Zobrazeno 1 - 10
of 315
pro vyhledávání: '"H. R. Kaback"'
Autor:
H R Kaback
Publikováno v:
Annual Review of Biochemistry. 90:1-29
Bacterial cytoplasmic membrane vesicles provide a unique experimental system for studying active transport. Vesicles are prepared by lysis of osmotically sensitized cells (i.e., protoplasts or spheroplasts) and comprise osmotically intact, unit-membr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::19d9b20206052b8c128f4cbfd9ae8736
https://doi.org/10.1146/annurev-biochem-011520-105008
https://doi.org/10.1146/annurev-biochem-011520-105008
Publikováno v:
Biochemistry
Biochemistry, vol 53, iss 9
Jiang, X; Villafuerte, MKR; Andersson, M; White, SH; & Kaback, HR. (2014). Galactoside-binding site in LacY. Biochemistry, 53(9), 1536-1543. doi: 10.1021/bi401716z. UCLA: Retrieved from: http://www.escholarship.org/uc/item/6d48v662
Biochemistry, vol 53, iss 9
Jiang, X; Villafuerte, MKR; Andersson, M; White, SH; & Kaback, HR. (2014). Galactoside-binding site in LacY. Biochemistry, 53(9), 1536-1543. doi: 10.1021/bi401716z. UCLA: Retrieved from: http://www.escholarship.org/uc/item/6d48v662
Although an X-ray crystal structure of lactose permease (LacY) has been presented with bound galactopyranoside, neither the sugar nor the residues ligating the sugar can be identified with precision at ∼3.5 Å. Therefore, additional evidence is imp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::783f8e7a500c1f9371a73c3e5545c093
http://europepmc.org/articles/PMC3985706
http://europepmc.org/articles/PMC3985706
Publikováno v:
Nature Reviews Molecular Cell Biology. 2:610-620
Membrane transport proteins catalyse the movement of molecules into and out of cells and organelles, but their hydrophobic and metastable nature often makes them difficult to study by traditional means. Novel approaches that have been developed and a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::870fdf8355386e752d9a9d85b1926d2d
https://doi.org/10.1038/35085077
https://doi.org/10.1038/35085077
Publikováno v:
Biochemistry. 40:3184-3188
By exploiting substrate protection of Cys148 in lactose permease, a methanethiosulfonate nitroxide spin-label was directed specifically to one of two Cys residues in a double-Cys mutant, followed by labeling of Cys148 with a thiol-reactive chelator t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::99d43482bba04ec1cf8183bba4fa3dc8
https://doi.org/10.1021/bi002333e
https://doi.org/10.1021/bi002333e
Autor:
H R Kaback, Wolin Cd
Publikováno v:
Biochemistry. 40:1996-2003
Mutants with single amino acid deletions in the loops of lactose permease retain activity, while mutants with single deletions in transmembrane helices are inactive, and the loop--helix boundaries of helices IV, V, VII, VIII, and IX have been approxi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5e594dfab24940b2782a09f9cba52907
https://doi.org/10.1021/bi0025767
https://doi.org/10.1021/bi0025767
Publikováno v:
Biochemistry. 39:11381-11388
A series of nitroxide spin-labeled alpha- or beta-galactopyranosides and a nitroxide spin-labeled beta-glucopyranoside have been synthesized and examined for binding to the lactose permease of Escherichia coli. Out of the twelve nitroxide spin-labele
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::325a0f99de5f337192496e6c109128af
https://doi.org/10.1021/bi001075i
https://doi.org/10.1021/bi001075i
Autor:
H R Kaback, Wolin Cd
Publikováno v:
Biochemistry. 39:6130-6135
Glu126 (helix IV) and Arg144 (helix V) in the lactose permease of Escherichia coli are critical for substrate binding and transport, and the two residues are in close proximity and charge-paired. By using a functional permease construct with two tand
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a49a671bd31eb9705d40be1cc8df512d
https://doi.org/10.1021/bi0001269
https://doi.org/10.1021/bi0001269
Publikováno v:
Biochemistry. 39:3134-3140
The N- and C-terminal halves of lactose permease, each with a single-Cys residue in a cytoplasmic loop, were coexpressed, and cross-linking was studied in the absence or presence of ligand. Out of the 68 paired-Cys mutants in cytoplasmic loops IV/V a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dd5988d116ae23e188d3fe7dfc164aec
https://doi.org/10.1021/bi992509g
https://doi.org/10.1021/bi992509g
Autor:
Min Zhao, Jordi Hernández-Borrell, K.-C. Zen, Christian Altenbach, Wayne L. Hubbell, H R Kaback
Publikováno v:
Biochemistry. 38:15970-15977
Glu126 and Arg144 in helices IV and V, respectively, in the lactose permease of Escherichia coli, which play an indispensable role in substrate binding, are charge-paired and in close proximity [Venkatesan, P., Kaback, H. R. (1998) Proc. Natl. Acad.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::566a5bd968d0bd91164706c9cbb012ef
https://doi.org/10.1021/bi991754x
https://doi.org/10.1021/bi991754x
Autor:
Jenny C. Lee, H R Kaback, Gilbert G. Privé, J. le Coutre, Christian K Engel, Kym F. Faull, Julian P. Whitelegge
Publikováno v:
Proceedings of the National Academy of Sciences. 96:10695-10698
Genes encoding membrane proteins comprise a substantial proportion of genomes sequenced to date, but ability to perform structural studies on this portion of the proteome is limited. Electrospray ionization-MS (ESI-MS) of an intact protein generates
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::417a23ab7764fc21f0b669e0729a81c4
https://doi.org/10.1073/pnas.96.19.10695
https://doi.org/10.1073/pnas.96.19.10695