Search Results - "Chirgadze, D. Y."
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The structure of EXTL3 helps to explain the different roles of bi-domain exostosins in heparan sulfate synthesis
Published in Nature communications (08-06-2022)“…Heparan sulfate is a highly modified O -linked glycan that performs diverse physiological roles in animal tissues. Though quickly modified, it is initially…”
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Thyroid stimulating autoantibody M22 mimics TSH binding to the TSH receptor leucine rich domain: a comparative structural study of protein–protein interactions
Published in Journal of molecular endocrinology (01-05-2009)“…The TSH receptor (TSHR) ligands M22 (a thyroid stimulating human monoclonal antibody) and TSH, bind to the concave surface of the leucine rich repeats domain…”
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3
FSH and TSH binding to their respective receptors: similarities, differences and implication for glycoprotein hormone specificity
Published in Journal of molecular endocrinology (01-09-2008)“…The crystal structures of the leucine-rich repeat domain (LRD) of the FSH receptor (FSHR) in complex with FSH and the TSH receptor (TSHR) LRD in complex with…”
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4
Characteristics of a human monoclonal autoantibody to the thyrotropin receptor: sequence structure and function
Published in Thyroid (New York, N.Y.) (01-08-2004)“…The properties of a human monoclonal antibody to the thyrotropin receptor (TSHR) (M22) with the characteristics of patient sera thyroid stimulating…”
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Characteristics of a monoclonal antibody to the thyrotropin receptor that acts as a powerful thyroid-stimulating autoantibody antagonist
Published in Thyroid (New York, N.Y.) (01-07-2005)“…Analysis of nine mouse monoclonal antibodies (mAbs) to the thyrotropin receptor (TSHR) with TSH antagonist activity showed that only one of the mAbs (RSR B2)…”
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Crystal Structures of Yersinia enterocolitica Salicylate Synthase and its Complex with the Reaction Products Salicylate and Pyruvate
Published in Journal of molecular biology (24-03-2006)“…The salicylate synthase, Irp9, from Yersinia enterocolitica is involved in the biosynthesis of the siderophore yersiniabactin. It is a bifunctional enzyme that…”
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Crystal structures of NK1-heparin complexes reveal the basis for NK1 activity and enable engineering of potent agonists of the MET receptor
Published in The EMBO journal (15-10-2001)“…NK1 is a splice variant of the polypeptide growth factor HGF/SF, which consists of the N‐terminal (N) and first kringle (K) domain and requires heparan sulfate…”
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Structure of an Xrcc4–DNA ligase IV yeast ortholog complex reveals a novel BRCT interaction mode
Published in DNA repair (07-03-2006)“…DNA ligase IV catalyses the final ligation step in the non-homologous end-joining (NHEJ) DNA repair pathway and requires interaction of the ligase with the…”
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Snapshot of Protein Structure Evolution Reveals Conservation of Functional Dimerization through Intertwined Folding
Published in Structure (London) (01-08-2004)“…Protein-protein interactions govern a wide range of cellular processes. Molecular recognition responsible for homodimerization and heterodimerization in the…”
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Structural basis for collagen recognition by the immune receptor OSCAR
Published in Blood (04-02-2016)“…The osteoclast-associated receptor (OSCAR) is a collagen-binding immune receptor with important roles in dendritic cell maturation and activation of…”
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Crystal structure of the NK1 fragment of HGF/SF suggests a novel mode for growth factor dimerization and receptor binding
Published in Nature structural biology (01-01-1999)“…Although ligand-induced receptor dimerization is a common prerequisite for receptor activation, the mode by which different growth factors bind their receptors…”
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Insights into the structure of hepatocyte growth factor/scatter factor (HGF/SF) and implications for receptor activation
Published in FEBS Letters (23-06-1998)“…The modular structure of HGF/SF offers a reductionist or `divide and rule' approach to the analysis of structure and function. Domain deletion experiments have…”
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A Nanobody Binding to Non-Amyloidogenic Regions of the Protein Human Lysozyme Enhances Partial Unfolding but Inhibits Amyloid Fibril Formation
Published in The journal of physical chemistry. B (24-10-2013)“…We report the effects of the interaction of two camelid antibody fragments, generally called nanobodies, namely cAb-HuL5 and a stabilized and more…”
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High-resolution crystal structure of the human Notch 1 ankyrin domain
Published in Biochemical journal (15-11-2005)“…The Notch receptor is part of a highly conserved signalling system of central importance to animal development. Its ANK (ankyrin) domain is required for…”
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Crystal structure of the β‐chain of human hepatocyte growth factor‐like/macrophage stimulating protein
Published in The FEBS journal (01-11-2005)“…Hepatocyte growth factor like/macrophage stimulating protein (HGFl/MSP) and hepatocyte growth factor/scatter factor (HGF/SF) define a distinct family of…”
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Structural constraints on protein self-processing in L-aspartate-α-decarboxylase
Published in The EMBO journal (01-12-2003)“…Aspartate decarboxylase, which is translated as a pro‐protein, undergoes intramolecular self‐cleavage at Gly24–Ser25. We have determined the crystal structures…”
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Molecular Dissection of the Interaction between the Small G Proteins Rac1 and RhoA and Protein Kinase C-related Kinase 1 (PRK1)
Published in The Journal of biological chemistry (12-12-2003)“…PRK1 is a serine/threonine kinase that belongs to the protein kinase C superfamily. It can be activated either by members of the Rho family of small G…”
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Crystal structures of NK1-heparin complexes reveal the basis for NK1 activity and enable engineering of potent agonists of the MET receptor
Published in Acta crystallographica. Section A, Foundations of crystallography (06-08-2002)“…Abstract only…”
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A New Crystal Form of the NK1 Splice Variant of HGF/SF Demonstrates Extensive Hinge Movement and Suggests That the NK1 Dimer Originates by Domain Swapping
Published in Journal of molecular biology (31-05-2002)“…NK1 is a splice variant of the polypeptide growth factor HGF/SF that consists of the N terminal (N) and first kringle (K) domains and retains receptor binding…”
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