Mutation analysis of a Sandhoff disease patient in the Maronite community in Cyprus,” Hum. Genet. 94:136-140. [cited by applicant]
Helenius et al. (Mar. 2001). “Intracellular functions of N-linked glycans,” Science 291(5512):2364-2369. [cited by applicant]
Hembrough et al. (2004). “Identification and characterization of a very low density lipoprotein receptor-binding peptide from tissue factor pathway inhibitor that has antitumor and antiangiogenic activity,” Blood 103(9)… [cited by applicant]
Heng et al. (2001). “Synthesis of a mannotetraose—the repeating unit of the cell-wall mannans of Microsporum gypseum and related species of Trychophyton,” J. Carb. Chem. 20(3-4):285-296. [cited by applicant]
Henry (1999). “Cyclosporine and tacrolimus (FK506): A comparison of efficacy and safety profiles,” Clin. Transplant 13:209-220. [cited by applicant]
Hers (1965). “Inborn lysosomal diseases,” Gastroenterology 48(5):625-633. [cited by applicant]
Himmelspach et al. (1971). “Use of 1-(m-aminophenyl)flavazoles for the preparation of immunogens with oligosaccharide determinant groups,” Eur. J. Immunol. 1(2):106-112. [cited by applicant]
Hinman et al. (1993). “Preparation and characterization of monoclonal antibody conjugates of the calicheamicins: a novel and potent family of antitumor antibiotics,” Cancer Res. 53:3336-3342. [cited by applicant]
Hirschhorn (1995). “Glycogen storage disease type II: acid α-glucosidase (acid maltase) deficiency” in the metabolic and molecular bases of inherited disease, 7th edition, Scriver et al. (eds.), McGraw-Hill, New York, C… [cited by applicant]
Hodosi et al. (1997). “A fundamentally new, simple, sterospecific synthesis of oligosaccharides containing the β-mannopyranosyl and β-Rhamnopyranosyl linkage,” J. Am. Chem. Soc. 119:2335-2336. [cited by applicant]
Hodosi et al. (1998). “Glycosylation via locked anomeric configuration: stereospecific synthesis of oligosaccharides containing the β-D-mannopyranosyl and β-L-rhamnopyranosyl linkage,” Carbohydr. Res. 308:63-75. [cited by applicant]
Hoefsloot et al. (1990). “Characterization of the human lysosomal α-glucosidase gene,” Biochem. J. 272:493-497. [cited by applicant]
Hoefsloot et al. (1988). “Primary structure and processing of lysosomal α-glucosidase; homology with the intestinal sucrase-isomaltase complex,” EMBO J. 7:1697-1704. [cited by applicant]
Hojo et al. (2000). “Recent progress in the solid-phase synthesis of glycopeptide,” Current Prot. Peptide Sci. 1:23-48. [cited by applicant]
Hollak et al. (1994). “Marked elevation of plasma chitotriosidase activity. A novel hallmark of Gaucher disease,” J. Clin. Invest. 93(3):1288-1292. [cited by applicant]
Hong et al. (2000). : Immunosuppressive agents in organ transplantation: past, present, and future, Semin. Nephrol. 20(2):108-125. [cited by applicant]
Horinouchi et al. (1995). “Acid sphingomyelinase deficient mice: a model of types A and B Niemann-Pick disease,” Nat. Genet. 10:288-293. [cited by applicant]
Ideguchi et al. (2000). “Local adenovirus-mediated CTLA4-immunoglobulin expression suppresses the immune responses to adenovirus vectors in the brain,” Neuroscience 95(1):217-226. [cited by applicant]
International Search Report and Written Opinion issued in international patent application No. PCT/US2006/012698, date of mailing: Nov. 10, 2006. [cited by applicant]
International Search Report issued in international patent application No. PCT/US2001/19579, date of mailing: Aug. 28, 2002. [cited by applicant]
International Search Report and Written Opinion issued in international patent application No. PCT/US2008/051429, date of mailing: Oct. 7, 2008. [cited by applicant]
International Search Report and Written Opinion issued in international patent application No. PCT/US2008/051327, date of mailing: Jul. 10, 2008. [cited by applicant]
International Search Report and Written Opinion issued in international patent application No. PCT/US2009/067775, date of mailing: Nov. 17, 2010. [cited by applicant]
Ioannou et al. (2001). “Fabry disease: preclinical studies demonstrate the effectiveness of alpha-galactosidase A replacement in enzyme-deficient mice,” Am. J. Hum. Genet. 68:14-25. [cited by applicant]
Ioannou et al. (1996). “Fabry disease: enzyme replacement therapy in α-galactosidase a deficient mice,” Am. J. Hum. Genet. 59(4 Suppl.):A15, Abstr. 71. [cited by applicant]
Ioannou et al. (Dec. 1992). “Overexpression of human alpha-galactosidase A results in its intracellular aggregation, crystallization in lysosomes, and selective secretion,” J. Cell Biol. 119(5):1137-1150. [cited by applicant]
Ito et al. (2000). “Induction of CTL responses by simultaneous administration of liposomal peptide vaccine with anti-CD40 and anti-CTLA-4 mAb,” J. Immunol. 164:1230-1235. [cited by applicant]
Itoh et al. (1995). Synthesis of alkyl β-mannosides from mannobiose by aspergillus niger β-mannosidase, J. Fermentation & Bioengin. 80(5):510-512. [cited by applicant]
Jeyakumar et al. (May 1999). “Delayed symptom onset and increased life expectancy in Sandhoff disease mice treated with N-butyldeoxynojirimycin,” PNAS 96:6388-6393. [cited by applicant]
Jeyakumar et al. (Jan. 2001). “Enhanced survival in Sandhoff disease mice receiving a combination of substrate deprivation therapy and bone marrow transplantation,” Blood 97(1):327-329. [cited by applicant]
Jeyakumar et al. (2002). “Glycosphingolipid lysosomal storage diseases: therapy and pathogenesis,” Neuropathol. Appl. Neurobiol. 28:343-357. [cited by applicant]
Kakavanos et al. (2003). “Immune tolerance after long-term enzyme-replacement therapy among patients who have mucopolysaccharidosis I,” Lancet 361:1608-1613. [cited by applicant]
Kakkis et al. (1996). “Long-term and high-dose trials of enzyme replacement therapy in the canine model of mucopolysaccharidosis I,” Biochem. Mol. Med. 58(2):156-167. [cited by applicant]
Kakkis et al. (1994). “Overexpression of the human lysosomal enzyme alpha-L-iduronidase in Chinese hamster ovary cells,” Prot. Express. Purif. 5:225-232. [cited by applicant]
Kakkis et al. (2004). “Successful induction of immune tolerance to enzyme replacement therapy in canine mucopolysaccharidosis I,” PNAS 101(3):829-834. [cited by applicant]
Kamada et al. (Apr. 2003). “Synthesis of a poly(vinylpyrrolidone-co-dimethyl maleic anhydride) co-polymer and its application for renal drug targeting,” Nat. Biotechnol. 21:399-404. [cited by applicant]
Kaneko et al. (1991). “New hydrazone derivatives of adriamycin and their immunoconjugates—a correlation between acid stability and cytotoxicity,” Bioconjugate Chem. 2(3):133-141. [cited by applicant]
Kaye et al. (Sep. 1990). “A single amino acid substitution results in a retinoblastoma protein defective in phosphorylation and oncoprotein binding,” PNAS 87:6922-6926. [cited by applicant]
Keeling et al. (2001). “Gentamicin-mediated suppression of Hurler syndrome stop mutations restores a low level of α-L-iduronidase activity and reduces lysosomal glycosaminoglycan accumulation,” Hum. Molec. Genet. 10(3):… [cited by applicant]
Kelly et al. (1996). “Primary structure of bovine adenosine deaminase,” J. Pharm. Biomed. Analysis 14:1513-1519. [cited by applicant]
Kikuchi et al., “Clinical and Metabolic Correction of Pompe Disease by Enzyme Therapy in Acid Maltase deficient Quail” J. Clin. Invest. 101(4):827-833 (1998). [cited by applicant]
Kim et al., “Mutational spectrum of the iduronate 2 sulfatase gene in 25 unrelated Korean Hunter syndrome patients: Identification of 13 novel mutations” Hum. Mutat. 21:499-450 (2003). [cited by applicant]
Kim et al., J. “Stereoselective direct glycosylalion with anomeric hydroxyl sugars by activation with phthalic anhydride and trifluoromethanesulfonic anhydride involving glycosyl phthalate intermediates.” J. Am. Chem. S… [cited by applicant]
Kim et al., “Identification of Novel SNPs in the Interleukin 6 Receptor Gene (IL6R)” Hum. Mutat. 21:450-451 (2003). Online citation: Mutation in Brief #601, 5 pp., http://onlinelibrary.wiley.com/doi/10.2002/humu.9130/pd… [cited by applicant]
King et al., “Preparation of Protein Conjugates via Intermolecular Hydrazone Linkage” Biochemistry 25:5774-5779 (1986). [cited by applicant]
King et al., “Monoclonal Antibody Conjugates of Doxorubicin Prepared with Branched Linkers: A Novel Method for Increasing the Potency of Doxorubicin Immunoconjugates” Bioconjugate Chem. I0:279-288 (1999). [cited by applicant]
Kleinhammer et al., “Synthesis and immunological properties of an artificial antigen with the repeating oligosaccharide unit of [cited by applicant]
Ko et al., “Atypical Fabry's Disease, An Oligosymptomatic Variant” Arch. Pathol. Lab. Med. 120:86-89 (1996). [cited by applicant]
Kolodny et al., “Storage Diseases of the Reticuloendothelial System” in Nathan and Oski's Hematology of Infancy and Childhood, 5th Edition. vol. 2. David G. Nathan and Stuart H. Orkin (Eds.) W.B. Saunders Co.: 1998; Ch … [cited by applicant]
Kolonin et al., “Reversal of obesity by targeted ablation of adipose tissue” Nature Med. 10:625-632 (2004). [cited by applicant]
Kornfeld et al., The Biogenesis of Lysosomes Annu. Rev: Cell Biol. 5:483-525 (1989). [cited by applicant]
Kralovec et al., “Synthesis of site-specific methotrexate-IgG conjugates. Comparison of stability and antihumor activity with active ester-based conjugates” Cancer Immunol. Immunother,. 29:293-302 (1989). [cited by applicant]
Kurlberg et al., “Blockade of the B7-CD26 Pathway by CTLA4-Ig Counteracts Rejection and Prolongs Survival in Small Bowel Transplantation” Scand. J. Immunol. 51:224-230 (2000). [cited by applicant]
Lanciotti et al., “Targeting Adenoviral Vectors Using Heterofunctional Polyethylene Glycol FGF2 Conjugates” Mol. Ther. 8(1):99-107 (2003). [cited by applicant]
Lansmann et al., “Human acid sphingomyelinase. Assignment of the disulfide bond pattern” Eur. J. Biochem. 270:1076-1088 (2003). [cited by applicant]
Lebowitz et al., “Glycosylation-independent targeting enhances enzyme delivery to lysosomes and decreases storage in mucopolysaccharidosis type VII mice” PNAS 101(9):3083-3088 (Mar. 2004). [cited by applicant]
Lecolley et al., “A new approach to bioconjugates for proteins and peptides (pegylation▪) utilising living radical polymerisation” Chem. Commun. 18:2026-2027 (2004). [cited by applicant]
Lee et al., “2-Imino-2-Methoxyethyl 1-Thioglycosides: New Reagents for Attaching Sugars to Proteins” Biochemistry 15(18):3956-3963 (1976). [cited by applicant]
Lee et al., “A Biochemical and Pharmacological Comparison of Enzyme Replacement Therapies for the Glycolipid Storage Disorder Fabry Disease” Glycobiology 13(4):305-313 (2003). [cited by applicant]
Lee et al., “Improved Inhibitors of Glucosylceramide Synthase” J. Biol. Chem. 274(21):14662-14669 (May 21, 1999). [cited by applicant]
Lee et al., “Receptor mediated uptake of peptides that bind the human transferrin receptor” Eur. J. Biochem. 268:2004-2012 (2001). [cited by applicant]
Lee et al., “N-Terminal Site-Specific Mono-PEGylation of Epidermal Growth Factor” Pharm. Res. 20(5):818-825 (May 2003). [cited by applicant]
Lees et al., “Versatile and efficient synthesis of protein-polysaccharide conjugate vaccines using aminooxy reagents and oxime chemistry” Vaccine 24:716-729 (2006). [cited by applicant]
Lemieux et al., “The Properties of a ‘Synthetic’ Antigen Related to the Human Blood-Group Lewis a” J. Am. Chem. Soc. 97(14):4076-4083 (1975). [cited by applicant]
Leonard et al., “Cytokine Receptor Signaling Pathways” J. Allergy Clin. Immunol. 105:877-888 (2000). [cited by applicant]
Li et al., “Isolation and Characterization of Mannose 6-Phosphate/Insulin-Like Growth Factor II Receptor from Bovine Serum” Glycobiol. 1(5):511-517 (1991). [cited by applicant]
Li et al., “Direct Multiplex Assay of Lysosomal Enzymes in Dried Blood Spots for Newborn Screening” Clin. Chem. 50(10):1785-1796 (2004). [cited by applicant]
Liou et al., “Analyses of Variant Acid β▪Glucosidases. Effects of Gaucher Disease Mutations” J. Biol. Chem. 281(7):4242-4253 (Feb. 2006). [cited by applicant]
Lisi et al., “Enzyme Therapy. I. Polyethylene Glycol:β-Glucuronidase Conjugates as Potential Therapeutic Agents in Acid Mucopolysaccharidosis” J. Appl. Biochem. 4:19-33 (1982). [cited by applicant]
Litjens et al., “An N-acetylgalactosamine-4-sulfatase mutation (Δ G228) results in a severe Maroteaux-Lamy phenotype” Hum. Mut. 1(5):397-402 (1992). [cited by applicant]
Lovering et al., “Mechanistic and Structural Analysis of a Family 31 a-Glycosidase and Its glycosyl-enzyme Intermediate” J. Biol. Chem. 280(3):2105-2115 (2005). [cited by applicant]
Macdermott et al.,“Anderson-Fabry disease: clinical manifestations and impact of disease in a cohort of 98 hemizygous males” J. Med. Genet. 38:750-760 (2001). [cited by applicant]
Mann et al., “Endocytosis and targeting of exogenous HIV-1 Tat protein” EMBO J. 10(7):1733-1739 (1991). [cited by applicant]
Marinova-Mutafchieva et al., “A Comparative Study Into the Mechanisms of Action of Anti-Tumor Necrosis Factor α. Anti CD4, and Combined Anti-Tumor Necrosis Factor α/anti-CD4 Treatment in Early Collagen-Induced Arthritis… [cited by applicant]
Marshall et al., “Improved management of lysosomal glucosylceramide levels in a mouse model of type 1 Gaucher disease using enzyme and substrate reduction therapy” J. Inherit. Metab. Dis. 33:281-289 (2010). [cited by applicant]
Marshall et al., “Demonstration of Feasibility of In Vivo Gene Therapy for Gaucher Disease Using a Chemically Induced Mouse Model” Mol. Ther. 6(2):179-189 (Aug. 2002). [cited by applicant]
Martiniuk et al., “Isolation of a cDNA for human acid α-glucosidase and detection of genetic heterogeneity for mRNA, in three α-glucosidase-deficient patients” Proc. Natl. Acad. Sci. USA 83:9641-9644 (1986). [cited by applicant]
Masson et al., “Fabry Disease: A Review” Joint Bone Spine 71:381-383 (2004). [cited by applicant]
Masterson et al., “Hip Dysplasia in Hurler's Syndrome: Orthopaedic Management After Bone Marrow Transplantation” J. Pediatr. Ortho. 16:731-733 (1996). [cited by applicant]
Matsuura et al., “Human α-Galactosidase A: Characterization of the N-Linked Oligosaccharides on the Intracellular and Secreted Glycoforms Overexpressed by Chinese Hamster Ovary Cells” Glycobiology 8(4):329-339 (1998). [cited by applicant]
Matsuzawa et al., “Fabry disease: correlation between structural changes in α-galactosidase, and clinical and biochemical phenotypes” Hum. Genet. 117:317-328 (2005). [cited by applicant]
Mayer et al., “Synthesis of Labeled Glycosyl Phosphatidyl Inositol (GPI) Anchors” Eur. J. Org. Chem. 1999(10):2563-2571 (1999). [cited by applicant]
Mayes et al., “Differential assay for lysosomal α-galactosidases in human tissues and its application to Fabry's disease” Clin. Chem. Acta 112:247-251 (1981). [cited by applicant]