Nucleotide sequence and expression of the selenocysteine-containing polypeptide of formate dehydrogenase (formate-hydrogen-lyase-linked) from Escherichia coli - Wikidata - awgldk - TriplyDB

Nucleotide sequence and expression of the selenocysteine-containing polypeptide of formate dehydrogenase (formate-hydrogen-lyase-linked) from Escherichia coli

Nucleotide sequence and expression of the selenocysteine-containing polypeptide of formate dehydrogenase (formate-hydrogen-lyase-linked) from Escherichia coli

http://www.wikidata.org/entity/Q24628744

about

Selenocysteine, pyrrolysine, and the unique energy metabolism of methanogenic archaea cDNA cloning, purification, and characterization of mouse liver selenocysteine lyase. Candidate for selenium delivery protein in selenoprotein synthesis Cloning and functional characterization of human selenophosphate synthetase, an essential component of selenoprotein synthesis NAD(+)-dependent formate dehydrogenase How selenium has altered our understanding of the genetic code Molecular cloning and characterization of an interferon induced human cDNA with sequence homology to a mammalian peptide chain release factor Catalytic properties of an Escherichia coli formate dehydrogenase mutant in which sulfur replaces selenium Cotranslational insertion of selenocysteine into formate dehydrogenase from Escherichia coli directed by a UGA codon Reversible interconversion of carbon dioxide and formate by an electroactive enzyme Cloning and sequencing of a putative Escherichia coli [NiFe] hydrogenase-1 operon containing six open reading frames Organization and growth phase-dependent transcription of methane genes in two regions of the Methanobacterium thermoautotrophicum genome The molecular biology of selenocysteine Selenoproteins in nervous system development and function Synthesis and decoding of selenocysteine and human health Crystal structure of human selenocysteine tRNA Structural Insights into the Recovery of Aldolase Activity inN-Acetylneuraminic Acid Lyase by Replacement of the Catalytically Active Lysine with γ-Thialysine by Using a Chemical Mutagenesis Strategy Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): a vehicle for direct determination of three-dimensional structure Substrate-specific selenoprotein B of glycine reductase from Eubacterium acidaminophilum. Biochemical and molecular analysis Selenium-containing xanthine dehydrogenase from Eubacterium barkeri Cloning and sequencing of the genes encoding the periplasmic-cytochrome B-containing selenate reductase of Thauera selenatis Dual functions of codons in the genetic code In vitro synthesis of selenocysteinyl-tRNA(UCA) from seryl-tRNA(UCA): involvement and characterization of the selD gene product Identification of a protein component of a mammalian tRNA(Sec) complex implicated in the decoding of UGA as selenocysteine.Insights into CO2 Fixation Pathway of Clostridium autoethanogenum by Targeted Mutagenesis Complete genome sequence of Enterobacter sp. IIT-BT 08: A potential microbial strain for high rate hydrogen production Enhanced hydrogen production from formic acid by formate hydrogen lyase-overexpressing Escherichia coli strains.Recent evidence for evolution of the genetic code Coordination of FocA and pyruvate formate-lyase synthesis in Escherichia coli demonstrates preferential translocation of formate over other mixed-acid fermentation products.Selenium in chemistry and biochemistry in comparison to sulfur.The functional role of selenocysteine (Sec) in the catalysis mechanism of large thioredoxin reductases: proposition of a swapping catalytic triad including a Sec-His-Glu state.Nitrate respiration in relation to facultative metabolism in enterobacteria.Localizing transcripts to single cells suggests an important role of uncultured deltaproteobacteria in the termite gut hydrogen economy Anaerobic induction of Escherichia coli formate dehydrogenase (hydrogenase-linked) is enhanced by gyrase inactivation.Features of the formate dehydrogenase mRNA necessary for decoding of the UGA codon as selenocysteine.Selenocysteine inserting tRNAs: an overview.Genes for selenium dependent and independent formate dehydrogenase in the gut microbial communities of three lower, wood-feeding termites and a wood-feeding roach.Clustered genes encoding the methyltransferases of methanogenesis from monomethylamine Characterization of potential selenium-binding proteins in the selenophosphate synthetase system Regulation and function of selenoproteins in human disease The iscS gene is essential for the biosynthesis of 2-selenouridine in tRNA and the selenocysteine-containing formate dehydrogenase H

P2860

Q21296868-4B9F4E5D-2DFD-458D-8A97-5AB0AFBB32AC Q22253238-F16C0B6D-37C6-4D4A-8F9F-A638081D07D4 Q24337157-621E6816-161D-4231-8F26-12D48D59C27B Q24528257-FD986966-A96B-4E6E-9B0E-1D528D2D39A7 Q24537426-88E5352D-AB02-40CD-A55C-99D3FD7AFBB3 Q24555707-555369FC-AE0B-4877-B1D7-16A65AEEF870 Q24561818-D461F0AF-9AE9-424C-9F0C-3C32D693A7BB Q24610152-9F78B076-0CEE-4772-991C-102F8BF10C77 Q24652765-80F5396C-13B2-4D23-8078-6842E42A2126 Q24673350-BE733E6D-39D4-4E5B-A9FB-06FB7E637327 Q24673562-8BBF270A-7EF5-4D57-A0AA-1235B1ABB9A4 Q27000485-2F6E4DCF-2DC5-4821-8024-6337A34FCB31 Q27009087-FB7A845D-35D0-467F-816B-C181CC9CAE66 Q27022391-DC4AA328-21DF-4020-9727-37AE32AF9869 Q27657082-03146985-C416-4B45-95AD-1E327B2C29F6 Q27676442-975D186D-95AA-4CAC-B739-3186BA51D192 Q27860618-5B48081E-1B2F-47CC-BE9F-BAAFC40E4E51 Q28139587-8958B983-9095-45CB-9ADF-7F2EF8476E0D Q28144660-FF53B217-4F0B-4CA4-9158-AFED82D09B39 Q28145148-C4888A79-609C-401B-A5A5-1AA5BF0FAE98 Q28281447-41AB9A9D-446F-4955-B665-A2992CC91C8C Q28493198-87F9ADF9-3392-41B1-9010-295570615316 Q28569529-8046148B-786C-42A3-926E-A390DEEACD96 Q28601659-731C8F22-4FF6-441F-A7B0-1673EF6C588A Q28657943-0ACC04D0-7380-47E3-8D3E-CAD4C0FF915B Q28769030-6057EFEF-12FF-4269-AB67-8E467EE7508A Q28776139-DE946F58-729B-4AEC-84B7-9369CEDCE996 Q30317900-EEF78902-30AE-455E-A3A5-7EAC4A161858 Q30319747-65222560-8E00-4728-8D63-F8AA2B85D769 Q30320299-AC4EDEA4-36E7-4D47-AB0B-B565F95BA10B Q30449796-46F01BA8-1CE1-44D7-AAAF-439372B42963 Q30548800-D986FFBB-9092-4BCF-BD0B-6679492A2928 Q33552354-6393B7B3-0044-4297-B0D8-079DD259AA17 Q33637893-2D2B106A-F081-43B0-A670-CB2D36DABCAC Q33660986-C5D46E3A-550C-4413-9044-500592FB9357 Q33684934-0E5250F8-BCEE-4077-A2A2-4E68F77C4DF6 Q33732717-2454EC31-9509-4813-BDD9-45976CDEAFCB Q33763227-192A9907-0B9A-4852-ACB3-F16F1D3F7A9D Q34029071-A35E1985-9D82-47C7-BB65-5559196B51AD Q34067251-CBC2E258-E3D0-4D67-AFBC-CBF77D9DAE0A

P2860

Nucleotide sequence and expression of the selenocysteine-containing polypeptide of formate dehydrogenase (formate-hydrogen-lyase-linked) from Escherichia coli

http://www.wikidata.org/entity/Q24628744

description

1986 nî lūn-bûn

@nan

1986 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

1986 թվականի հուլիսին հրատարակված գիտական հոդված

@hy

1986年の論文

@ja

1986年論文

@yue

1986年論文

@zh-hant

1986年論文

@zh-hk

1986年論文

@zh-mo

1986年論文

@zh-tw

1986年论文

@wuu

name

Nucleotide sequence and expres ...... -linked) from Escherichia coli

@ast

Nucleotide sequence and expres ...... -linked) from Escherichia coli

@en

Nucleotide sequence and expres ...... -linked) from Escherichia coli

@nl

type

label

Nucleotide sequence and expres ...... -linked) from Escherichia coli

@ast

Nucleotide sequence and expres ...... -linked) from Escherichia coli

@en

Nucleotide sequence and expres ...... -linked) from Escherichia coli

@nl

prefLabel

Nucleotide sequence and expres ...... -linked) from Escherichia coli

@ast

Nucleotide sequence and expres ...... -linked) from Escherichia coli

@en

Nucleotide sequence and expres ...... -linked) from Escherichia coli

@nl

P1433

Q24628744-9879C4C7-D974-4CBA-A403-4F32279AA415

P1476

Q24628744-B8E955D9-B742-4160-9D02-17F5FBB2FF0D

P2093

Q24628744-536DE828-0F52-487D-95C1-1C087920E22C

Q24628744-84558089-BE78-46D1-866B-9FAD66E832DF

Q24628744-8EF67F6C-F949-431B-924C-3A592304015C

P2860

Q24628744-00750F84-1202-4EEE-8043-5936A964EC8D

Q24628744-1060E4F1-C3BA-46DB-A979-4C53C7292E42

Q24628744-1187C099-D49F-41E7-B313-B5369267FF73

Q24628744-4E931C15-C9F7-4B0D-85D1-D69615CC96B8

Q24628744-51E4C20D-F69F-4105-BD5A-AD12B99D2614

Q24628744-7F39FD10-E0FE-4391-B777-C726E0CDD205

Q24628744-9E861750-EA6F-41FB-86F7-49DC25435F5A

Q24628744-A513592E-314D-421F-9C93-B0DE5DFA69F3

Q24628744-BD1BFD04-1E4C-45F3-86E6-EF3503220E67

Q24628744-C8F4FF96-EADE-486A-BB83-5E547FA07C3D

P304

Q24628744-881F2E91-4E4B-4F65-B99D-AAC2098018A4

P31

Q24628744-6DCFEE8A-2EF1-425B-A032-D7385C95B622

P3181

Q24628744-0EC1DFFF-42BF-4076-A4F0-3C0BB87D3E36

P356

Q24628744-3C95ED13-6C18-4DCF-9BF3-5981E9825398

P407

Q24628744-773BB254-2E4B-45C2-B7A7-2AD25526C43B

P433

Q24628744-883331EA-1C13-41D4-A476-DE9A6B37294F

P478

Q24628744-644B094F-2969-4A0E-B4E1-4236D01318CE

P50

Q24628744-22062AEF-E446-4069-BB4E-B94680A50062

P577

Q24628744-ECF6F036-8293-4EE7-89F1-2380FE511388

P5875

Q24628744-96BC8D49-BC1F-4C86-8BDA-376E64ACA522

P698

Q24628744-2413F31E-A006-45F7-99BB-20561ED57FB8

P921

Q24628744-0E4097CC-7C35-4606-8105-7DD473B64788

Q24628744-F540ABDC-238F-4A7E-A468-A3F0CBA1B9A5

P932

Q24628744-56F42A4E-4AB5-490A-A0E1-A6EFBF362127

P3181

P356

PNAS.83.13.4650

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Nucleotide sequence and expres ...... -linked) from Escherichia coli

@en

P2093

A Birkmann

http://www.w3.org/2001/XMLSchema#string

A Böck

http://www.w3.org/2001/XMLSchema#string

F Zinoni

http://www.w3.org/2001/XMLSchema#string

P2860

Sequencing end-labeled DNA with base-specific chemical cleavages

Construction and characterization of amplifiable multicopy DNA cloning vehicles derived from the P15A cryptic miniplasmid

Structure of the orgin of DNA replication of bacteriophage fd

Lactose genes fused to exogenous promoters in one step using a Mu-lac bacteriophage: in vivo probe for transcriptional control sequences.

In vitro gene fusions that join an enzymatically active beta-galactosidase segment to amino-terminal fragments of exogenous proteins: Escherichia coli plasmid vectors for the detection and cloning of translational initiation signals.

A different genetic code in human mitochondria.

UGA is read as tryptophan in Mycoplasma capricolum.

Resolution of distinct selenium-containing formate dehydrogenases from Escherichia coli.

Simple method for identification of plasmid-coded proteins.

Bacterial peptide chain release factors: conserved primary structure and possible frameshift regulation of release factor 2.

P304

4650-4

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P3181

1402092

http://www.w3.org/2001/XMLSchema#string

P356

10.1073/PNAS.83.13.4650

http://www.w3.org/2001/XMLSchema#string

P407

P433

13

http://www.w3.org/2001/XMLSchema#string

P478

83

http://www.w3.org/2001/XMLSchema#string

P50

Thressa Stadtman

P577

1986-07-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

20214016

http://www.w3.org/2001/XMLSchema#string

P698

2941757

http://www.w3.org/2001/XMLSchema#string

P921

Escherichia coli

L-selenocysteine

P932

323799

http://www.w3.org/2001/XMLSchema#string