Effective cotranslational folding of firefly luciferase without chaperones of the Hsp70 family.
about
Techniques for Screening Translation InhibitorsKinetic analysis of ribosome-bound fluorescent proteins reveals an early, stable, cotranslational folding intermediate.Heterologous protein expression is enhanced by harmonizing the codon usage frequencies of the target gene with those of the expression host.YB-1 promotes microtubule assembly in vitro through interaction with tubulin and microtubules.Mitochondria-targeted antioxidants as highly effective antibiotics.Cotranslational folding increases GFP folding yieldMadumycin II inhibits peptide bond formation by forcing the peptidyl transferase center into an inactive state.Chaperones rescue luciferase folding by separating its domains.Amicoumacin a inhibits translation by stabilizing mRNA interaction with the ribosomeAttenuation-based dual-fluorescent-protein reporter for screening translation inhibitors.Mechanistic Insight into the Reactivation of BCAII Enzyme from Denatured and Molten Globule States by Eukaryotic Ribosomes and Domain V rRNAsComparing the functional properties of the Hsp70 chaperones, DnaK and BiP.Kinetic analysis of β-galactosidase and β-glucuronidase tetramerization coupled with protein translationN-terminal domains of native multidomain proteins have the potential to assist de novo folding of their downstream domains in vivo by acting as solubility enhancersUnraveling co-translational protein folding: Concepts and methods.Binding and Action of Amino Acid Analogs of Chloramphenicol upon the Bacterial Ribosome.Competing Pathways and Multiple Folding Nuclei in a Large Multidomain Protein, Luciferase.
P2860
Q26746984-D0076CE2-9A48-4D61-B25F-1834BEDE241BQ30155421-0D127DD6-9E25-405D-BA34-EB1F036F43BEQ30369393-DF201AC8-4A2B-4AD6-949F-63DA2D39C801Q33369541-89825CA7-0DDD-482E-B9AF-6943CCA4D207Q33684135-3465A250-83D7-40D2-AF0A-D1D2B14B7B06Q33767764-63F94526-EFD1-4258-9B83-9488517FF78DQ33878132-FD16D166-6638-4254-B496-FD44753C5F0BQ34317468-02ABE4E7-BCC3-46A4-8C14-6EEBEF39A343Q34617861-2DA2A667-49B0-4A83-8B7F-76EF41880683Q35867290-475EDCED-377A-470C-BA63-8FA4C86A4B4CQ35995635-7AC9461B-5EB1-4FB5-9A27-D37E587A4C36Q38504100-7A6254F0-2EE2-4697-BD03-3FDCEA44199BQ42015407-55C1921C-EB91-433A-9656-4A732744F41CQ42020736-98CB195F-C105-4B12-A7A4-63A60E504A5BQ47314016-B5806E16-BF2E-4DBD-9F44-F4DD1CF331EFQ50150775-9E9B9C2B-08D4-428D-89F3-EDE6BF618FE7Q50879283-9BBCDE61-4C57-4115-BDAE-752F747485F8
P2860
Effective cotranslational folding of firefly luciferase without chaperones of the Hsp70 family.
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
Effective cotranslational fold ...... haperones of the Hsp70 family.
@en
Effective cotranslational fold ...... haperones of the Hsp70 family.
@nl
type
label
Effective cotranslational fold ...... haperones of the Hsp70 family.
@en
Effective cotranslational fold ...... haperones of the Hsp70 family.
@nl
prefLabel
Effective cotranslational fold ...... haperones of the Hsp70 family.
@en
Effective cotranslational fold ...... haperones of the Hsp70 family.
@nl
P2093
P2860
P356
P1433
P1476
Effective cotranslational fold ...... haperones of the Hsp70 family.
@en
P2093
Aigar Kommer
Alexander S Spirin
Maxim S Svetlov
Vyacheslav A Kolb
P2860
P304
P356
10.1110/PS.051752506
P577
2005-12-29T00:00:00Z