Zobrazeno 1 - 10
of 272
pro vyhledávání: '"Giuseppe, Inesi"'
Autor:
Giuseppe Inesi
Publikováno v:
Substantia, Vol 3, Iss 1 (2018)
Ca2+ and Cu2+ ATPases are enzyme proteins that utilize ATP for active transport of Ca2+ or Cu2+ across intracellular or cellular membranes.1-4 These enzymes are referred to as P-type ATPases since they utilize ATP through formation of a phosphorylate
Externí odkaz:
https://doaj.org/article/bdb65feb3c2a4356b0572ac6903926b4
Autor:
Giuseppe Inesi
Publikováno v:
IUBMB Life. 69:211-217
Copper has a wide and important role in biological systems, determining conformation and activity of many metalloproteins and enzymes, such as cytochrome oxidase and superoxide dismutase . Furthermore, due to its possible reactivity with nonspecific
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0d33412b7916bc8111a684435e17a797
https://doi.org/10.1002/iub.1590
https://doi.org/10.1002/iub.1590
Publikováno v:
Biochemical Journal
Copper ATPases, in analogy with other members of the P-ATPase superfamily, contain a catalytic headpiece including an aspartate residue reacting with ATP to form a phosphoenzyme intermediate, and transmembrane helices containing cation-binding sites
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::572b6f2b12885b81c43c0cf6c5762e15
http://europepmc.org/articles/PMC4179477
http://europepmc.org/articles/PMC4179477
Publikováno v:
Journal of Cell Communication and Signaling
The Ca(2+) transport ATPase (SERCA) of sarcoplasmic reticulum (SR) plays an important role in muscle cytosolic signaling, as it stores Ca(2+) in intracellular membrane bound compartments, thereby lowering cytosolic Ca(2+) to induce relaxation. The st
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::768396d1a759c2eac154b5b914fb5cc1
https://doi.org/10.1007/s12079-013-0213-7
https://doi.org/10.1007/s12079-013-0213-7
Publikováno v:
Nature. 495:260-264
The X-ray crystal structures of SERCA1a, a Ca2+-ATPase from the sarcoplasmic reticulum, in the presence and absence of sarcolipin are reported; the structures indicate that sarcolipin stabilizes SERCA1a in an ‘open’ state that has not been well c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3f65ef044ab4ee19828066c6556d2006
https://doi.org/10.1038/nature11899
https://doi.org/10.1038/nature11899
Autor:
Giuseppe Inesi, Anand Mohan Prasad
Publikováno v:
American Journal of Physiology-Heart and Circulatory Physiology. 300:H173-H180
Resting intracellular Ca2+can be raised, in neonatal rat cardiac myocytes, by exposure to very low concentration of thapsigargin (TG). Such a Ca2+rise yields calcineurin (CN) activation demonstrated by increased expression of transfected luciferase c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bf7552b42c2827dc6ccf23bf3710f26c
https://doi.org/10.1152/ajpheart.00841.2010
https://doi.org/10.1152/ajpheart.00841.2010
Publikováno v:
Biochemistry
ATP7A and ATP7B are P-type ATPases required for copper homeostasis and involved in the etiology of Menkes and Wilson diseases. We used heterologous expression of ATP7A or ATP7B in COS-1 cells infected with adenovirus vectors to characterize different
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::07aa06761b053f5bcb209796db134c7f
https://doi.org/10.1021/bi101423j
https://doi.org/10.1021/bi101423j
Publikováno v:
Biochemistry
Copper transport ATPases sustain important roles in homeostasis of heavy metals and delivery of copper to metalloenzymes. The copper transport ATPase from Thermotoga maritima (CopA) provides a useful system for mechanistic studies, due to its heterol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4e626a3720c2a79544c8c768e05f0232
https://doi.org/10.1021/bi900338n
https://doi.org/10.1021/bi900338n
Publikováno v:
Archives of Biochemistry and Biophysics. 476:87-94
Ligand binding to transport sites constitutes the initial step in the catalytic cycle of transport ATPases. Here, we consider the well characterized Ca2+ ATPase of sarcoplasmic reticulum (SERCA) and describe a series of Ca2+ binding isotherms obtaine
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c6ede67b2b9ede9ec4ce1a27ccf32ee9
https://doi.org/10.1016/j.abb.2008.04.035
https://doi.org/10.1016/j.abb.2008.04.035
Autor:
Giuseppe Inesi, Yuta Hatori, Chikashi Toyoshima, Rajendra Pilankatta, Ayami Hirata, David Lewis
Publikováno v:
The Journal of Biological Chemistry
Recombinant and purified Thermotoga maritima CopA sustains ATPase velocity of 1.78-2.73 micromol/mg/min in the presence of Cu+ (pH 6, 60 degrees C) and 0.03-0.08 micromol/mg/min in the absence of Cu+. High levels of enzyme phosphorylation are obtaine
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bd104a27dd3525435994fd4957899a5e
https://doi.org/10.1074/jbc.m802735200
https://doi.org/10.1074/jbc.m802735200