Proteomic analyses reveal an acidic prime side specificity for the astacin metalloprotease family reflected by physiological substrates - Wikidata - wikimedia - TriplyDB

Proteomic analyses reveal an acidic prime side specificity for the astacin metalloprotease family reflected by physiological substrates

Proteomic analyses reveal an acidic prime side specificity for the astacin metalloprotease family reflected by physiological substrates

http://www.wikidata.org/entity/Q35264713

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Genetic Background is a Key Determinant of Glomerular Extracellular Matrix Composition and Organization Evaluation of ¹¹¹in-labelled exendin-4 derivatives containing different meprin β-specific cleavable linkers Functional decorations: post-translational modifications and heart disease delineated by targeted proteomics.Proteomic protease specificity profiling of clostridial collagenases reveals their intrinsic nature as dedicated degraders of collagen.UVB-induced gene expression in the skin of Xiphophorus maculatus Jp 163 B.Enhanced activity of meprin-α, a pro-migratory and pro-angiogenic protease, in colorectal cancer.Microbial-induced meprin β cleavage in MUC2 mucin and a functional CFTR channel are required to release anchored small intestinal mucus.Urinary signatures of Renal Cell Carcinoma investigated by peptidomic approaches.Cleavage specificity analysis of six type II transmembrane serine proteases (TTSPs) using PICS with proteome-derived peptide libraries Biochemical characterization and N-terminomics analysis of leukolysin, the membrane-type 6 matrix metalloprotease (MMP25): chemokine and vimentin cleavages enhance cell migration and macrophage phagocytic activities.Development of high throughput screening assays and pilot screen for inhibitors of metalloproteases meprin α and β.Metalloproteinases in Drosophila to humans that are central players in developmental processes.Origin and Diversification of Meprin Proteases.Identification of Protease Specificity by Combining Proteome-Derived Peptide Libraries and Quantitative Proteomics Meprinα transactivates the epidermal growth factor receptor (EGFR) via ligand shedding, thereby enhancing colorectal cancer cell proliferation and migration SheddomeDB: the ectodomain shedding database for membrane-bound shed markers.A Single Glycan at the 99-Loop of Human Kallikrein-related Peptidase 2 Regulates Activation and Enzymatic Activity.The substrate degradome of meprin metalloproteases reveals an unexpected proteolytic link between meprin β and ADAM10.The metalloproteases meprin α and meprin β: unique enzymes in inflammation, neurodegeneration, cancer and fibrosis.Active site specificity profiling datasets of matrix metalloproteinases (MMPs) 1, 2, 3, 7, 8, 9, 12, 13 and 14.Metalloproteases meprin α and meprin β are C- and N-procollagen proteinases important for collagen assembly and tensile strength Global cellular response to chemotherapy-induced apoptosis.Identification and function of proteolysis regulators in seminal fluid.Meprin metalloproteases inactivate interleukin 6.Meprin Metalloproteases Generate Biologically Active Soluble Interleukin-6 Receptor to Induce Trans-Signaling.Mass spectrometry-based proteomics strategies for protease cleavage site identification.Proteomic identification of protease cleavage sites: cell-biological and biomedical applications.Mapping orphan proteases by proteomics: meprin metalloproteases deciphered as potential therapeutic targets.Proteomic and other analyses to determine the functional consequences of deregulated kallikrein-related peptidase (KLK) expression in prostate and ovarian cancer.Proteases and proteomics: cutting to the core of human skin pathologies.A Strong Neutrophil Elastase Proteolytic Fingerprint Marks the Carcinoma Tumor Proteome.Peptidase specificity from the substrate cleavage collection in the MEROPS database and a tool to measure cleavage site conservation.Generation of aggregation prone N-terminally truncated amyloid β peptides by meprin β depends on the sequence specificity at the cleavage site.Handling Metalloproteinases.Novel Biological Substrates of Human Kallikrein 7 Identified through Degradomics.The Metalloprotease Meprin β Is an Alternative β-Secretase of APP.Sharpening Host Defenses during Infection: Proteases Cut to the Chase.Cancer-associated mutations in the canonical cleavage site do not influence CD99 shedding by the metalloprotease meprin β but alter cell migration in vitro.Sizzled is unique among secreted frizzled-related proteins for its ability to specifically inhibit bone morphogenetic protein-1 (BMP-1)/tolloid-like proteinases.The metalloprotease meprin β generates amino terminal-truncated amyloid β peptide species.

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P2860

Proteomic analyses reveal an acidic prime side specificity for the astacin metalloprotease family reflected by physiological substrates

http://www.wikidata.org/entity/Q35264713

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2011 nî lūn-bûn

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2011 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2011 թվականի հունիսին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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Molecular & Cellular Proteomics

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Proteomic analyses reveal an a ...... ed by physiological substrates

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André Schütte

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Anke Ohler

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Christoph Becker-Pauly

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Claudia Broder

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Oliver Schilling

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Olivier Barré

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Reinhild Kappelhoff

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Ulrich Auf dem Keller

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Walter Stöcker

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P2860

The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools

Identification and characterization of human and mouse ovastacin: a novel metalloproteinase similar to hatching enzymes from arthropods, birds, amphibians, and fish

Human recombinant endopeptidase PHEX has a strict S1' specificity for acidic residues and cleaves peptides derived from fibroblast growth factor-23 and matrix extracellular phosphoglycoprotein

The SWISS-MODEL Repository of annotated three-dimensional protein structure homology models

MEROPS: the peptidase database

Meprins, membrane-bound and secreted astacin metalloproteinases

MolProbity: all-atom structure validation for macromolecular crystallography

The astacin family of metalloendopeptidases

MrBayes 3: Bayesian phylogenetic inference under mixed models

Structure of astacin and implications for activation of astacins and zinc-ligation of collagenases

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M111.009233

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10.1074/MCP.M111.009233

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9

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10

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Christopher Overall

Christoph Becker-Pauly

Walter Stöcker

Ulrich auf dem Keller

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2011-06-21T00:00:00Z

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21693781

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3186203

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