Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Amy S. Hearn"'
Autor:
Harry S. Nick, Haiqain An, David N. Silverman, Isabel A. Abreu, Amy S. Hearn, Diane E. Cabelli
Publikováno v:
Biochemistry. 47:2350-2356
Deinococcus radiodurans (Drad), a bacterium with an extraordinary capacity to tolerate high levels of ionizing radiation, produces only a manganese-containing superoxide dismutase (MnSOD). As MnSOD has been shown to remove superoxide radical with var
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bac2595fa7b523f5a43cfc5f2d912c5b
https://doi.org/10.1021/bi7016206
https://doi.org/10.1021/bi7016206
Autor:
David N. Silverman, James R. Zucali, Amy S. Hearn, Anupam Agarwal, Harry S. Nick, Jorge E. Garcia, Vincent Leveque, Bradley S. Fletcher, Christopher A. Davis, J. Andres Melendez, Justin S. Bickford
Publikováno v:
Journal of Biological Chemistry. 279:12769-12776
Mn-SOD serves as the primary cellular defense against oxidative damage by converting superoxide radicals () to O2 and H2O2. A unique characteristic of this mitochondrial anti-oxidant enzyme is the conservation from bacteria to man of a rapidly formed
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ef520191db002e77d3640c52773d24c2
https://doi.org/10.1074/jbc.m310623200
https://doi.org/10.1074/jbc.m310623200
Autor:
James P. Luba, Harry S. Nick, David N. Silverman, John A. Tainer, Cecilia A. Ramilo, Diane E. Cabelli, M. Elizabeth Stroupe, Amy S. Hearn
Publikováno v:
Biochemistry. 42:2781-2789
Catalysis of the disproportionation of superoxide by human manganese superoxide dismutase (MnSOD) is characterized by an initial burst of catalysis followed by a much slower region that is zero order in superoxide and due to a product inhibition by p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9621282838165113e046139910e0abb3
https://doi.org/10.1021/bi0266481
https://doi.org/10.1021/bi0266481
Autor:
James R. Lepock, David N. Silverman, Diane E. Cabelli, Harry S. Nick, John A. Tainer, M.E. Stroupe, Amy S. Hearn
Publikováno v:
Biochemistry. 40:12051-12058
Manganese superoxide dismutase (MnSOD) cycles between the Mn(II) and Mn(III) states during the catalyzed disproportionation of O(2)(*-), a catalysis that is limited at micromolar levels of superoxide by a peroxide-inhibited complex with the metal. We
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b9dbd32aa991425a4bfe9cee2b4c32a0
https://doi.org/10.1021/bi011047f
https://doi.org/10.1021/bi011047f
Autor:
David N. Silverman, Vincent Leveque, Amy S. Hearn, Harry S. Nick, John A. Tainer, Yue Guan, Diane E. Cabelli
Publikováno v:
Biochemistry. 38:11686-11692
Tryptophan 161 is a highly conserved residue that forms a hydrophobic side of the active site cavity of manganese superoxide dismutase (MnSOD), with its indole ring adjacent to and about 5 A from the manganese. We have made a mutant containing the co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fe59fb0455131ee684127c67599d667c
https://doi.org/10.1021/bi9909142
https://doi.org/10.1021/bi9909142
Publikováno v:
Journal of Biological Chemistry. 274:24457-24460
The reduction with excess H(2)O(2) of human Mn(III) superoxide dismutase (SOD) and the active-site mutant Y34F Mn(III)SOD was measured by scanning stopped-flow spectrophotometry and revealed the presence of an intermediate in the reduction of the man
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ec1f9a62b88f2f025bbf573e8a8e43b0
https://doi.org/10.1074/jbc.274.35.24457
https://doi.org/10.1074/jbc.274.35.24457
Autor:
Harry S. Nick, Diane E. Cabelli, J. Jefferson P. Perry, David N. Silverman, Amy S. Hearn, John A. Tainer
Publikováno v:
Biochemistry. 48(15)
Superoxide dismutase (SOD) enzymes are critical in controlling levels of reactive oxygen species (ROS) that are linked to aging, cancer, and neurodegenerative disease. Superoxide (O(2)(*-)) produced during respiration is removed by the product of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::71faa2d742d491adfa578ccc6bce0441
https://pubmed.ncbi.nlm.nih.gov/19265433
https://pubmed.ncbi.nlm.nih.gov/19265433
Autor:
John A. Tainer, M. Elizabeth Stroupe, Harry S. Nick, Amy S. Hearn, David N. Silverman, J. Jefferson P. Perry, William B. Greenleaf, Diane E. Cabelli, James R. Lepock
Publikováno v:
Biochemistry. 43(22)
The side chain of Gln143, a conserved residue in manganese superoxide dismutase (MnSOD), forms a hydrogen bond with the manganese-bound solvent and is critical in maintaining catalytic activity. The side chains of Tyr34 and Trp123 form hydrogen bonds
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7f0b75e8556122e79e7f989bebc44f2a
https://pubmed.ncbi.nlm.nih.gov/15170341
https://pubmed.ncbi.nlm.nih.gov/15170341
Autor:
Christopher A, Davis, Amy S, Hearn, Bradley, Fletcher, Justin, Bickford, Jorge E, Garcia, Vincent, Leveque, J Andres, Melendez, David N, Silverman, James, Zucali, Anupam, Agarwal, Harry S, Nick
Publikováno v:
The Journal of biological chemistry. 279(13)
Mn-SOD serves as the primary cellular defense against oxidative damage by converting superoxide radicals (O(2)(-)) to O(2) and H(2)O(2). A unique characteristic of this mitochondrial anti-oxidant enzyme is the conservation from bacteria to man of a r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::36ef42a88583c886728322e57eebb39c
https://pubmed.ncbi.nlm.nih.gov/14688256
https://pubmed.ncbi.nlm.nih.gov/14688256
Autor:
James R. Lepock, David N. Silverman, Li Fan, James P. Luba, William B. Greenleaf, Amy S. Hearn, Harry S. Nick, John A. Tainer, Diane E. Cabelli
Publikováno v:
The Journal of biological chemistry. 279(7)
The side chains of His30 and Tyr166 from adjacent subunits in the homotetramer human manganese superoxide dismutase (Mn-SOD) form a hydrogen bond across the dimer interface and participate in a hydrogen-bonded network that extends to the active site.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1c92682edad536b0fc57b5a5e85acb30
https://pubmed.ncbi.nlm.nih.gov/14638684
https://pubmed.ncbi.nlm.nih.gov/14638684