Structural characterization of the ectodomain of a disintegrin and metalloproteinase-22 (ADAM22), a neural adhesion receptor instead of metalloproteinase: insights on ADAM function - Wikidata - wikimedia - TriplyDB

Structural characterization of the ectodomain of a disintegrin and metalloproteinase-22 (ADAM22), a neural adhesion receptor instead of metalloproteinase: insights on ADAM function

Structural characterization of the ectodomain of a disintegrin and metalloproteinase-22 (ADAM22), a neural adhesion receptor instead of metalloproteinase: insights on ADAM function

http://www.wikidata.org/entity/Q37431248

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ADAM and ADAMTS Family Proteins and Snake Venom Metalloproteinases: A Structural Overview A Disintegrin and Metalloprotease (ADAM): Historical Overview of Their Functions Dysfunctional ADAM22 implicated in progressive encephalopathy with cortical atrophy and epilepsy Phenotypic diversity of breast cancer-related mutations in metalloproteinase-disintegrin ADAM12 Loss of zebrafish lgi1b leads to hydrocephalus and sensitization to pentylenetetrazol induced seizure-like behavior.Cross-domain inhibition of TACE ectodomain N-glycosylation regulates ADAM8 processing and activation Evidence for restricted reactivity of ADAMDEC1 with protein substrates and endogenous inhibitors.Secretion-Positive LGI1 Mutations Linked to Lateral Temporal Epilepsy Impair Binding to ADAM22 and ADAM23 Receptors Enzymatic toxins from snake venom: structural characterization and mechanism of catalysis.ADAM-15 disintegrin-like domain structure and function.Extracellular metalloproteinases in neural crest development and craniofacial morphogenesis.Novel Catalytically-Inactive PII Metalloproteinases from a Viperid Snake Venom with Substitutions in the Canonical Zinc-Binding Motif.Molecular basis for the mechanism of action of an anti-TACE antibody.Structural Basis for Regulated Proteolysis by the α-Secretase ADAM10.Multiple non-catalytic ADAMs are novel integrin α4 ligands.Structural basis of epilepsy-related ligand-receptor complex LGI1-ADAM22.ADAMs and protein disulfide isomerase: the key to regulated cell-surface protein ectodomain shedding?: Figure 1

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Structural characterization of the ectodomain of a disintegrin and metalloproteinase-22 (ADAM22), a neural adhesion receptor instead of metalloproteinase: insights on ADAM function

http://www.wikidata.org/entity/Q37431248

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article científic

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bilimsel makale

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scientific article published on 18 August 2009

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JBC.M109.014258

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Journal of Biological Chemistry

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Ann H R Shim

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Heli Liu

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Xiaolin He

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P2860

Ataxia and peripheral nerve hypomyelination in ADAM22-deficient mice

Crystal structures of the two major aggrecan degrading enzymes, ADAMTS4 and ADAMTS5

Crystal structure of the catalytic domain of human tumor necrosis factor-alpha-converting enzyme

MolProbity: all-atom contacts and structure validation for proteins and nucleic acids

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Processing of X-ray diffraction data collected in oscillation mode

Crystal structure of the catalytic domain of human ADAM33

Crystal structures of catrocollastatin/VAP2B reveal a dynamic, modular architecture of ADAM/adamalysin/reprolysin family proteins

Crystal structures of human ADAMTS-1 reveal a conserved catalytic domain and a disintegrin-like domain with a fold homologous to cysteine-rich domains

High resolution crystal structure of the catalytic domain of ADAMTS-5 (aggrecanase-2)

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