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Proteinase-activated receptors, targets for kallikrein signaling
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scholarly article
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title
Proteinase-activated receptors, targets for kallikrein signaling
(English)
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main subject
Kallikrein related peptidase 6
1 reference
stated in
GOA release 2020-03-11
Kallikrein related peptidase 14
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stated in
GOA release 2020-03-11
Kallikrein related peptidase 5
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stated in
GOA release 2020-03-11
positive regulation of G protein-coupled receptor signaling pathway
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stated in
GOA release 2020-03-11
author
Eleftherios P. Diamandis
series ordinal
11
object named as
Eleftherios P Diamandis
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Michael Blaber
object named as
Michael Blaber
series ordinal
5
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author name string
Katerina Oikonomopoulou
series ordinal
1
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Kristina K Hansen
series ordinal
2
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Mahmoud Saifeddine
series ordinal
3
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Illa Tea
series ordinal
4
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Sachiko I Blaber
series ordinal
6
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Isobel Scarisbrick
series ordinal
7
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Patricia Andrade-Gordon
series ordinal
8
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Graeme S Cottrell
series ordinal
9
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Nigel W Bunnett
series ordinal
10
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Morley D Hollenberg
series ordinal
12
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language of work or name
English
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publication date
27 October 2006
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published in
Journal of Biological Chemistry
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volume
281
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issue
43
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page(s)
32095-112
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cites work
Prostatic kallikrein hK2, but not prostate-specific antigen (hK3), activates single-chain urokinase-type plasminogen activator
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Organization and evolution of the glandular kallikrein locus in Mus musculus
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Characterization of the enzymatic activity of human kallikrein 6: Autoactivation, substrate specificity, and regulation by inhibitors
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Role of kallikrein enzymes in the central nervous system
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Human kallikrein 6 (zyme/protease M/neurosin): a new serum biomarker of ovarian carcinoma
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The role of the C-terminal tail in protease-activated receptor-2-mediated Ca2+ signalling, proline-rich tyrosine kinase-2 activation, and mitogen-activated protein kinase activity.
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Plasmin Desensitization of the PAR1 Thrombin Receptor: Kinetics, Sites of Truncation, and Implications for Thrombolytic Therapy†
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The emerging roles of human tissue kallikreins in cancer
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The power and promise of population genomics: from genotyping to genome typing
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Glycosylation and the activation of proteinase-activated receptor 2 (PAR(2)) by human mast cell tryptase
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Modulation of visceral pain and inflammation by protease-activated receptors
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Proteinase-activated receptor-4: evaluation of tethered ligand-derived peptides as probes for receptor function and as inflammatory agonists in vivo
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Protease activated receptors: theme and variations
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Glycosylation of human proteinase-activated receptor-2 (hPAR2): role in cell surface expression and signalling
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Expression and localization of tissue kallikrein mRNAs in human epidermis and appendages
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Specificity of coagulation factor signaling
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Proteinase-activated receptors 1 and 4 counter-regulate endostatin and VEGF release from human platelets
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Molecular cloning of a potential proteinase activated receptor
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Evidence for the presence of a protease-activated receptor distinct from the thrombin receptor in human keratinocytes
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Endothelial cell thrombin receptors and PAR-2. Two protease-activated receptors located in a single cellular environment
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Interactions of mast cell tryptase with thrombin receptors and PAR-2.
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A polymorphic protease-activated receptor 2 (PAR2) displaying reduced sensitivity to trypsin and differential responses to PAR agonists
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Modified proteinase-activated receptor-1 and -2 derived peptides inhibit proteinase-activated receptor-2 activation by trypsin
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1 reference
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Crossref
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Enzymatic profiling of human kallikrein 14 using phage-display substrate technology
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Up-regulation and Activation of Proteinase-Activated Receptor 2 in Early and Delayed Radiation Injury in the Rat Intestine: Influence of Biological Activators of Proteinase-Activated Receptor 2
1 reference
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7 January 2021
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Characterization of thrombin-induced leukocyte rolling and adherence: a potential proinflammatory role for proteinase-activated receptor-4
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1074%2FJBC.M513138200
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
Identifiers
DOI
10.1074/JBC.M513138200
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4237252
OpenCitations bibliographic resource ID
4237252
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4237252
PubMed publication ID
16885167
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4237252
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