Zobrazeno 1 - 10
of 55
pro vyhledávání: '"Robert A. Hallewell"'
Autor:
Robert A. Hallewell, Neil F. Fairweather, Jean Lud Cadet, Christopher C. Matthews, Jan B. Wollack, Dayse M. Figueiredo, Paul S. Fishman, Gordon Dougan
Publikováno v:
Journal of Molecular Neuroscience. 14:155-166
There is evidence that raising cellular levels of Cu2+/Zn2+ superoxide dismutase (SOD1) can protect neurons from oxidative injury. We compared a novel method of elevating neuronal SOD activity using a recombinant hybrid protein composed of the atoxic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::807b240143b7892b84ad5efcfd21dd71
https://doi.org/10.1385/jmn:14:3:155
https://doi.org/10.1385/jmn:14:3:155
Autor:
John A. Tainer, Terence P. Lo, Diane E. Cabelli, Paul Beroza, Robert A. Hallewell, Cindy L. Fisher, Elizabeth D. Getzoff
Publikováno v:
Proteins: Structure, Function, and Genetics. 29:103-112
Key charged residues in Cu,Zn superoxide dismutase (Cu,Zn SOD) promote electrostatic steering of the superoxide substrate to the active site Cu ion, resulting in dismutation of superoxide to oxygen and hydrogen peroxide. Lys-136, along with the adjac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e328206951afca68837725f9a86d83f7
https://doi.org/10.1002/(sici)1097-0134(199709)29:1<103::aid-prot8>3.0.co
https://doi.org/10.1002/(sici)1097-0134(199709)29:1<103::aid-prot8>3.0.co
Autor:
Gordon Dougan, Joseph M. Savitt, Dayse M. Figueiredo, Li Li Chen, Neil F. Fairweather, Robert A. Hallewell, Deborah A. Parks, Paul S. Fishman
Publikováno v:
Experimental Neurology. 145:546-554
The nontoxic C fragment of tetanus toxin (TC) can transport other proteins from the circulation to central nervous system (CNS) motor neurons. Increased levels of CuZn superoxide dismutase (SOD) are protective in experimental models of stroke and Par
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2331b329da9dc099a4ab185403457441
https://doi.org/10.1006/exnr.1997.6490
https://doi.org/10.1006/exnr.1997.6490
Autor:
John A. Tainer, Maurice Boissinot, Elizabeth D. Getzoff, Diane E. Cabelli, S. Karnas, James R. Lepock, Robert A. Hallewell
Publikováno v:
The EMBO Journal. 16:2171-2178
Human Cu,Zn superoxide dismutase (SOD) is a single domain all beta-sheet protein with its eight beta-strands arranged as a Greek key beta-barrel or immunoglobulin fold. Three circularly permuted variants of SOD were made by joining the native amino-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::71a9cc618333e153feb5229e8531f570
https://doi.org/10.1093/emboj/16.9.2171
https://doi.org/10.1093/emboj/16.9.2171
Autor:
John A. Tainer, Michael J. Hickey, James R. Lepock, Hans E. Parge, Diane E. Cabelli, Robert A. Hallewell, Gloria E. O. Borgstahl, Michael J. Johnson, Maurice Boissinot
Publikováno v:
Biochemistry. 35:4287-4297
Human manganese superoxide dismutase (MnSOD) is a homotetrameric enzyme which protects mitochondria against oxygen-mediated free radical damage. Within each subunit, both the N-terminal helical hairpin and C-terminal alpha/beta domains contribute lig
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d6f6cbbf4a380166ed0266f7b9b029fa
https://doi.org/10.1021/bi951892w
https://doi.org/10.1021/bi951892w
Autor:
Edwin Soriano, Wu Yen Hung, Allen D. Roses, Afif Hentati, Teepu Siddique, Brian Herzfeldt, Hans E. Parge, Zafar Iqbal, Raymond P. Roos, Annarueber Cayabyab, Ping Hu, John A. Tainer, Aftab Ahmed, Han Xiang Deng, Elizabeth D. Getzoff, Celestine Smyth, Gang Deng, Margaret A. Pericak-Vance, Robert A. Hallewell, Carolyn Warner
Publikováno v:
Science. 261:1047-1051
Single-site mutants in the Cu,Zn superoxide dismutase (SOD) gene (SOD1) occur in patients with the fatal neurodegenerative disorder familial amyotrophic lateral sclerosis (FALS). Complete screening of the SOD1 coding region revealed that the mutation
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c047aa6ea70f57445b8a93372e7b3a11
https://doi.org/10.1126/science.8351519
https://doi.org/10.1126/science.8351519
Autor:
Diane E. Cabelli, Elizabeth D. Getzoff, Robert A. Hallewell, Lucia Banci, Maria Silvia Viezzoli
Publikováno v:
Journal of Inorganic Biochemistry. 50:89-100
Negatively charged glutamic acid residues at positions 132 and 133 in human Cu 2 Zn 2 SOD are located at the entrance to the active site cavity and affect electrostatic interactions with the negatively charged substrate. The mutants in which these re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4237e852be8d3ecb41de0e5f6a6d8ad8
https://doi.org/10.1016/0162-0134(93)80016-3
https://doi.org/10.1016/0162-0134(93)80016-3
Publikováno v:
Biochemistry. 32:4384-4388
The preparation and biophysical characterization of a mutant of superoxide dismutase in which the native Thr 137 has been substituted with a positive Arg residue are reported. Thr 137 forms, together with Arg 143, a bottleneck at the entrance to the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c57de94870e5df4caa52fb37161bcb59
https://doi.org/10.1021/bi00067a030
https://doi.org/10.1021/bi00067a030
Autor:
John A. Tainer, Gloria E. O. Borgstahl, Robert A. Hallewell, Wayne F. Beyer, Hans E. Parge, Michael J. Hickey
Publikováno v:
Cell. 71:107-118
The 2.2 A resolution crystal structure of recombinant human manganese superoxide dismutase, a homotetrameric enzyme that protects mitochondria against oxygen-mediated free radical damage, has been determined. Within each subunit, both the N-terminal
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ff1cc2fb5c14b303a829098dd9488eba
https://doi.org/10.1016/0092-8674(92)90270-m
https://doi.org/10.1016/0092-8674(92)90270-m
Autor:
Robert A. Hallewell, Lucia Banci, Cindy L. Fisher, Elizabeth D. Getzoff, Hans E. Parge, Diane E. Cabelli, Maria Silvia Viezzoli
Publikováno v:
Nature. 358:347-351
The enzyme Cu, Zn superoxide dismutase (SOD) protects against oxidative damage by dismuting the superoxide radical O2-. to molecular oxygen and hydrogen peroxide at the active-site Cu ion in a reaction that is rate-limited by diffusion and enhanced b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fa46f3846a643479922697a7c6e1df24
https://doi.org/10.1038/358347a0
https://doi.org/10.1038/358347a0