Anthony Martonosi
State University of New York System
70 Papers
1.7K Citations
Anthony Martonosi is an academic researcher from State University of New York System. The author has contributed to research in topics: Endoplasmic reticulum & Calcium ATPase. The author has an hindex of 31, co-authored 70 publications. Previous affiliations of Anthony Martonosi include State University of New York Upstate Medical University.
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Papers
Crystallization of intramembrane particles in rabbit sarcoplasmic reticulum vesicles by vanadate.
TL;DR: The data suggest that vanadate induces a conformational change in the Ca2+-transport ATPase, with crystallization of the intramembrane particles.
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Ca2+ release from caged-Ca2+ alters the FTIR spectrum of sarcoplasmic reticulum.
TL;DR: Light-induced Ca2+ release from theCa2+ complex of Nitr-5 altered the FTIR spectra of sarcoplasmic reticulum vesicles and purified Ca(2+)-ATPase preparations, suggesting that changes in side chain vibrations, although some changes in secondary structures may also contribute.
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•Journal Article
Structure of Ca2+-ATPase in sarcoplasmic reticulum.
Anthony Martonosi,László Dux,Kenneth A. Taylor,H.P. Ting-Beall,S Varga,P. Csermely,N Mullner,Sandor Papp,Istvan Jona +8 more
TL;DR: In this paper, the morphology of sarcoplasmic reticulum, classification of Ca(2+)-ATPase (SERCA) isoenzymes presented in this membrane system, as well as their topology is reviewed.
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The regulation of ATPase-ATPase interactions in sarcoplasmic reticulum membrane. II. The influence of membrane potential.
László Dux,Anthony Martonosi +1 more
TL;DR: Changes in enzyme conformation caused by potential changes during the contraction-relaxation cycle could regulate ATPase interactions in a similar manner in vivo, with effects upon the Ca2+ transport activity and permeability of the sarcoplasmic reticulum.
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Conformational responses of the tryptic cleavage products of the Ca2+-ATPase of sarcoplasmic reticulum.
TL;DR: Vanadate protected the A and B fragments from further hydrolysis and preserved the ability of the cleaved Ca2-ATPase to form crystals and to show the characteristic conformational changes in response to Ca2+ and EGTA that are observed with the intact enzyme.
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