Superoxide dismutases: active sites that save, but a protein that kills.
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Contribution of human manganese superoxide dismutase tyrosine 34 to structure and catalysisCrystal structure of the cambialistic superoxide dismutase from Aeropyrum pernix K1--insights into the enzyme mechanism and stabilityIdentification and Analysis of 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS) Gene from Glyphosate Resistant Ochrobactrum intermedium Sq20.Regulation of CuZnSOD and its redox signaling potential: implications for amyotrophic lateral sclerosisThe Chemistry of Neurodegeneration: Kinetic Data and Their Implications.Contributions of the C-terminal helix to the structural stability of a hyperthermophilic Fe-superoxide dismutase (TcSOD)Evolutionary history of redox metal-binding domains across the tree of life.Expression, purification and crystallization of Chaetomium thermophilum Cu,Zn superoxide dismutase.Cupricyclins, novel redox-active metallopeptides based on conotoxins scaffold.Spectroscopic and computational investigation of three Cys-to-Ser mutants of nickel superoxide dismutase: insight into the roles played by the Cys2 and Cys6 active-site residues.Geometric and electronic structure of a peroxomanganese(III) complex supported by a scorpionate ligand.Peroxynitrite mediates active site tyrosine nitration in manganese superoxide dismutase. Evidence of a role for the carbonate radical anionMetal-dioxygen and metal-dinitrogen complexes: where are the electrons?Superoxide dismutases and superoxide reductases.Formation of high-order oligomers by a hyperthemostable Fe-superoxide dismutase (tcSOD).Multifrequency Pulsed EPR Studies of Biologically Relevant Manganese(II) ComplexesLight-driven oxygen production from superoxide by Mn-binding bacterial reaction centers.Reaction landscape of a pentadentate N5-ligated Mn(II) complex with O2˙- and H2O2 includes conversion of a peroxomanganese(III) adduct to a bis(μ-oxo)dimanganese(III,IV) species.Unique Characteristics of Recombinant Hybrid Manganese Superoxide Dismutase from Staphylococcus equorum and S. saprophyticus.Accessing Ni(III)-thiolate versus Ni(II)-thiyl bonding in a family of Ni-N2S2 synthetic models of NiSODClass I ribonucleotide reductases: metallocofactor assembly and repair in vitro and in vivo.Dipeptide-based models of nickel superoxide dismutase: solvent effects highlight a critical role to Ni-S bonding and active site stabilization.X-ray absorption near-edge spectroscopy in bioinorganic chemistry: Application to M-O2 systemsConcerted proton-coupled electron transfers in aquo/hydroxo/oxo metal complexes: electrochemistry of [OsII(bpy)2py(OH2)]2+ in water.Inverse regulation of Fe- and Ni-containing SOD genes by a Fur family regulator Nur through small RNA processed from 3'UTR of the sodF mRNAIn vivo production of active nickel superoxide dismutase from Prochlorococcus marinus MIT9313 is dependent on its cognate peptidaseGeometric and electronic structures of manganese-substituted iron superoxide dismutaseThe SODyssey: superoxide dismutases from biochemistry, through proteomics, to oxidative stress, aging and nutraceuticals.Peroxomanganese complexes as an aid to understanding redox-active manganese enzymes.Oxidative Stress and Neurobiology of Demyelination.Superoxide dismutase--mentor of abiotic stress tolerance in crop plants.A Single Outer-Sphere Mutation Stabilizes apo-Mn Superoxide Dismutase by 35 °C and Disfavors Mn Binding.SOD mimetic activity and antiproliferative properties of a novel tetra nuclear copper (II) complex.Overexpression of CuZnSOD from Arachis hypogaea alleviates salinity and drought stress in tobacco.In vitro leishmanicidal activity of pyrazole-containing polyamine macrocycles which inhibit the Fe-SOD enzyme of Leishmania infantum and Leishmania braziliensis species.Suppression of mitochondrial NADP(+)-dependent isocitrate dehydrogenase activity enhances curcumin-induced apoptosis in HCT116 cells.Modulation of superoxide dismutase (SOD) isozymes by organ development and high long-term salinity in the halophyte Cakile maritima.Imidazole-containing phthalazine derivatives inhibit Fe-SOD performance in Leishmania species and are active in vitro against visceral and mucosal leishmaniasis.Novel tripeptide model of nickel superoxide dismutase.High-affinity manganese coordination by human calprotectin is calcium-dependent and requires the histidine-rich site formed at the dimer interface.
P2860
Q24318481-2010D288-0E26-4523-ABBE-616D8A699ADDQ27666408-24A0CE30-462E-4996-8D67-953AFF313C35Q30402419-396655AC-244C-4B8F-A3D0-465B2310FED6Q30432317-18A6A80A-6EDF-40AC-922F-3A5CE3BE3BABQ30973484-B0381A04-C724-478A-A53E-EB4401D80552Q33572826-0A9624E5-F79F-4E86-930B-06E3EB180603Q33627357-B06AAFA5-C1A7-446A-A27D-2FBDE29685ADQ34109618-C50A5C97-E0F4-456B-80BD-FFB8A6A62ED0Q34154653-1F5F19AF-DE52-4FF6-95F5-141706095E0EQ34382885-B6035A5D-73B9-450C-BAEC-3509BAFC0758Q34543399-87D9FB53-F1C9-4CEA-884B-C06FB6927EE4Q34634246-31550CE9-4217-4047-B803-F8EFC622FBCCQ34731623-D7DF4692-E210-41EE-9810-F8767085A4AEQ35049047-56A7C552-1864-40C1-8440-923F5149B149Q35330064-4C2B7390-2CC4-4DA3-9B94-FE215E1B5A44Q35622913-AD0AD927-516E-4B7A-A16A-CFDF0575E3D6Q35787251-FCF22DF0-5EE7-4530-B253-5FFCB7645838Q35838133-D4FE1648-D937-4EF5-8FF6-BA97422C6E05Q35951583-98AFECB3-E05A-41E0-BC24-0A80C125DE97Q36243050-5F77C5C9-E186-4EFF-806A-680E192629F8Q36435630-715419A6-A017-4AA7-A73A-0E300BB19B0EQ36580065-599D06E6-08F5-43CA-BDD4-2D9547CF7782Q36697523-D20D6ED3-3FC8-431B-A797-9D2B39871AD3Q37274447-D972CAC1-6802-413F-854D-A18089BB542AQ37574204-4F741434-0523-4DBF-89FD-669B53B5C5DFQ37596295-743979AD-08C3-4926-90B0-4EC65357A4A6Q37682121-711C4D91-D4AB-4FF7-9F44-63BD002002D5Q37890428-DEDC35C8-DC46-408E-8488-C21592FF46D8Q38166671-C402D6F9-B2D5-42CA-98FC-67AC38C44A95Q38287176-688B9851-2141-4CEE-B992-9B773A0CC4DFQ38447777-159ED897-F44D-4D34-A701-3AD762C29FC8Q38681084-E96A24D4-77E8-4943-A1ED-C29A23B277B2Q38821195-EFD30B07-F012-49F3-BF56-96D26C1B21BEQ38906471-68157EE1-43A2-4BA4-BC0A-106047D315C4Q39014739-33663EA0-2AC6-40C5-8401-1BB28CE5D25DQ39626958-58513CBA-F0C1-4ADA-A58D-A8C9D5908B0BQ40753462-5AC66207-5141-4135-A2DF-34A9CA816133Q41370122-0B7824D2-ECFC-4991-880C-E403D9192863Q41867509-533CDACF-B4CB-442A-B4AC-5377ACBCA14FQ42127170-B94DD747-E78C-4951-8D37-E628CC0AA80B
P2860
Superoxide dismutases: active sites that save, but a protein that kills.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
2004年论文
@zh
2004年论文
@zh-cn
name
Superoxide dismutases: active sites that save, but a protein that kills.
@ast
Superoxide dismutases: active sites that save, but a protein that kills.
@en
type
label
Superoxide dismutases: active sites that save, but a protein that kills.
@ast
Superoxide dismutases: active sites that save, but a protein that kills.
@en
prefLabel
Superoxide dismutases: active sites that save, but a protein that kills.
@ast
Superoxide dismutases: active sites that save, but a protein that kills.
@en
P1476
Superoxide dismutases: active sites that save, but a protein that kills.
@en
P2093
Anne-Frances Miller
P304
P356
10.1016/J.CBPA.2004.02.011
P577
2004-04-01T00:00:00Z