Zobrazeno 1 - 10
of 142
pro vyhledávání: '"J. H. Exton"'
Autor:
J H Exton
Publikováno v:
Annual Review of Pharmacology and Toxicology. 36:481-509
The actions of many hormones, neurotransmitters, and growth factors are mediated by the hydrolysis of phosphatidylinositol 4,5-bisphosphate catalyzed by specific isozymes of phospholipase C. This hydrolysis releases inositol 1,4,5-trisphosphate, whic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a1bbc99dc08eb9bf6958eae53fa37594
https://doi.org/10.1146/annurev.pa.36.040196.002405
https://doi.org/10.1146/annurev.pa.36.040196.002405
Autor:
J H, Exton
Publikováno v:
Reviews of physiology, biochemistry and pharmacology. 144
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::40313cd5266940c2e267045191fbdf87
https://pubmed.ncbi.nlm.nih.gov/11987824
https://pubmed.ncbi.nlm.nih.gov/11987824
Conserved amino acids at the C-terminus of rat phospholipase D1 are essential for enzymatic activity
Publikováno v:
European journal of biochemistry. 267(24)
Rat brain phospholipase D1 (rPLD1) has two highly conserved motifs [H(X)K(X)4D, denoted HKD] located at the N-terminal and C-terminal halves, which are required for activity. Association of the two halves is essential for rPLD1 activity, which probab
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::d9ae3d2c68133ff17530385182fefdb6
https://pubmed.ncbi.nlm.nih.gov/11106425
https://pubmed.ncbi.nlm.nih.gov/11106425
Publikováno v:
The Journal of biological chemistry. 275(32)
Rat brain phospholipase D1 (rPLD1) belongs to a superfamily defined by the highly conserved catalytic motif (H(X)K(X)(4)D, denoted HKD. rPLD1 contains two HKD domains, located in the N- and C-terminal regions. The integrity of the two HKD domains is
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::0e410f92d9ecebf21e3a5603471cf195
https://pubmed.ncbi.nlm.nih.gov/10825182
https://pubmed.ncbi.nlm.nih.gov/10825182
Autor:
J. H. Exton
Publikováno v:
Principles of Molecular Regulation ISBN: 9781617371042
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fe3401d323ff7b31aec199117d7e5246
https://doi.org/10.1007/978-1-59259-032-2_13
https://doi.org/10.1007/978-1-59259-032-2_13
Autor:
J H, Exton
Publikováno v:
Advances in experimental medicine and biology.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::382bafd9aa2c3e662fe52bb4b2a5aeb0
https://pubmed.ncbi.nlm.nih.gov/9547530
https://pubmed.ncbi.nlm.nih.gov/9547530
Publikováno v:
The Journal of biological chemistry. 271(22)
Small GTP-binding proteins of the Rho family are implicated in the in vitro regulation of phosphatidylcholine hydrolysis by phospholipase D (PLD). However, their role in agonist-stimulated PLD activity in whole cells is not clear. The ribosyltransfer
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::53ea8513cb73a590de875d3f2b9c988b
https://pubmed.ncbi.nlm.nih.gov/8662844
https://pubmed.ncbi.nlm.nih.gov/8662844
Publikováno v:
The Journal of biological chemistry. 270(15)
Phospholipase D (PLD) activity that was stimulated by guanosine 5'-O-(3-thiotriphosphate) (GTP gamma S) was detected in cytosol and membranes of HL60 cells. GTP gamma S-stimulated PLD activity was detected in the membranes when exogenous labeled phos
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::e763e99b19fe5d4d86e723f51cb8b86d
https://pubmed.ncbi.nlm.nih.gov/7721742
https://pubmed.ncbi.nlm.nih.gov/7721742
Publikováno v:
The Journal of biological chemistry. 269(45)
Platelet-derived growth factor (PDGF) stimulates phosphatidylcholine hydrolysis via phospholipase D (PLD) in several tissues. To determine whether PLD activation is dependent on phosphoinositide hydrolysis by phospholipase C (PLC), we measured the fo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::5e016260d921e6abdae1dcb0fe7cd29c
https://pubmed.ncbi.nlm.nih.gov/7961710
https://pubmed.ncbi.nlm.nih.gov/7961710