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Expression and mutagenesis of the catalytic domain of cGMP-inhibited phosphodiesterase (PDE3) cloned from human platelets
scientific journal article
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scholarly article
1 reference
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PubMed
PubMed ID
9173884
retrieved
4 January 2017
title
Expression and mutagenesis of the catalytic domain of cGMP-inhibited phosphodiesterase (PDE3) cloned from human platelets
(English)
1 reference
stated in
PubMed
PubMed ID
9173884
retrieved
4 January 2017
main subject
Phosphodiesterase 3A
1 reference
stated in
GOA release 2020-03-11
cGMP-inhibited cyclic-nucleotide phosphodiesterase activity
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stated in
GOA release 2020-03-11
author name string
K. M. Tang
series ordinal
1
1 reference
stated in
PubMed
PubMed ID
9173884
retrieved
4 January 2017
E. K. Jang
series ordinal
2
1 reference
stated in
PubMed
PubMed ID
9173884
retrieved
4 January 2017
R. J. Haslam
series ordinal
3
1 reference
stated in
PubMed
PubMed ID
9173884
retrieved
4 January 2017
language of work or name
English
0 references
publication date
1 April 1997
1 reference
stated in
PubMed
PubMed ID
9173884
retrieved
4 January 2017
published in
Biochemical Journal
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stated in
PubMed
PubMed ID
9173884
retrieved
4 January 2017
volume
323 ( Pt 1)
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stated in
PubMed
PubMed ID
9173884
retrieved
4 January 2017
page(s)
217–224
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stated in
PubMed
PubMed ID
9173884
retrieved
4 January 2017
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Characterization of two recombinant PDE3 (cGMP-inhibited cyclic nucleotide phosphodiesterase) isoforms, RcGIP1 and HcGIP2, expressed in NIH 3006 murine fibroblasts and Sf9 insect cells
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Molecular cloning of the rat adipocyte hormone-sensitive cyclic GMP-inhibited cyclic nucleotide phosphodiesterase
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Immunological identification of the major platelet low-Km cAMP phosphodiesterase: probable target for anti-thrombotic agents
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Platelet activation.
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Inhibitors of cyclic AMP phosphodiesterase. 3. Synthesis and biological evaluation of pyrido and imidazolyl analogues of 1,2,3,5-tetrahydro-2-oxoimidazo[2,1-b]quinazoline
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Preparation of suspensions of washed platelets from humans.
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A potent and selective inhibitor of cyclic AMP phosphodiesterase with potential cardiotonic and antithrombotic properties
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Purification and characterization of a cyclic GMP-stimulated cyclic nucleotide phosphodiesterase from the cytosol of human platelets
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A new cGMP phosphodiesterase isolated from bovine platelets is substrate for cAMP- and cGMP-dependent protein kinases: evidence for a key role in the process of platelet activation
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Purification and characterization of a human platelet cyclic nucleotide phosphodiesterase
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Platelet cGMP-binding phosphodiesterase
1 reference
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PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/9173884
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Molecular basis of the synergistic inhibition of platelet function by nitrovasodilators and activators of adenylate cyclase: inhibition of cyclic AMP breakdown by cyclic GMP
1 reference
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PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/9173884
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12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Two isoforms of cGMP-inhibited cyclic nucleotide phosphodiesterases in human tissues distinguished by their responses to vesnarinone, a new cardiotonic agent
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/9173884
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Cytosolic and sarcoplasmic reticulum-associated low Km, cGMP-inhibited cAMP phosphodiesterase in mammalian myocardium
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/9173884
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Single-step affinity purification, partial structure and properties of human platelet cGMP inhibited cAMP phosphodiesterase
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/9173884
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1042/BJ3230217
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4793314
OpenCitations bibliographic resource ID
4793314
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4793314
PMCID
1218297
0 references
PubMed ID
9173884
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4793314
ResearchGate publication ID
14044663
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