A cradle for new proteins: trigger factor at the ribosome.
about
Microscale to manufacturing scale-up of cell-free cytokine production--a new approach for shortening protein production development timelinesChemical and biological approaches for adapting proteostasis to ameliorate protein misfolding and aggregation diseases: progress and prognosisPpiD is a player in the network of periplasmic chaperones in Escherichia coli.Molecular Determinants of Mutant Phenotypes, Inferred from Saturation Mutagenesis DataIdentification of a potential hydrophobic peptide binding site in the C-terminal arm of trigger factor.Structure of trigger factor binding domain in biologically homologous complex with eubacterial ribosome reveals its chaperone actionMegadalton complexes in the chloroplast stroma of Arabidopsis thaliana characterized by size exclusion chromatography, mass spectrometry, and hierarchical clusteringAglycosylated antibodies and antibody fragments produced in a scalable in vitro transcription-translation system.Expression and purification of the functional ectodomain of human anthrax toxin receptor 2 in Escherichia coli Origami B cells with assistance of bacterial Trigger FactorAssociation of protein biogenesis factors at the yeast ribosomal tunnel exit is affected by the translational status and nascent polypeptide sequence.Trigger factor from the psychrophilic bacterium Psychrobacter frigidicola is a monomeric chaperonePhenotypic and genetic consequences of protein damage.A homolog of Bacillus subtilis trigger factor in Listeria monocytogenes is involved in stress tolerance and bacterial virulence.Expression and in vitro functional analyses of recombinant Gam1 proteinComprehensive analysis of the effects of Escherichia coli ORFs on protein translation reactionTransmembrane segments form tertiary hairpins in the folding vestibule of the ribosome.Integrating protein homeostasis strategies in prokaryotes.Chaperone discovery.Production of prone-to-aggregate proteins.Structure and function of glycosylated tandem repeats from Candida albicans Als adhesins.The Mechanism and Function of Group II Chaperonins.Repair or destruction-an intimate liaison between ubiquitin ligases and molecular chaperones in proteostasisIdentification of nascent chain interaction sites on trigger factor.Targeted protein degradation by Salmonella under phagosome-mimicking culture conditions investigated using comparative peptidomics.Production and characterization of neurosecretory protein GM using Escherichia coli and Chinese Hamster Ovary cells.Altered Co-Translational Processing Plays a Role in Huntington's Pathogenesis-A Hypothesis.Versatility of trigger factor interactions with ribosome-nascent chain complexes.Quantifying epistatic interactions among the components constituting the protein translation systemStress responses of Acinetobacter strain Y during phenol degradation.Expression Profiling of Ribosomal Protein Gene Family in Dehydration Stress Responses and Characterization of Transgenic Rice Plants Overexpressing RPL23A for Water-Use Efficiency and Tolerance to Drought and Salt Stresses.Metagenomic and metaproteomic analyses of Accumulibacter phosphatis-enriched floccular and granular biofilm.Activation tagging in indica rice identifies ribosomal proteins as potential targets for manipulation of water-use efficiency and abiotic stress tolerance in plants.
P2860
Q24599175-B72C8D60-D07B-4E70-9098-D0D7DA7EA4C0Q27004511-79E40C7B-AEB1-4BFD-992D-283A29778846Q30156004-92CBF17F-8D25-4481-B289-BD31C3056525Q31123704-242D028C-2081-4348-BF27-A1E86ABB3963Q33285751-95430919-38A1-416D-A336-137E40C74F5FQ33913724-D3CED8D0-21FF-4EBA-A92F-699FB3318B87Q34122093-BD1C753F-D66B-438F-8598-CA683D796413Q34179215-F20BC1D3-0C93-4E66-962B-EE23ABDF970AQ34462631-E1C4303E-16B8-41C0-9E84-F5D8366CFB4AQ34603048-639CDFA9-3227-4865-98F7-5139C24B9D58Q34896951-35B75E1B-6510-4C6B-9DB2-59EC450FE4B3Q34998365-8FD2E309-F307-49BF-B46B-968CE1748CC4Q35091824-D7CA2183-0A7D-4486-A468-989E148D1341Q35449374-15D67922-FF4A-4315-ACC5-3EF439122154Q36818147-F3084095-3CB9-4D1D-99DB-BFE8BD251BC7Q37412726-2B989324-DDBE-47DA-9D67-45A9F3D67B62Q37858328-D13AA3D9-9BB1-4F03-87CD-35CDE8653327Q38042579-BE45CECA-FDA7-4727-B1A0-15BF68C3EA27Q38161235-06CA6450-6E32-49FF-A422-7BCA9B0DFC42Q38349717-80D1A01B-59A1-4204-BC53-924E48D3EAEAQ38455984-4ACB9820-F9D7-4EFA-AD0A-D16B7CD75BCFQ39430414-BF54054D-9222-4E7E-BB21-94D07465CB13Q40171796-A6691231-7C1B-4370-B011-9FD67FC54F29Q40460045-FFBC6C99-F973-4828-9CFB-38CE63FCAD89Q41788499-8159A5B4-CF50-4F28-BD4E-6E867D6BF85FQ41851500-6E8DD8F2-39C9-4752-90D8-405C68FA4A7AQ42430469-C9541B2A-4D66-405D-8335-B8DD31D47915Q42543353-57D930EB-581E-45C6-B2C4-B6DF2AC072CCQ46472735-79BC8720-F86E-44D0-85D7-EF409F94F1D6Q47119074-29F0EF02-96A5-4627-A95C-EA1512C2FF39Q48145763-0D7B5960-CCE0-4BE7-88DC-CA411AAD68F4Q51250422-1F8076CF-97CA-4DE9-8C77-CA6936E3686D
P2860
A cradle for new proteins: trigger factor at the ribosome.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
2005年论文
@zh
2005年论文
@zh-cn
name
A cradle for new proteins: trigger factor at the ribosome.
@ast
A cradle for new proteins: trigger factor at the ribosome.
@en
type
label
A cradle for new proteins: trigger factor at the ribosome.
@ast
A cradle for new proteins: trigger factor at the ribosome.
@en
prefLabel
A cradle for new proteins: trigger factor at the ribosome.
@ast
A cradle for new proteins: trigger factor at the ribosome.
@en
P1476
A cradle for new proteins: trigger factor at the ribosome.
@en
P2093
Lars Ferbitz
Timm Maier
P304
P356
10.1016/J.SBI.2005.03.005
P577
2005-04-01T00:00:00Z