Genomic evidence that the intracellular proteins of archaeal microbes contain disulfide bonds. - Wikidata - awgldk - TriplyDB

Genomic evidence that the intracellular proteins of archaeal microbes contain disulfide bonds.

Genomic evidence that the intracellular proteins of archaeal microbes contain disulfide bonds.

http://www.wikidata.org/entity/Q34075149

about

JAMM: a metalloprotease-like zinc site in the proteasome and signalosome Comparative genomics of Thermus thermophilus and Deinococcus radiodurans: divergent routes of adaptation to thermophily and radiation resistance Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea A novel function of tissue-type transglutaminase: protein disulphide isomerase The oligomerization and ligand-binding properties of Sm-like archaeal proteins (SmAPs)Structural and functional studies of archaeal viruses Comprehensive de novo structure prediction in a systems-biology context for the archaea Halobacterium sp. NRC-1 The genomics of disulfide bonding and protein stabilization in thermophiles Archaeal Enzymes and Applications in Industrial Biocatalysts A survey of protein structures from archaeal viruses Discovery of a Thermophilic Protein Complex Stabilized by Topologically Interlinked Chains Crystal structure of highly thermostable glycerol kinase from a hyperthermophilic archaeon in a dimeric form Structures and Functional Implications of an AMP-Binding Cystathionine β-Synthase Domain Protein from a Hyperthermophilic Archaeon Structural and functional studies of the Thermus thermophilus 16S rRNA methyltransferase RsmG Crystallographic snapshots of iterative substrate translocations during nicotianamine synthesis in archaea Insights into the hyperthermostability and unusual region-specificity of archaeal Pyrococcus abyssi tRNA m1A57/58 methyltransferase An intersubunit disulfide bridge stabilizes the tetrameric nucleoside diphosphate kinase of Aquifex aeolicus Calculation of the relative chemical stabilities of proteins as a function of temperature and redox chemistry in a hot spring Structure and regulatory role of the C-terminal winged helix domain of the archaeal minichromosome maintenance complex Potential role of glutathione in evolution of thiol-based redox signaling sites in proteins MTH1745, a protein disulfide isomerase-like protein from thermophilic archaea, Methanothermobacter thermoautotrophicum involving in stress response Redox biology: computational approaches to the investigation of functional cysteine residues Cysteine function governs its conservation and degeneration and restricts its utilization on protein surfaces Occurrence of protein disulfide bonds in different domains of life: a comparison of proteins from the Protein Data Bank.Characterization of a multifunctional protein disulfide oxidoreductase from Sulfolobus solfataricus.Biochemical and structural characterization of mammalian-like purine nucleoside phosphorylase from the Archaeon Pyrococcus furiosus.Analysis on conservation of disulphide bonds and their structural features in homologous protein domain families Disulfide bond formation in prokaryotes: history, diversity and design Distance-dependent statistical potentials for discriminating thermophilic and mesophilic proteins Posttranslational protein modification in Archaea.Amylomaltase of Pyrobaculum aerophilum IM2 produces thermoreversible starch gels A primordial RNA modification enzyme: the case of tRNA (m1A) methyltransferase.Structure of the DPS-like protein from Sulfolobus solfataricus reveals a bacterioferritin-like dimetal binding site within a DPS-like dodecameric assembly The structure of G4, the poxvirus disulfide oxidoreductase essential for virus maturation and infectivity.Structural analysis of mevalonate-3-kinase provides insight into the mechanisms of isoprenoid pathway decarboxylases The archaeal Sec-dependent protein translocation pathway.Widespread disulfide bonding in proteins from thermophilic archaea GDAP: a web tool for genome-wide protein disulfide bond prediction.Intramolecular disulfide bond between catalytic cysteines in an intein precursor.Cysteine-cysteine contact preference leads to target-focusing in protein folding.

P2860

Q21092836-E29475D3-14EB-4593-B725-98214FF613DF Q21093605-46876EC1-F814-4A0E-B732-E4856D6BFE3B Q22065753-3D4E7729-BFAF-406D-8367-8B50FF07AF27 Q24530143-C76F2396-15B0-4850-A25E-BCEC35C54F26 Q24644821-E12D5638-D35A-4A91-B50B-6EC96AEB9D48 Q24651853-236975AE-54FD-4B28-9EB2-7B8B16EFEB54 Q24797455-18510E18-2A08-4374-9B62-E301F2696E8D Q24814780-A004472A-2283-452A-9E62-B1987161BC57 Q26780240-FEF2624D-48DF-4C74-81D9-D751F0952D10 Q26851891-C142BF26-E99D-4E31-B313-CA020098F302 Q27644275-18B4ED4A-29FB-4BA9-BAB8-E2808BF8DABD Q27650393-7A78FF2C-19A6-41D1-B1A7-87B1997E6D0B Q27650725-92C412EB-C620-4183-BFAF-D1078E57501F Q27656590-3A15AF3D-EE79-4698-9BBA-22E9907D0D7A Q27657686-33EAABBB-F55A-4805-A14F-7EC400B19538 Q27661744-8CEB5CE1-C26F-4678-B27A-148A0C5BF496 Q27678283-B8A1A083-9C9A-4A89-814D-3D1C462EAC8B Q28476522-AFD70220-428E-499C-8BC9-328081098299 Q28652461-B70EBB87-4E24-4F4B-86DF-24D8DB6DEA5A Q28652594-9339CC4C-5FF0-4CC4-AD66-B3AF82CCC53D Q28754640-15219ED1-280D-4F04-9164-9426C256AC34 Q30393259-F55A5697-8E0A-40D2-A166-7D399CC1A8EA Q30394922-ACB5D442-2491-45FE-B0FC-C9384F58661C Q30729945-39D63FA1-BF0E-401A-B7F8-942A16B63DAA Q31072248-538ABFC9-5190-4328-88F5-DD0456F220CA Q33281558-6278A9E9-A48F-4419-B3A9-20C69327C4C9 Q33396099-DB25249D-98CA-41CE-873C-1FDECD564180 Q33723782-986E41CD-0BD6-4355-8759-0EF996EBE796 Q33939487-47DF2F91-033A-462C-A263-3452DBC62E00 Q33940312-54A99607-4ED0-43A2-937F-02E297BC464C Q33996056-CEAABD58-B081-48B3-9839-43FF5E5BF54A Q34291797-2CCCF601-062F-4B61-8807-5AB49BC6C943 Q34563522-04BE7925-31FF-4D4A-861D-48D82919E467 Q35023719-B44F8CAA-EE00-4AFC-B99D-F621CC59B2B0 Q35044130-33B87DDE-D3F9-4372-8129-DA8D714F1661 Q35213995-7ACD7B08-61CC-47F4-A999-3BE6B4FD281D Q35224072-EE5E2171-0D32-4072-9AA6-CA13622825AD Q35555475-13731A43-800D-4746-9246-93671D0A3DB5 Q35757065-80A2D271-7E47-48A9-A413-B8D85CF5C0ED Q35878643-87FB9185-7FEF-438E-BCED-7C1BEC3A5A89

P2860

Genomic evidence that the intracellular proteins of archaeal microbes contain disulfide bonds.

http://www.wikidata.org/entity/Q34075149

description

2002 nî lūn-bûn

@nan

2002 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի հուլիսին հրատարակված գիտական հոդված

@hy

2002年の論文

@ja

2002年論文

@yue

2002年論文

@zh-hant

2002年論文

@zh-hk

2002年論文

@zh-mo

2002年論文

@zh-tw

2002年论文

@wuu

name

Genomic evidence that the intr ...... robes contain disulfide bonds.

@ast

Genomic evidence that the intr ...... robes contain disulfide bonds.

@en

Genomic evidence that the intr ...... robes contain disulfide bonds.

@nl

type

label

Genomic evidence that the intr ...... robes contain disulfide bonds.

@ast

Genomic evidence that the intr ...... robes contain disulfide bonds.

@en

Genomic evidence that the intr ...... robes contain disulfide bonds.

@nl

prefLabel

Genomic evidence that the intr ...... robes contain disulfide bonds.

@ast

Genomic evidence that the intr ...... robes contain disulfide bonds.

@en

Genomic evidence that the intr ...... robes contain disulfide bonds.

@nl

P1433

Q34075149-3337F866-81C0-45CC-93F9-B39636409CC9

P1476

Q34075149-74F15F24-C498-4A16-8CEF-0FFEB9743DE6

P2093

Q34075149-70F7BC35-090E-4796-A945-35EEA97571E8

Q34075149-7BFC3E70-7CF7-43B3-BBC3-E3C390012C5E

Q34075149-99A6AE3E-EA6E-41B9-AABD-CF57102D4D75

P2860

Q34075149-09CE34F7-7454-426E-997A-D0DF0A9F89F9

Q34075149-0DF30554-4E9B-48E3-9D7D-2F686D60997E

Q34075149-0EDFD83D-AB91-4AA6-A6ED-3849CB3866EE

Q34075149-10098434-3257-4D08-BE62-6E3E003A7949

Q34075149-14A10301-76F8-470C-8EE7-7564EAB45BC3

Q34075149-1A5C34FC-2030-4841-9F4D-12AA368E2F7F

Q34075149-1BBD7091-1DC1-48C3-9B6F-4BEBE1D6A502

Q34075149-283D03F2-73AE-4398-9F1E-921266C92C1A

Q34075149-2868450C-1CE8-4214-A784-B9F94367BAA3

Q34075149-30EC0620-F22A-4AFA-9F0D-6BB3C1FD5874

P304

Q34075149-8B13158E-B149-411E-AAA6-08E290300B75

P31

Q34075149-65654E8B-DABD-454C-B689-65DE17D79B5D

P356

Q34075149-81AFB73A-5DE0-4359-9BCE-5933F6C05AF1

P407

Q34075149-323F70C3-CF12-4E86-9DCA-1E96990DEB1F

P433

Q34075149-64D90DB9-EAE8-48F4-B5A1-D34E54FD68F8

P478

Q34075149-205FD712-3A68-4F1D-822D-012EDC27ED80

P50

Q34075149-8B1227F9-FAAF-4B17-A319-D3E74A3CEE10

P577

Q34075149-0B388B89-996D-4F68-A3E4-C1C7320CB972

P5875

Q34075149-698CA93E-2774-4201-AE64-02E7F6FE19F2

P698

Q34075149-7D30B173-741D-4032-B819-310295EDBC3A

P932

Q34075149-233655EE-883D-4230-834A-99E33AAAA2EF

P356

P1433

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

P1476

Genomic evidence that the intr ...... robes contain disulfide bonds.

@en

P2093

Daniel R Boutz

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

David Eisenberg

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

Parag Mallick

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

P2860

Complete Genome Sequence of an Aerobic Hyper-thermophilic Crenarchaeon, Aeropyrum pernix K1

Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum aerophilum.

The complete genome of the hyperthermophilic bacterium Aquifex aeolicus

The Protein Data Bank

Gapped BLAST and PSI-BLAST: a new generation of protein database search programs

YPD, PombePD and WormPD: model organism volumes of the BioKnowledge library, an integrated resource for protein information

Pyrobaculum aerophilum sp. nov., a novel nitrate-reducing hyperthermophilic archaeum

The crystal structure of triosephosphate isomerase (TIM) from Thermotoga maritima: a comparative thermostability structural analysis of ten different TIM structures

The crystal structure of adenylosuccinate lyase from Pyrobaculum aerophilum reveals an intracellular protein with three disulfide bonds

Structural basis of the redox switch in the OxyR transcription factor

P304

9679-9684

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

P31

scholarly article

P356

10.1073/PNAS.142310499

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

P407

P433

15

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

P478

99

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

P50

P577

2002-07-09T00:00:00Z

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

P5875

11271716

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

P698

12107280

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

P932

124975

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