Specificity profiling of seven human tissue kallikreins reveals individual subsite preferences - Wikidata - awgldk - TriplyDB

Specificity profiling of seven human tissue kallikreins reveals individual subsite preferences

Specificity profiling of seven human tissue kallikreins reveals individual subsite preferences

http://www.wikidata.org/entity/Q28243373

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Chymotryptic specificity determinants in the 1.0 A structure of the zinc-inhibited human tissue kallikrein 7 LEKTI fragments specifically inhibit KLK5, KLK7, and KLK14 and control desquamation through a pH-dependent interaction Vaspin inhibits kallikrein 7 by serpin mechanism Structural basis for the Zn2+ inhibition of the zymogen-like kallikrein-related peptidase 10 Structural determinants of limited proteolysis.Inhibitor fingerprinting of metalloproteases using microplate and microarray platforms: an enabling technology in Catalomics.Defining the extended substrate specificity of kallikrein 1-related peptidases.Guinea pig chymase is leucine-specific: a novel example of functional plasticity in the chymase/granzyme family of serine peptidases Substrate specificity of human kallikreins 1 and 6 determined by phage display.Substrate specificity determination of mouse implantation serine proteinase and human kallikrein-related peptidase 6 by phage display.Hemoglobin cleavage site-specificity of the Plasmodium falciparum cysteine proteases falcipain-2 and falcipain-3.Kallikrein-related peptidase 4: a new activator of the aberrantly expressed protease-activated receptor 1 in colon cancer cells A completed KLK activome profile: investigation of activation profiles of KLK9, 10, and 15 Enzyme-triggered gelation: targeting proteases with internal cleavage sites Proteolytic activity of prostate-specific antigen (PSA) towards protein substrates and effect of peptides stimulating PSA activity Proteolytic activation of prochemerin by kallikrein 7 breaks an ionic linkage and results in C-terminal rearrangement.Natural and synthetic inhibitors of kallikrein-related peptidases (KLKs).Engineering kunitz domain 1 (KD1) of human tissue factor pathway inhibitor-2 to selectively inhibit fibrinolysis: properties of KD1-L17R variant Proteolytic action of kallikrein-related peptidase 7 produces unique active matrix metalloproteinase-9 lacking the C-terminal hemopexin domains Analysis of prostate-specific antigen transcripts in chimpanzees, cynomolgus monkeys, baboons, and African green monkeys.Proteomic analyses reveal an acidic prime side specificity for the astacin metalloprotease family reflected by physiological substrates Molecular insights into substrate specificity of prostate specific antigen through structural modeling Serine Protease Activation Essential for Endothelial-Mesenchymal Transition in Vascular Calcification.Rab31 expression levels modulate tumor-relevant characteristics of breast cancer cells.The substrate degradome of meprin metalloproteases reveals an unexpected proteolytic link between meprin β and ADAM10.Kallikreins - The melting pot of activity and function Activation profiles of human kallikrein-related peptidases by proteases of the thrombostasis axis Reflections on the tissue kallikrein and kallikrein-related peptidase family - from mice to men - what have we learnt in the last two decades?New insights into the functional mechanisms and clinical applications of the kallikrein-related peptidase family.Functional roles of human kallikrein-related peptidases.Functional intersection of the kallikrein-related peptidases (KLKs) and thrombostasis axis.Prostate-specific antigen: an overlooked candidate for the targeted treatment and selective imaging of prostate cancer.Cyclotides as a basis for drug design.Function and clinical relevance of kallikrein-related peptidases and other serine proteases in gynecological cancers.Proteomic and other analyses to determine the functional consequences of deregulated kallikrein-related peptidase (KLK) expression in prostate and ovarian cancer.Unleashing the therapeutic potential of human kallikrein-related serine proteases.Propeptides as modulators of functional activity of proteases.Mass spectrometry-based determination of Kallikrein-related peptidase 7 (KLK7) cleavage preferences and subsite dependency.Novel Biological Substrates of Human Kallikrein 7 Identified through Degradomics.Emerging challenges in the design of selective substrates, inhibitors and activity-based probes for indistinguishable proteases.

P2860

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P2860

Specificity profiling of seven human tissue kallikreins reveals individual subsite preferences

http://www.wikidata.org/entity/Q28243373

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2006 nî lūn-bûn

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2006年論文

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2006年論文

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Specificity profiling of seven ...... individual subsite preferences

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Specificity profiling of seven ...... individual subsite preferences

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Specificity profiling of seven ...... individual subsite preferences

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Charles S Craik

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Friedrich Lottspeich

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Martina Valachova

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Mekdes Debela

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Norman Schechter

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Viktor Magdolen

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Youngchool Choe

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P2860

Molecular cloning and characterization of prostase, an androgen-regulated serine protease with prostate-restricted expression

Purification, molecular cloning, and expression of a human stratum corneum trypsin-like serine protease with possible function in desquamation

Identification and characterization of KLK-L4, a new kallikrein-like gene that appears to be down-regulated in breast cancer tissues

Tissue-specific expression patterns and fine mapping of the human kallikrein (KLK) locus on proximal 19q13.4

Molecular cloning of the human kallikrein 15 gene (KLK15). Up-regulation in prostate cancer

Mutation in kallikrein 4 causes autosomal recessive hypomaturation amelogenesis imperfecta

A proteolytic cascade of kallikreins in the stratum corneum

Crystal structure reveals basis for the inhibitor resistance of human brain trypsin

Crystal structure and biochemical characterization of human kallikrein 6 reveals that a trypsin-like kallikrein is expressed in the central nervous system

Crystal structure of a prostate kallikrein isolated from stallion seminal plasma: a homologue of human PSA

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10.1074/JBC.M602372200

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35

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281

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16740631

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