FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W1969842022> ?p ?o ?g. }

• W1969842022 endingPage "1801" @default.
• W1969842022 startingPage "1791" @default.
• W1969842022 abstract "Oxidation of either Met(145) or Met(146) in wheat germ calmodulin (CaM) to methionine sulfoxide prevents the CaM-dependent activation of the plasma membrane (PM) Ca-ATPase (D. Yin, K. Kuczera, and T. C. Squier, 2000, Chem. Res. Toxicol. 13:103-110). To investigate the structural basis for the inhibition of the PM-Ca-ATPase by oxidized CaM (CaM(ox)), we have used circular dichroism (CD) and fluorescence spectroscopy to resolve conformational differences within the complex between CaM and the PM-Ca-ATPase. The similar excited-state lifetime and solvent accessibility of the fluorophore N-1-pyrenyl-maleimide covalently bound to Cys(26) in unoxidized CaM and CaM(ox) indicates that the globular domains within CaM(ox) assume a native-like structure following association with the PM-Ca-ATPase. However, in comparison with oxidized CaM there are increases in the 1) molar ellipticity in the CD spectrum and 2) conformational heterogeneity between the opposing globular domains for CaM(ox) bound to the CaM-binding sequence of the PM-Ca-ATPase. Furthermore, CaM(ox) binds to the PM-Ca-ATPase with high affinity at a distinct, but overlapping, site to that normally occupied by unoxidized CaM. These results suggest that alterations in binding interactions between CaM(ox) and the PM-Ca-ATPase block important structural transitions within the CaM-binding sequence of the PM-Ca-ATPase that are normally associated with enzyme activation." @default.
• W1969842022 created "2016-06-24" @default.
• W1969842022 creator A5011954542 @default.
• W1969842022 creator A5023637844 @default.
• W1969842022 creator A5034507169 @default.
• W1969842022 date "2001-04-01" @default.
• W1969842022 modified "2023-09-25" @default.
• W1969842022 title "Oxidatively Modified Calmodulin Binds to the Plasma Membrane Ca-ATPase in a Nonproductive and Conformationally Disordered Complex" @default.
• W1969842022 cites W1482593432 @default.
• W1969842022 cites W1487437286 @default.
• W1969842022 cites W1494998770 @default.
• W1969842022 cites W1497338818 @default.
• W1969842022 cites W1506043065 @default.
• W1969842022 cites W1520560572 @default.
• W1969842022 cites W1535540228 @default.
• W1969842022 cites W1553039892 @default.
• W1969842022 cites W1572268730 @default.
• W1969842022 cites W1911339081 @default.
• W1969842022 cites W1963577254 @default.
• W1969842022 cites W1968901680 @default.
• W1969842022 cites W1969163423 @default.
• W1969842022 cites W1974682436 @default.
• W1969842022 cites W1975597921 @default.
• W1969842022 cites W1978042266 @default.
• W1969842022 cites W1980971338 @default.
• W1969842022 cites W1982647833 @default.
• W1969842022 cites W1985802835 @default.
• W1969842022 cites W1987159249 @default.
• W1969842022 cites W1993432598 @default.
• W1969842022 cites W1996042616 @default.
• W1969842022 cites W1997321300 @default.
• W1969842022 cites W1997870466 @default.
• W1969842022 cites W1998763047 @default.
• W1969842022 cites W2001535102 @default.
• W1969842022 cites W2007629902 @default.
• W1969842022 cites W2009304738 @default.
• W1969842022 cites W2011179412 @default.
• W1969842022 cites W2011836829 @default.
• W1969842022 cites W2012088552 @default.
• W1969842022 cites W2012206465 @default.
• W1969842022 cites W2012704789 @default.
• W1969842022 cites W2012710118 @default.
• W1969842022 cites W2022703044 @default.
• W1969842022 cites W2024142216 @default.
• W1969842022 cites W2025488831 @default.
• W1969842022 cites W2025679060 @default.
• W1969842022 cites W2027270341 @default.
• W1969842022 cites W2031683219 @default.
• W1969842022 cites W2031811477 @default.
• W1969842022 cites W2033212918 @default.
• W1969842022 cites W2033604459 @default.
• W1969842022 cites W2037116841 @default.
• W1969842022 cites W2037300064 @default.
• W1969842022 cites W2039042657 @default.
• W1969842022 cites W2041115411 @default.
• W1969842022 cites W2042675658 @default.
• W1969842022 cites W2045099525 @default.
• W1969842022 cites W2045860840 @default.
• W1969842022 cites W2046761749 @default.
• W1969842022 cites W2052366943 @default.
• W1969842022 cites W2057347947 @default.
• W1969842022 cites W2057704439 @default.
• W1969842022 cites W2060714866 @default.
• W1969842022 cites W2063963320 @default.
• W1969842022 cites W2067546080 @default.
• W1969842022 cites W2068615039 @default.
• W1969842022 cites W2070746053 @default.
• W1969842022 cites W2075691686 @default.
• W1969842022 cites W2076510866 @default.
• W1969842022 cites W2085444999 @default.
• W1969842022 cites W2092551351 @default.
• W1969842022 cites W2093929400 @default.
• W1969842022 cites W2107919301 @default.
• W1969842022 cites W2115612202 @default.
• W1969842022 cites W2141378441 @default.
• W1969842022 cites W2155240101 @default.
• W1969842022 cites W2167135214 @default.
• W1969842022 cites W2172712627 @default.
• W1969842022 cites W2200436717 @default.
• W1969842022 cites W2203086356 @default.
• W1969842022 cites W4247441327 @default.
• W1969842022 doi "https://doi.org/10.1016/s0006-3495(01)76149-8" @default.
• W1969842022 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1301368" @default.
• W1969842022 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/11259292" @default.
• W1969842022 hasPublicationYear "2001" @default.
• W1969842022 type Work @default.
• W1969842022 sameAs 1969842022 @default.
• W1969842022 citedByCount "46" @default.
• W1969842022 countsByYear W19698420222012 @default.
• W1969842022 countsByYear W19698420222013 @default.
• W1969842022 countsByYear W19698420222014 @default.
• W1969842022 countsByYear W19698420222015 @default.
• W1969842022 countsByYear W19698420222016 @default.
• W1969842022 countsByYear W19698420222017 @default.
• W1969842022 countsByYear W19698420222018 @default.
• W1969842022 countsByYear W19698420222020 @default.
• W1969842022 countsByYear W19698420222022 @default.
• W1969842022 crossrefType "journal-article" @default.

• next