Zobrazeno 1 - 10
of 13
pro vyhledávání: '"David I. Kreimer"'
Publikováno v:
Biochemistry. 39:14183-14195
The membrane-bound complex of the Salmonella typhimurium histidine permease, an ABC transporter (or traffic ATPase), is composed of two membrane proteins, HisQ and HisM, and two identical copies of an ATP-hydrolyzing protein, HisP. We have developed
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::af3eab066e0aa11e88ced324158231b8
https://doi.org/10.1021/bi001066+
https://doi.org/10.1021/bi001066+
Autor:
Henrik Malak, Valery L. Shnyrov, Joseph R. Lakowicz, Enrique Villar, Sergei Trakhanov, David I. Kreimer
Publikováno v:
European Journal of Biochemistry. 267:4242-4252
The bacterial histidine permease is a model system for ABC transporters (traffic ATPases). The water-soluble receptor of this permease, HisJ, binds l-histidine and l-arginine (tightly) and l-lysine and l-ornithine (less tightly) in the periplasm, int
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::06040ae52f61038f46e3fab39ea05636
https://doi.org/10.1046/j.1432-1033.2000.01470.x
https://doi.org/10.1046/j.1432-1033.2000.01470.x
Publikováno v:
Proceedings of the National Academy of Sciences. 94:2848-2852
Acetylcholinesterase from Torpedo californica partially unfolds to a state with the physicochemical characteristics of a “molten globule” upon mild thermal denaturation or upon chemical modification of a single nonconserved buried cysteine residu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::56a8db4658c73e118af4f281fc5fb3ad
https://doi.org/10.1073/pnas.94.7.2848
https://doi.org/10.1073/pnas.94.7.2848
Publikováno v:
Proceedings of the National Academy of Sciences. 91:12145-12149
Cys-231 of Torpedo californica acetylcholinesterase (EC 3.1.1.7) was selectively labeled with the mercury derivative of a stable nitroxyl radical. In 1.5 M guanidinium chloride, this conjugate exists in a molten globule state (MG), whereas in 5 M den
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a31df81a61fc3fb7eda25da259645aba
https://doi.org/10.1073/pnas.91.25.12145
https://doi.org/10.1073/pnas.91.25.12145
Publikováno v:
Biochemical and Biophysical Research Communications. 198:915-922
Exposure of purified acetylcholinesterase from Torpedo californica to a system generating oxygen radicals (viz, ascorbic acid/Fe(EDTA) 2 /H 2 O 2 ) inactivated the enzyme. The enzyme retained its native dimeric form, but electrophoresis under denatur
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1c9dda0b16b7380185a26d1a3652cee6
https://doi.org/10.1006/bbrc.1994.1130
https://doi.org/10.1006/bbrc.1994.1130
Publikováno v:
Protein science : a publication of the Protein Society. 7(3)
To further investigate favorable effects of divalent cations on the formation of protein crystals, three complexes of Salmonella typhimurium histidine-binding protein were crystallized with varying concentrations of cadmium salts. For each of the thr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::67c84e0dadf7bc2c21237aca9e2eae8c
https://pubmed.ncbi.nlm.nih.gov/9541391
https://pubmed.ncbi.nlm.nih.gov/9541391
Chemical modification with sulfhydryl reagents of the single, nonconserved cysteine residue Cys231 in each subunit of a disulfide-linked dimer of Torpedo californica acetylcholinesterase produces a partially unfolded inactive state. Another partially
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bc3bf2148ed4a6e8f5aa9c50378337cc
https://europepmc.org/articles/PMC2143540/
https://europepmc.org/articles/PMC2143540/
Autor:
David I. Kreimer, Joel L. Sussman, Lev Weiner, Mia L. Raves, Elena A. Dolginova, Israel Silman
Publikováno v:
Biochemistry. 33(48)
Chemical modification of Torpedo californica acetylcholinesterase by various sulfhydryl reagents results in its conversion to one of two principal states. One of these states, viz., that produced by disulfides and alkylating agents, is stable. The se
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a78470b2d36886c5426e44ec18cb238c
https://pubmed.ncbi.nlm.nih.gov/7981200
https://pubmed.ncbi.nlm.nih.gov/7981200
Publikováno v:
The Journal of biological chemistry. 269(48)
Torpedo acetylcholinesterase is a disulfide-linked homodimer containing three intramolecular disulfide bonds, as well as a single free thiol on Cys-231. We report that in a "molten globule" state, produced by 1.5 M guanidine hydrochloride, this enzym
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::19739c56905daa45ca3215951c844484
https://pubmed.ncbi.nlm.nih.gov/7982909
https://pubmed.ncbi.nlm.nih.gov/7982909
Autor:
Kreimer, David I.1, Malak, Henrik2, Lakowicz, Joseph R.2, Trakhanov, Sergei1, Villar, Enrique3, Shnyrov, Valery L.3,4
Publikováno v:
European Journal of Biochemistry. Jul2000 Part 1, Vol. 267 Issue 13, p4242-4252. 11p. 1 Black and White Photograph, 3 Charts, 6 Graphs.