Substrates of the prostate-specific serine protease prostase/KLK4 defined by positional-scanning peptide libraries.
about
Expression and functional characterization of the cancer-related serine protease, human tissue kallikrein 14Specificity profiling of seven human tissue kallikreins reveals individual subsite preferencesHuman tissue kallikrein 5 is a member of a proteolytic cascade pathway involved in seminal clot liquefaction and potentially in prostate cancer progressionHypomaturation enamel defects in Klk4 knockout/LacZ knockin miceKallikrein-related peptidase-4 (KLK4): role in enamel formation and revelations from ablated miceDental enamel development: proteinases and their enamel matrix substratesMastering the canonical loop of serine protease inhibitors: enhancing potency by optimising the internal hydrogen bond networkHepatocyte growth factor is a preferred in vitro substrate for human hepsin, a membrane-anchored serine protease implicated in prostate and ovarian cancersDefining the extended substrate specificity of kallikrein 1-related peptidases.Using specificity to strategically target proteases.Natural and synthetic inhibitors of kallikrein-related peptidases (KLKs).Enzymatic properties of human kallikrein-related peptidase 12 (KLK12).Enzymatic triggered release of an HIV-1 entry inhibitor from prostate specific antigen degradable microparticles.The androgen-regulated protease TMPRSS2 activates a proteolytic cascade involving components of the tumor microenvironment and promotes prostate cancer metastasis.Clinical significance of kallikrein-related peptidase-4 in oral cancerThe kallikrein world: an update on the human tissue kallikreins.Recombinant kallikrein expression: site-specific integration for hK6 production in human cells.The role of kallikrein-related peptidases in prostate cancer: potential involvement in an epithelial to mesenchymal transition.Kallikreins - The melting pot of activity and functionEpithelial-mesenchymal transition in prostate cancer and the potential role of kallikrein serine proteases.Functions of KLK4 and MMP-20 in dental enamel formationProstatic trypsin-like kallikrein-related peptidases (KLKs) and other prostate-expressed tryptic proteinases as regulators of signalling via proteinase-activated receptors (PARs).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.Metastasis of ovarian cancer is mediated by kallikrein related peptidases.Prognostic value and biological role of the kallikrein-related peptidases in human malignancies.Natural and engineered kallikrein inhibitors: an emerging pharmacopoeia.Proteomic and other analyses to determine the functional consequences of deregulated kallikrein-related peptidase (KLK) expression in prostate and ovarian cancer.Targeting kallikrein-related peptidases in prostate cancer.Unleashing the therapeutic potential of human kallikrein-related serine proteases.Kallikrein-related peptidase 4 induces cancer-associated fibroblast features in prostate-derived stromal cellsKallikrein-related peptidases (KLKs) and the hallmarks of cancer.Novel Biological Substrates of Human Kallikrein 7 Identified through Degradomics.Kallikrein-Related Peptidases in Prostate Cancer: From Molecular Function to Clinical ApplicationSecretome and degradome profiling shows that Kallikrein-related peptidases 4, 5, 6, and 7 induce TGFβ-1 signaling in ovarian cancer cells.Kallikrein-related peptidase 4 gene (KLK4) in prostate tumors: quantitative expression analysis and evaluation of its clinical significance.Quantification of Human Kallikrein-Related Peptidases in Biological Fluids by Multiplatform Targeted Mass Spectrometry Assays.Kallikrein-related peptidase 4 (KLK4) initiates intracellular signaling via protease-activated receptors (PARs). KLK4 and PAR-2 are co-expressed during prostate cancer progression.Interplay of human tissue kallikrein 4 (hK4) with the plasminogen activation system: hK4 regulates the structure and functions of the urokinase-type plasminogen activator receptor (uPAR).Mass spectrometry based proteomics analyses in kallikrein-related peptidase research: implications for cancer research and therapy.
P2860
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P2860
Substrates of the prostate-specific serine protease prostase/KLK4 defined by positional-scanning peptide libraries.
description
2005 nî lūn-bûn
@nan
2005 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Substrates of the prostate-spe ...... al-scanning peptide libraries.
@ast
Substrates of the prostate-spe ...... al-scanning peptide libraries.
@en
type
label
Substrates of the prostate-spe ...... al-scanning peptide libraries.
@ast
Substrates of the prostate-spe ...... al-scanning peptide libraries.
@en
prefLabel
Substrates of the prostate-spe ...... al-scanning peptide libraries.
@ast
Substrates of the prostate-spe ...... al-scanning peptide libraries.
@en
P2093
P356
P1433
P1476
Substrates of the prostate-spe ...... al-scanning peptide libraries.
@en
P2093
Ami S Bhatt
Charles S Craik
Dennis Andress
Masazumi Matsumura
Nigel Clegg
Peter S Nelson
Thomas K Takayama
P2860
P356
10.1002/PROS.20101
P577
2005-01-01T00:00:00Z