Review
. 1992 Nov 30:671:32-47; discussion 48.
doi: 10.1111/j.1749-6632.1992.tb43782.x.
Long-range intramolecular linked functions in activation and inhibition of SERCA ATPases
Affiliations
- PMID: 1288328
- DOI: 10.1111/j.1749-6632.1992.tb43782.x
Item in Clipboard
Review
Long-range intramolecular linked functions in activation and inhibition of SERCA ATPases
Ann N Y Acad Sci.
.
No abstract available
Similar articles
-
Thapsigargin: potent inhibitor of Ca2+ transport ATP-ases of endoplasmic and sarcoplasmic reticulum.Acta Biochim Pol. 1993;40(3):309-19. Acta Biochim Pol. 1993. PMID: 8249487 Review. No abstract available.
-
Total synthesis of two novel subpicomolar sarco/endoplasmatic reticulum Ca2+-ATPase inhibitors designed by an analysis of the binding site of thapsigargin.J Med Chem. 2005 Nov 3;48(22):7005-11. doi: 10.1021/jm058036v. J Med Chem. 2005. PMID: 16250659
-
Thapsigargin, a high affinity and global inhibitor of intracellular Ca2+ transport ATPases.Arch Biochem Biophys. 1992 Nov 1;298(2):313-7. doi: 10.1016/0003-9861(92)90416-t. Arch Biochem Biophys. 1992. PMID: 1416963 Review. No abstract available.
-
Thapsigargin inhibits the sarcoplasmic or endoplasmic reticulum Ca-ATPase family of calcium pumps.J Biol Chem. 1991 Sep 15;266(26):17067-71. J Biol Chem. 1991. PMID: 1832668
-
Ca2+ transport by the sarcoplasmic reticulum ATPase.Biochim Biophys Acta. 1997 Jan 16;1318(1-2):52-70. doi: 10.1016/s0005-2728(96)00132-6. Biochim Biophys Acta. 1997. PMID: 9030255 Review. No abstract available.
Cited by
-
The functional importance of the extreme C-terminal tail in the gene 2 organellar Ca(2+)-transport ATPase (SERCA2a/b).Biochem J. 1994 Nov 1;303 ( Pt 3)(Pt 3):979-84. doi: 10.1042/bj3030979. Biochem J. 1994. PMID: 7980471 Free PMC article.
-
Inhibition of L-type calcium-channel activity by thapsigargin and 2,5-t-butylhydroquinone, but not by cyclopiazonic acid.Biochem J. 1994 Aug 15;302 ( Pt 1)(Pt 1):147-54. doi: 10.1042/bj3020147. Biochem J. 1994. PMID: 7520693 Free PMC article.
-
Lys515-Lys492 cross-linking by DIDS interferes with substrate utilization by the sarcoplasmic reticulum ATPase.Biophys J. 1997 Oct;73(4):2149-55. doi: 10.1016/S0006-3495(97)78245-6. Biophys J. 1997. PMID: 9336210 Free PMC article.
-
Characterization of calcium, nucleotide, phosphate, and vanadate bound states by derivatization of sarcoplasmic reticulum ATPase with ThioGlo1.Biophys J. 1999 Oct;77(4):2217-25. doi: 10.1016/S0006-3495(99)77062-1. Biophys J. 1999. PMID: 10512841 Free PMC article.
-
Trinitrophenyl derivatives bind differently from parent adenine nucleotides to Ca2+-ATPase in the absence of Ca2+.Proc Natl Acad Sci U S A. 2011 Feb 1;108(5):1833-8. doi: 10.1073/pnas.1017659108. Epub 2011 Jan 14. Proc Natl Acad Sci U S A. 2011. PMID: 21239683 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
