about
Amine-synthesizing enzyme N-substituted formamide deformylase: screening, purification, characterization, and gene cloningMetals in cyanobacteria: analysis of the copper, nickel, cobalt and arsenic homeostasis mechanismsOn the origin of life in the Zinc world. 2. Validation of the hypothesis on the photosynthesizing zinc sulfide edifices as cradles of life on EarthCobalt substitution of mouse R2 ribonucleotide reductase as a model for the reactive diferrous state: spectroscopic and structural evidence for a ferromagnetically coupled dinuclear cobalt clusterCrystal structures of the liganded and unliganded nickel-binding protein NikA from Escherichia coliCrystal structure of aldoxime dehydratase and its catalytic mechanism involved in carbon-nitrogen triple-bond synthesisResponse of CnrX from Cupriavidus metallidurans CH34 to nickel bindingDiscovery of a novel enzyme, isonitrile hydratase, involved in nitrogen-carbon triple bond cleavageComparative and functional genomic analysis of prokaryotic nickel and cobalt uptake transporters: evidence for a novel group of ATP-binding cassette transportersProteomic and metabolomic analyses reveal metabolic responses to 3-hydroxypropionic acid synthesized internally in cyanobacterium Synechocystis sp. PCC 6803Dinuclear cobalt(II) and cobalt(III) complexes of bis-bidentate napthoquinone ligands.Cobalt immobilization by manganese oxidizing bacteria from the Indian ridge system.Global gene expression profiling in human lung cells exposed to cobalt.Comparative genomic analyses of nickel, cobalt and vitamin B12 utilizationSelf-subunit swapping chaperone needed for the maturation of multimeric metalloenzyme nitrile hydratase by a subunit exchange mechanism also carries out the oxidation of the metal ligand cysteine residues and insertion of cobalt.General trends in trace element utilization revealed by comparative genomic analyses of Co, Cu, Mo, Ni, and Se.Fluorescent sensors for measuring metal ions in living systemsRcnB is a periplasmic protein essential for maintaining intracellular Ni and Co concentrations in Escherichia coli.Substrate specificity of nickel/cobalt permeases: insights from mutants altered in transmembrane domains I and II.Novel aldoxime dehydratase involved in carbon-nitrogen triple bond synthesis of Pseudomonas chlororaphis B23. Sequencing, gene expression, purification, and characterization.Photoactive Ruthenium Nitrosyls: Effects of Light and Potential Application as NO Donors.Discovery of a reaction intermediate of aliphatic aldoxime dehydratase involving heme as an active center.Interaction between the functional polymorphisms of the alcohol-metabolism genes in protection against alcoholism.The tRNase Z family of proteins: physiological functions, substrate specificity and structural properties.Self-subunit swapping occurs in another gene type of cobalt nitrile hydrataseEstablishment of Bioprocess for Synthesis of Nicotinamide by Recombinant Escherichia coli Expressing High-Molecular-Mass Nitrile Hydratase.Sinorhizobium meliloti bluB is necessary for production of 5,6-dimethylbenzimidazole, the lower ligand of B12Environmental factors influencing the structural dynamics of soil microbial communities during assisted phytostabilization of acid-generating mine tailings: a mesocosm experiment.Strategy for successful expression of the Pseudomonas putida nitrile hydratase activator P14K in Escherichia coli.Comparative genomics of trace element dependence in biology.Environmental adaptability and stress tolerance of Laribacter hongkongensis: a genome-wide analysis.Influence of Co and B 12 on the growth and nitrogen fixation of TrichodesmiumHow does single oxygen atom addition affect the properties of an Fe-nitrile hydratase analogue? The compensatory role of the unmodified thiolate.Sulfur K-edge XAS and DFT calculations on nitrile hydratase: geometric and electronic structure of the non-heme iron active siteSolving the Measurement Problem and then Steppin' Out over the Line Riding the Rarest Italian: Crossing the Streams to Retrieve Stable Bioactivity in Majorana Bound States of Dialy zed Human Platelet Lysates.Successful expression of the Bordetella petrii nitrile hydratase activator P14K and the unnecessary role of Ser115Promiscuity in the Enzymatic Catalysis of Phosphate and Sulfate Transfer.New function of aldoxime dehydratase: Redox catalysis and the formation of an unexpected product.Construction of a subunit-fusion nitrile hydratase and discovery of an innovative metal ion transfer pattern.Use of metallopeptide based mimics demonstrates that the metalloprotein nitrile hydratase requires two oxidized cysteinates for catalytic activity
P2860
Q24564660-52D7E84E-324A-46A2-BCB2-8BF3529FC945Q27008192-08AFC2AE-94E4-4BF0-8EC1-9A7F79D5479CQ27498817-B78A5545-F06C-4714-9711-A59026D1D264Q27639266-A88C38FD-0839-452E-9863-D4CE2670D103Q27641971-63C7F7CD-C556-4A69-B083-EB3A9F7EE005Q27676138-F6C40833-90B8-42D4-8B1F-3BCE628452BAQ27697674-E9E5C191-6119-4121-BCC5-E3CB20C432B8Q28212912-886F31D7-A5F4-4729-B563-2FA37AE99496Q28563578-B67DC1F8-4E6B-4E52-B945-68838BC3A985Q28597889-09363AB7-4CD4-4F7D-8D3C-746F269A153FQ30708279-7A36D7D0-4BA2-4FC2-A7CC-FAE9DE3C8DD4Q30991570-27C85BDD-CD7A-46EB-B14C-7C7F9E3ED990Q33286948-8467A5E7-ADD3-4484-8981-B5185A3E5928Q33408048-4585828E-BB1C-46CC-B2E2-BDC11C4AD662Q33426734-9D886447-CC6E-4B9F-9518-665991BCFB23Q33661673-4BB629F2-D3BB-4CB9-BD52-DC4AEECE43CDQ33896372-F816F43D-4682-4CDE-97BE-14D1D1328BDAQ33930253-8BE8489B-3D6E-4B13-BC59-38643B67DC4FQ34132793-08F56A60-41BC-4BF4-A40C-666A893147D3Q34201045-A67BBB94-A6A4-4679-9485-5C4C6E736AF5Q34259551-039DC7C4-1890-4046-AD49-1CA3510E8516Q34270740-D1135A0A-0AB2-4F7B-A325-3BFC3A43F55AQ34390264-19057228-FE57-4618-B226-FD6BC5998882Q34473841-DB0897B5-9F9B-46C8-98F1-973ABECFD652Q34505988-68AE6D4A-899F-43A7-9B81-EA48414B956BQ34550466-4CFF05AA-8524-4D26-AF2C-9F326552364CQ34574884-15578346-05F4-437B-95A1-961C1B01BABEQ34620086-2958459B-51E9-4B12-88A8-C708B787C9B5Q34754324-BDCE6949-8C7B-4C1B-B724-8AB7461A4FD2Q35084946-90C4D1D0-B7C0-4CCE-BA62-3D8848EFEC10Q35102721-4FA46668-1E82-4F20-A4C7-F5FB8AC72AA5Q35753367-06A1DB64-B49D-4F89-AF0D-B4350E57C34BQ35785498-E4AEB294-4360-434F-B3EF-6367F5F98BEDQ35798432-03D991E6-0EB1-47CA-8A04-2729D2A25162Q35856010-1197F117-57DA-4A60-B22B-8ACDE77D85DCQ35929368-8EA26B47-0E5B-4A30-9A47-17CD73D3E27BQ36019839-49000139-363E-4875-A203-A7F0F32287C1Q36347255-C41D8B06-BDEB-4C70-85A8-C7AA1A1E4B14Q36453634-240D65AF-DE97-4A5D-A85E-39C82BFCC471Q36603367-E4BCD60A-9F17-4853-B682-E73F69EA1C89
P2860
description
1999 nî lūn-bûn
@nan
1999 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Cobalt proteins.
@ast
Cobalt proteins.
@en
Cobalt proteins.
@nl
type
label
Cobalt proteins.
@ast
Cobalt proteins.
@en
Cobalt proteins.
@nl
prefLabel
Cobalt proteins.
@ast
Cobalt proteins.
@en
Cobalt proteins.
@nl
P2860
P1433
P1476
Cobalt proteins.
@en
P2093
M Kobayashi
P2860
P356
10.1046/J.1432-1327.1999.00186.X
P407
P577
1999-04-01T00:00:00Z