A protein residing at the subunit interface of the bacterial ribosome
about
Ribosomal proteins mediate the hepatitis C virus IRES-HeLa 40S interactionRibosome-associated factor Y adopts a fold resembling a double-stranded RNA binding domain scaffoldStructure ofVibrio choleraeribosome hibernation promoting factorHow Hibernation Factors RMF, HPF, and YfiA Turn Off Protein SynthesisRibosome binding proteins YhbH and YfiA have opposite functions during 100S formation in the stationary phase of Escherichia coliStructural basis for the control of translation initiation during stressLactococcus lactis YfiA is necessary and sufficient for ribosome dimerizationOver 1000 genes are involved in the DNA damage response of Escherichia coliThe plastid ribosomal proteins. Identification of all the proteins in the 50 S subunit of an organelle ribosome (chloroplast).RNase activity of polynucleotide phosphorylase is critical at low temperature in Escherichia coli and is complemented by RNase IIDNA microarray-mediated transcriptional profiling of the Escherichia coli response to hydrogen peroxide.Semiquantitative proteomic analysis of the human spliceosome via a novel two-dimensional gel electrophoresis methodQuantitative proteome profiling of C. burnetii under tetracycline stress conditions.The bacterial translation stress response.Characterization of hibernating ribosomes in mammalian cells.The VrrA sRNA controls a stationary phase survival factor Vrp of Vibrio cholerae.Control and regulation of the cellular responses to cold shock: the responses in yeast and mammalian systems.Involvement of cyclic AMP receptor protein in regulation of the rmf gene encoding the ribosome modulation factor in Escherichia coliThe weird and wonderful world of bacterial ribosome regulation.Adaptation of enteropathogenic Yersinia to low growth temperature.Role of the ribosome-associated protein PY in the cold-shock response of Escherichia coli.Multiple effects of S13 in modulating the strength of intersubunit interactions in the ribosome during translation.Optimization of a ribosomal structural domain by natural selection.The Escherichia coli Cpx envelope stress response regulates genes of diverse function that impact antibiotic resistance and membrane integrityA general mechanism of ribosome dimerization revealed by single-particle cryo-electron microscopyThe cryo-EM structure of hibernating 100S ribosome dimer from pathogenic Staphylococcus aureusThe Cyanobacterial Ribosomal-Associated Protein LrtA Is Involved in Post-Stress Survival in Synechocystis sp. PCC 6803.Ribosome-associated protein that inhibits translation at the aminoacyl-tRNA binding stageThe sarcin-ricin loop of 23S rRNA is essential for assembly of the functional core of the 50S ribosomal subunit.Proteomic identification of all plastid-specific ribosomal proteins in higher plant chloroplast 30S ribosomal subunit.Ribosomal protein S1 from Thermus thermophilus: its detection, identification and overproduction.Role of 100S ribosomes in bacterial decay period.SsTypA1, a chloroplast-specific TypA/BipA-type GTPase from the halophytic plant Suaeda salsa, plays a role in oxidative stress tolerance.Role of HPF (hibernation promoting factor) in translational activity in Escherichia coli.The how and Y of cold shock.Lso2 is a conserved ribosome-bound protein required for translational recovery in yeast
P2860
Q27472964-9CFF1563-AE07-4208-AE9C-067191D1E645Q27639870-E782A1E9-02F3-44E6-8E9B-E33C55029600Q27676970-45B396E3-A6A8-42B3-A1E9-85F8FA118B3EQ27679167-2C0F963B-5214-4DE7-80E9-FB8FEF2870B8Q28284860-621FCF60-F940-47AE-8683-C1681F06CC7AQ28289449-1F2B1865-0C55-425C-AB47-6A625EFC370CQ28302827-89B7054D-89C8-432E-972E-E457ABB474D7Q28611182-7DA7C3C2-83AE-404D-A0ED-ED48626A18EAQ30883203-86428C4A-B174-40DF-9DBC-5B0ADAC0064DQ33349686-15686EAC-9763-4E33-92C7-D89B281231F9Q33996654-79AFB7AF-127D-4BBB-BC50-4A4F3D0723F4Q34181884-A8D7FF6A-FBA4-42A9-B5AD-993858040592Q34206345-2BA70A8C-454B-4B76-8362-71A2396CAE60Q34490409-977FC1C2-BC6A-4DBE-B767-B1E590985B23Q35559950-CAA167C7-CE84-4017-8EA5-54D289B21CAEQ36191630-5A4DD18F-1FCE-4B7C-8AE1-46F121C7604AQ36515340-5CD433E8-D628-45C5-845B-876EAC0BCF52Q36833067-5BAE9ED1-3CFC-4748-9304-77950A20DF15Q36846903-968D85B9-2B8B-44AF-BB47-65482BF30996Q37678398-463602BF-0AF9-4EC3-85BD-4F76194E2410Q40014077-8F5A378C-80BE-442C-A023-832A13B3E30DQ40690983-711E40D8-3630-440F-A2ED-E22F904327A6Q41374826-2D4D00AD-0200-4533-BE4A-80E9EEF79250Q41445473-02EE3C99-8223-4D7C-8188-BFB06CAC5B17Q41596245-23124295-2B6D-4F85-8B7B-F2C0F7730447Q41596253-EAF92DCE-5F5B-43B5-9CE0-9403A0797B08Q41902961-C63384B4-2DF6-4500-B00D-7775EB484EFBQ41915699-7AD26FDD-F6AF-4242-BA16-B0D18D16DCB2Q42909062-433FD531-AA88-4596-B881-10C8E2BE911FQ48258012-E9132D0A-6BF8-437D-85E1-500EDEEA89A2Q48289270-8510AF31-EAA5-45D8-87E3-AE0B619DA196Q50248433-A301ED3F-2EA7-4FB0-A9DD-3C614CCFD7A6Q50640614-2C178366-7E0F-4DFA-A139-4905D69A7DA2Q54428443-C0C96D03-1E26-4F99-8533-B4223DD75CE7Q54496600-9AEAE7F8-30FE-4A2D-950B-059DAA50E2E0Q58748104-8514332E-3C50-4DA4-83AD-418C057D791B
P2860
A protein residing at the subunit interface of the bacterial ribosome
description
1999 nî lūn-bûn
@nan
1999 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հոտեմբերին 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
A protein residing at the subunit interface of the bacterial ribosome
@ast
A protein residing at the subunit interface of the bacterial ribosome
@en
A protein residing at the subunit interface of the bacterial ribosome
@nl
type
label
A protein residing at the subunit interface of the bacterial ribosome
@ast
A protein residing at the subunit interface of the bacterial ribosome
@en
A protein residing at the subunit interface of the bacterial ribosome
@nl
prefLabel
A protein residing at the subunit interface of the bacterial ribosome
@ast
A protein residing at the subunit interface of the bacterial ribosome
@en
A protein residing at the subunit interface of the bacterial ribosome
@nl
P2093
P2860
P3181
P356
P1476
A protein residing at the subunit interface of the bacterial ribosome
@en
P2093
A S Spirin
D E Agafonov
I V Nazimov
P2860
P304
P3181
P356
10.1073/PNAS.96.22.12345
P407
P577
1999-10-26T00:00:00Z