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Genomes and Genes | S R HubbardSummaryAffiliation: New York University Country: USA Publications
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Publications
Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analogS R Hubbard
Department of Pharmacology and Skirball Institute of Biomolecular Medicine, 540 First Avenue, New York University Medical Center, New York, NY 10016, USA
EMBO J 16:5572-81. 1997..The structure thus reveals the molecular basis for insulin receptor activation via autophosphorylation, and provides insights into tyrosine kinase substrate specificity and the mechanism of phosphotransfer...- Structural analysis of receptor tyrosine kinasesS R Hubbard
Skirball Institute of Biomolecular Medicine, New York University Medical Center, New York 10016, USA
Prog Biophys Mol Biol 71:343-58. 1999..This review will highlight the key results that have emerged from these structural studies... - Protein tyrosine kinase structure and functionS R Hubbard
Skirball Institute of Biomolecular Medicine and Department of Pharmacology, New York University School of Medicine, New York, New York 10016, USA
Annu Rev Biochem 69:373-98. 2000..This review will highlight the important results that have emerged from these structural studies... - Crystallographic and solution studies of an activation loop mutant of the insulin receptor tyrosine kinase: insights into kinase mechanismJ H Till
Skirball Institute of Biomolecular Medicine and Department of Pharmacology, New York University School of Medicine, New York, New York 10016, USA
J Biol Chem 276:10049-55. 2001..The crystallographic and solution studies provide new insights into the mechanism by which the activation loop controls phosphoryl transfer as catalyzed by the insulin receptor... - Structural basis for FGF receptor dimerization and activationA N Plotnikov
Department of Pharmacology, New York University School of Medicine, New York 10016, USA
Cell 98:641-50. 1999..A general model for FGF- and heparin-induced FGFR dimerization is inferred from the crystal structure, unifying a wealth of biochemical data... - Crystal structures of two FGF-FGFR complexes reveal the determinants of ligand-receptor specificityA N Plotnikov
Department of Pharmacology, New York University School of Medicine, New York 10016, USA
Cell 101:413-24. 2000..These structures provide a molecular basis for FGF1 as a universal FGFR ligand and for modulation of FGF-FGFR specificity through primary sequence variations and alternative splicing... - Structures of the tyrosine kinase domain of fibroblast growth factor receptor in complex with inhibitorsM Mohammadi
Department of Pharmacology, New York University Medical Center, New York, NY 10016, USA
Science 276:955-60. 1997..This structural information will facilitate the design of new inhibitors for use in the treatment of cancer and other diseases in which cell signaling by tyrosine kinases plays a crucial role in disease pathogenesis... - Crystal structure of the ARF-GAP domain and ankyrin repeats of PYK2-associated protein betaV Mandiyan
Department of Pharmacology, Skirball Institute of Biomolecular Medicine, New York University Medical School, New York, NY 10016, USA
EMBO J 18:6890-8. 1999..An invariant arginine and several nearby hydrophobic residues are solvent exposed and are predicted to be the site of interaction with ARFs. Site-directed mutagenesis of these residues confirms their importance in ARF-GAP activity... - The BPS domain of Grb10 inhibits the catalytic activity of the insulin and IGF1 receptorsE G Stein
Skirball Institute of Biomolecular Medicine, Department of Pharmacology, New York University School of Medicine, NY, 10016, USA
FEBS Lett 493:106-11. 2001..These studies provide a molecular mechanism by which Grb10 functions as a negative regulator of insulin- and/or IGF1-mediated signaling... - Structure of the FGF receptor tyrosine kinase domain reveals a novel autoinhibitory mechanismM Mohammadi
Department of Pharmacology, New York University Medical Center, New York 10016, USA
Cell 86:577-87. 1996..Finally, the structure provides a basis for rationalizing the effects of kinase mutations in FGF receptors that lead to developmental disorders in nematodes and humans... - Theme and variations: juxtamembrane regulation of receptor protein kinasesS R Hubbard
Skirball Institute of Biomolecular Medicine and Department of Pharmacology, New York University School of Medicine, New York, NY 10016, USA
Mol Cell 8:481-2. 2001.... - Structural basis for inhibition of the insulin receptor by the adaptor protein Grb14Rafael S Depetris
Structural Biology Program, Skirball Institute of Biomolecular Medicine and Department of Pharmacology, New York University School of Medicine, New York, New York 10016, USA
Mol Cell 20:325-33. 2005..Together with the crystal structure of the SH2 domain, we present a model for the interaction of Grb14 with the insulin receptor, which indicates how Grb14 functions as a selective protein inhibitor of insulin signaling... - Crystal structure of a complex between protein tyrosine phosphatase 1B and the insulin receptor tyrosine kinaseShiqing Li
Structural Biology Program, Skirball Institute of Biomolecular Medicine and Department of Pharmacology, New York University School of Medicine, New York, New York 10016, USA
Structure 13:1643-51. 2005..The crystal structure provides evidence for a noncatalytic mode of interaction between PTP1B and IRK, which could be important for the selective recruitment of PTP1B to the insulin receptor... - EGF receptor activation: push comes to shoveStevan R Hubbard
Structural Biology Program, Skirball Institute of Biomolecular Medicine, and Department of Pharmacology, New York University School of Medicine, New York, NY 10016, USA
Cell 125:1029-31. 2006.... - Structural basis for phosphotyrosine recognition by the Src homology-2 domains of the adapter proteins SH2-B and APSJunjie Hu
Structural Biology Program, Skirball Institute of Biomolecular Medicine, and Department of Pharmacology, New York University School of Medicine, NY 10016, USA
J Mol Biol 361:69-79. 2006..This differential specificity is attributable to the difference in the oligomeric states of the two SH2 domains: monomeric for SH2-B and dimeric for APS... - Crystal structure of the agrin-responsive immunoglobulin-like domains 1 and 2 of the receptor tyrosine kinase MuSKAmy L Stiegler
Structural Biology Program, Skirball Institute of Biomolecular Medicine and Department of Pharmacology, New York University School of Medicine, New York, NY 10016, USA
J Mol Biol 364:424-33. 2006..Biochemical analyses of MuSK mutants introduced into MuSK(-/-) myotubes demonstrate that residues in this hydrophobic patch are critical for agrin-induced MuSK activation... - Receptor tyrosine kinases: mechanisms of activation and signalingStevan R Hubbard
Skirball Institute of Biomolecular Medicine and Department of Pharmacology, New York University School of Medicine, New York, NY 10016, USA
Curr Opin Cell Biol 19:117-23. 2007.... - Crystal structure of the human laminin receptor precursorKelly V Jamieson
Gene Therapy Center, Cancer Institute and Department of Pathology, New York University School of Medicine, New York, New York 10016, USA
J Biol Chem 283:3002-5. 2008..Here, we report the crystal structure of human LamR, which provides insights into its function and should facilitate the design of novel therapeutics targeting LamR... - How IRE1 reacts to ER stressDavid Ron
Kimmel Center for Biology and Medicine of the Skirball Institute, New York University School of Medicine, New York, NY 10016, USA
Cell 132:24-6. 2008..2008). This structure provides new insight into the mysterious coupling of kinase and endoribonuclease activities in the oldest, most-conserved branch of the unfolded protein response in eukaryotes... - Structural and biochemical characterization of the KRLB region in insulin receptor substrate-2Jinhua Wu
Structural Biology Program, Kimmel Center for Biology and Medicine of the Skirball Institute, and Department of Pharmacology, New York University School of Medicine, 540 First Avenue, New York, New York 10016, USA
Nat Struct Mol Biol 15:251-8. 2008..Although Tyr628 was phosphorylated by the insulin receptor, its catalytic turnover was poor, resulting in kinase inhibition. Our studies indicate that the KRLB region functions to limit tyrosine phosphorylation of IRS2... - Small-molecule inhibition and activation-loop trans-phosphorylation of the IGF1 receptorJinhua Wu
Structural Biology Program, Kimmel Center for Biology and Medicine of the Skirball Institute of Biomolecular Medicine, Department of Pharmacology, New York University School of Medicine, New York, NY 10016, USA
EMBO J 27:1985-94. 2008.... - EGF receptor inhibition: attacks on multiple frontsStevan R Hubbard
Structural Biology Program, Skirball Institute of Biomolecular Medicine, New York University School of Medicine, New York, New York 10016, USA
Cancer Cell 7:287-8. 2005..Cetuximab targets one of the ligand binding domains of EGFR, thus preventing ligand activation of the receptor... - Structural characterization of a novel Cbl phosphotyrosine recognition motif in the APS family of adapter proteinsJunjie Hu
Structural Biology Program, Skirball Institute of Biomolecular Medicine and Department of Pharmacology, New York University School of Medicine, New York, New York 10016, USA
J Biol Chem 280:18943-9. 2005..These studies reveal a novel mode of phosphopeptide interaction with the Cbl TKB domain, in which N-terminal residues distal to the phosphotyrosine directly contact residues of the four-helix bundle of the TKB domain... - Autoinhibitory mechanisms in receptor tyrosine kinasesStevan R Hubbard
Skirball Institute of Biomolecular Medicine and Department of Pharmacology, New York University School of Medicine, New York, NY 10016, USA
Front Biosci 7:d330-40. 2002..This review will focus on the autoinhibitory mechanisms that modulate RTK catalytic activity... - Crystal structure of the MuSK tyrosine kinase: insights into receptor autoregulationJeffrey H Till
Skirball Institute of Biomolecular Medicine and Department of Pharmacology, New York University School of Medicine, New York, NY 10016, USA
Structure 10:1187-96. 2002..These studies provide a molecular basis for understanding the regulation of MuSK catalytic activity and suggest that an additional in vivo component may contribute to regulation via the juxtamembrane region... - Protein tyrosine kinases: autoregulation and small-molecule inhibitionStevan R Hubbard
Skirball Institute of Biomolecular Medicine and Department of Pharmacology, New York University School of Medicine, New York 10016, USA
Curr Opin Struct Biol 12:735-41. 2002.... - Structural basis for dimerization of the Grb10 Src homology 2 domain. Implications for ligand specificityEvan G Stein
Skirball Institute of Biomolecular Medicine and Department of Pharmacology, New York University School of Medicine, New York, New York 10016, USA
J Biol Chem 278:13257-64. 2003..Moreover, the structure suggests the mechanism by which the Grb7 SH2 domain binds selectively to pTyr-1139 (pYVNQ) in Her2, which along with Grb7 is co-amplified in human breast cancers... - Structural and biochemical evidence for an autoinhibitory role for tyrosine 984 in the juxtamembrane region of the insulin receptorShiqing Li
Skirball Institute of Biomolecular Medicine and Department of Pharmacology, New York University School of Medicine, New York, New York 10016, USA
J Biol Chem 278:26007-14. 2003..In addition, the structural studies suggest a possible target site for small molecule activators of the insulin receptor, with potential use in the treatment of noninsulin-dependent diabetes mellitus... - Agrin/MuSK signaling: willing and AblSteven J Burden
Nat Neurosci 6:653-4. 2003 - Structural basis for recruitment of the adaptor protein APS to the activated insulin receptorJunjie Hu
Skirball Institute of Biomolecular Medicine and Department of Pharmacology, New York University School of Medicine, New York, NY 10016, USA
Mol Cell 12:1379-89. 2003..This structure provides a molecular visualization of one of the initial downstream recruitment events following insulin activation of its dimeric receptor... - Juxtamembrane autoinhibition in receptor tyrosine kinasesStevan R Hubbard
Skirball Institute of Biomolecular Medicine and Department of Pharmacology, New York University School of Medicine, New York 10016, USA
Nat Rev Mol Cell Biol 5:464-71. 2004 - Structural basis for phosphotyrosine recognition by suppressor of cytokine signaling-3Elisa Bergamin
Structural Biology Program, Skirball Institute of Biomolecular Medicine and Department of Pharmacology, New York University School of Medicine, New York, New York 10016, USA
Structure 14:1285-92. 2006..In addition, the structure provides insights into the possible mechanisms by which SOCS3 and SOCS1 inhibit JAK2 kinase activity... - Oncogenic mutations in B-Raf: some losses yield gainsStevan R Hubbard
Skirball Institute of Biomolecular Medicine and Department of Pharmacology, New York University School of Medicine, New York, NY 10016, USA
Cell 116:764-6. 2004..Surprisingly, several mutations lead to impaired B-Raf kinase activity, yet these mutants are nevertheless capable of stimulating downstream signaling through transactivation of C-Raf... - Bisubstrate analog probes for the insulin receptor protein tyrosine kinase: molecular yardsticks for analyzing catalytic mechanism and inhibitor designAliya C Hines
Department of Pharmacology and Molecular Sciences, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA
Bioorg Chem 33:285-97. 2005..Taken together, these results suggest that a combination of mechanism-based design and empirical synthetic manipulation will be necessary in producing optimized protein kinase bisubstrate analog inhibitors... - IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNAMarcella Calfon
Skirball Institute of Biomolecular Medicine, New York University School of Medicine, New York, NY 10016, USA
Nature 415:92-6. 2002..Our findings suggest that physiological ER load regulates a developmental decision in higher eukaryotes... - Lrp4 is a receptor for Agrin and forms a complex with MuSKNatalie Kim
Molecular Neurobiology Program, Skirball Institute of Biomolecular Medicine, Helen and Martin Kimmel Center for Biology and Medicine, NYU Medical School, New York, NY 10016, USA
Cell 135:334-42. 2008..Here, we report that Lrp4, a member of the LDLR family, is a receptor for Agrin, forms a complex with MuSK, and mediates MuSK activation by Agrin...