Proteomic analyses reveal an acidic prime side specificity for the astacin metalloprotease family reflected by physiological substrates
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Genetic Background is a Key Determinant of Glomerular Extracellular Matrix Composition and OrganizationEvaluation of ¹¹¹in-labelled exendin-4 derivatives containing different meprin β-specific cleavable linkersFunctional 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 librariesBiochemical 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 ProteomicsMeprinα transactivates the epidermal growth factor receptor (EGFR) via ligand shedding, thereby enhancing colorectal cancer cell proliferation and migrationSheddomeDB: 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 strengthGlobal 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.
P2860
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P2860
Proteomic analyses reveal an acidic prime side specificity for the astacin metalloprotease family reflected by physiological substrates
description
2011 nî lūn-bûn
@nan
2011 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Proteomic analyses reveal an a ...... ed by physiological substrates
@ast
Proteomic analyses reveal an a ...... ed by physiological substrates
@en
type
label
Proteomic analyses reveal an a ...... ed by physiological substrates
@ast
Proteomic analyses reveal an a ...... ed by physiological substrates
@en
prefLabel
Proteomic analyses reveal an a ...... ed by physiological substrates
@ast
Proteomic analyses reveal an a ...... ed by physiological substrates
@en
P2093
P2860
P50
P356
P1476
Proteomic analyses reveal an a ...... ed by physiological substrates
@en
P2093
André Schütte
Anke Ohler
Christoph Becker-Pauly
Claudia Broder
Oliver Schilling
Olivier Barré
Reinhild Kappelhoff
Ulrich Auf dem Keller
Walter Stöcker
P2860
P304
M111.009233
P356
10.1074/MCP.M111.009233
P577
2011-06-21T00:00:00Z