Structure in solution of the major cold-shock protein from Bacillus subtilis
about
A novel heterogeneous nuclear ribonucleoprotein-like protein interacts with NS1 of the minute virus of miceRalA interacts with ZONAB in a cell density-dependent manner and regulates its transcriptional activityunr, a cellular cytoplasmic RNA-binding protein with five cold-shock domains, is required for internal initiation of translation of human rhinovirus RNAAnalysis of the RNA-recognition motif and RS and RGG domains: conservation in metazoan pre-mRNA splicing factorsCrystal structure of inorganic pyrophosphatase from Thermus thermophilusSolution NMR structure of the cold-shock protein from the hyperthermophilic bacterium Thermotoga maritimaCommon mode of DNA binding to cold shock domains. Crystal structure of hexathymidine bound to the domain-swapped form of a major cold shock protein from Bacillus caldolyticusStructure of the cold-shock domain protein fromNeisseria meningitidisreveals a strand-exchanged dimerRNA single strands bind to a conserved surface of the major cold shock protein in crystals and solutionSolution structure of the single-stranded DNA binding protein of the filamentous Pseudomonas phage Pf3: similarity to other proteins binding to single-stranded nucleic acidsNMR solution structure of a dsRNA binding domain from Drosophila staufen protein reveals homology to the N-terminal domain of ribosomal protein S5Crystal structure of CspA, the major cold shock protein of Escherichia coliCold-shock induction of a family of TIP1-related proteins associated with the membrane in Saccharomyces cerevisiae.Characterization of the gene for dbpA, a family member of the nucleic-acid-binding proteins containing a cold-shock domainMolecular determinants for the complex formation between the retinoblastoma protein and LXCXE sequencesCold shock stress-induced proteins in Bacillus subtilisIn the absence of the mouse DNA/RNA-binding protein MSY2, messenger RNA instability leads to spermatogenic arrestUnusual dimerization of a BcCsp mutant leads to reduced conformational dynamics.Similarity and difference in the unfolding of thermophilic and mesophilic cold shock proteins studied by molecular dynamics simulationsAcquisition of double-stranded DNA-binding ability in a hybrid protein between Escherichia coli CspA and the cold shock domain of human YB-1.Cloning, overexpression, purification, and physicochemical characterization of a cold shock protein homolog from the hyperthermophilic bacterium Thermotoga maritima.The CspA family in Escherichia coli: multiple gene duplication for stress adaptation.The structure of the translational initiation factor IF1 from E.coli contains an oligomer-binding motif.Extremely rapid protein folding in the absence of intermediates.Solution NMR structure of the major cold shock protein (CspA) from Escherichia coli: identification of a binding epitope for DNA.Overview of protein structural and functional folds."Fuzzy oil drop" model verified positivelyPathogenic Yersinia species carry a novel, cold-inducible major cold shock protein tandem gene duplication producing both bicistronic and monocistronic mRNA.Formation of amyloid fibrils by peptides derived from the bacterial cold shock protein CspBRNA binding and chaperone activity of the E. coli cold-shock protein CspA.Redesign of a WW domain peptide for selective recognition of single-stranded DNA.Identification and developmental characterization of a novel Y-box protein from Drosophila melanogasterCoping with the cold: the cold shock response in the Gram-positive soil bacterium Bacillus subtilis.Transcription antitermination by translation initiation factor IF1.Diffusion control in an elementary protein folding reaction.Probing the protein-folding mechanism using denaturant and temperature effects on rate constantsRNA remodeling and gene regulation by cold shock proteinsMechanisms of Lin28-mediated miRNA and mRNA regulation--a structural and functional perspective.Mutational analysis of the putative nucleic acid-binding surface of the cold-shock domain, CspB, revealed an essential role of aromatic and basic residues in binding of single-stranded DNA containing the Y-box motif.RNA-binding strategies common to cold-shock domain- and RNA recognition motif-containing proteins.
P2860
Q22008520-E9CB4BED-6C56-4B0E-AD46-AFE0F5DC5D50Q24557505-BA2CD8D4-BE11-444B-BD31-CB55CEEAC387Q24608002-DC4E9893-994A-4869-B13A-963692AD8B91Q24629832-FD0069B8-0CE4-4A2D-A4DC-CABB7C08D4E8Q24675476-B36F509C-5FE8-4875-B1AE-44315CA5A97AQ27631380-8AC6EF40-99F4-470B-913C-D7623E9A8FF2Q27643708-DF8D9DEC-CFDE-4414-9F2C-21BAD0DFAC69Q27650256-ADCEB480-A152-48CD-BA90-404CE6086E43Q27675881-A99DCB14-C92D-4748-89DD-E2CE816E0973Q27729479-7F975CBB-AE9B-42E1-AF76-9D357880107AQ27729790-57315C9C-2F42-4E7B-AD55-984FCDA2E368Q27731411-40634883-02E0-4CCF-94FC-488B90641536Q27937389-58854E36-6935-4066-ACF7-B3A843378CA6Q28116670-AAE240E0-320A-47AE-87D0-0902E9798D16Q28268668-7512BA68-1C55-4416-A299-E172F82A479FQ28488921-53DF4FC0-5536-4A26-A4AA-1B999AB347CEQ28591769-381D7511-217B-468E-8274-030546E020D2Q30152637-FF702E14-BCB8-41F7-A326-B94959F408C9Q30159730-58AAD755-4882-497D-A057-F284FCD71AF3Q30168640-B4E88CB5-CDF6-463D-9036-C80340AF2436Q30175861-48F08DCC-B595-46B9-985B-5D640ED63FB1Q30176280-C38BECA3-6450-4CAB-9BC4-3BB0B092B8B8Q30176601-C9C64CB6-B008-4D2A-8414-F3BCD84E3830Q30193236-87007D56-C546-43D2-9099-C7F0CAFDBA7EQ30194318-FFAD8E8F-8BAE-44F0-8E52-2BE67A176362Q30368988-EA2D3E54-EC87-4130-A161-A2372F271B3DQ30400505-34CB975E-1E56-49DB-BD9D-FB1EC9FDEBCCQ30788563-95A8C476-860A-4B95-BB99-B7D477105E68Q33178598-5D1A2A09-2935-4692-92E2-B24C9B0F73E3Q33580316-85E04D2D-E4A6-4A5C-8D3B-3A8D45E8B484Q33754576-D2553B67-B719-4EB2-BD09-01C26B069707Q34646040-FB06F380-BC77-4C00-83FE-702CC37D7404Q34780391-7A0B63FB-3546-47E9-AD30-423AA4D9C79AQ35879284-2624295A-7D70-4283-A8A6-4BC2387BB64CQ36153029-2E20E732-17A0-4393-94C2-233DBD4FD087Q37240517-DC0555CD-EAA7-458A-9A83-52EBD95B3005Q37806516-E92D09B7-A4CE-41F8-B2A8-9217A8EE9422Q38128506-4ECE86E4-F38B-46A7-B9A1-0CAFE692DA04Q38296241-BEA65B6F-4EDB-4630-98DC-4A210CAABE1DQ38300395-50332639-B397-4ADD-8FA9-E10B31E599E5
P2860
Structure in solution of the major cold-shock protein from Bacillus subtilis
description
1993 nî lūn-bûn
@nan
1993 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1993 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
name
Structure in solution of the major cold-shock protein from Bacillus subtilis
@ast
Structure in solution of the major cold-shock protein from Bacillus subtilis
@en
Structure in solution of the major cold-shock protein from Bacillus subtilis
@nl
type
label
Structure in solution of the major cold-shock protein from Bacillus subtilis
@ast
Structure in solution of the major cold-shock protein from Bacillus subtilis
@en
Structure in solution of the major cold-shock protein from Bacillus subtilis
@nl
prefLabel
Structure in solution of the major cold-shock protein from Bacillus subtilis
@ast
Structure in solution of the major cold-shock protein from Bacillus subtilis
@en
Structure in solution of the major cold-shock protein from Bacillus subtilis
@nl
P2093
P356
P1433
P1476
Structure in solution of the major cold-shock protein from Bacillus subtilis
@en
P2093
A Schnuchel
G Willimsky
M A Marahiel
P Graumann
R Wiltscheck
P2888
P304
P356
10.1038/364169A0
P407
P577
1993-07-08T00:00:00Z
P6179
1032221991