A highly purified, fluorescently labeled in vitro translation system for single-molecule studies of protein synthesis.
about
smFRET studies of the 'encounter' complexes and subsequent intermediate states that regulate the selectivity of ligand bindingRibosomal initiation complex-driven changes in the stability and dynamics of initiation factor 2 regulate the fidelity of translation initiationEttA regulates translation by binding the ribosomal E site and restricting ribosome-tRNA dynamicsThe ABC-F protein EttA gates ribosome entry into the translation elongation cycleChemical biology-based approaches on fluorescent labeling of proteins in live cells.Transfer RNA-mediated regulation of ribosome dynamics during protein synthesis.The ribosome can discriminate the chirality of amino acids within its peptidyl-transferase center.Protein synthesis during cellular quiescence is inhibited by phosphorylation of a translational elongation factor.A dynamic RNA loop in an IRES affects multiple steps of elongation factor-mediated translation initiation.In vitro and in vivo single-molecule fluorescence imaging of ribosome-catalyzed protein synthesisTranslation initiation factor 3 regulates switching between different modes of ribosomal subunit joining.Conformational selection of translation initiation factor 3 signals proper substrate selection.Peptide release promoted by methylated RF2 and ArfA in nonstop translation is achieved by an induced-fit mechanismA conformational switch in initiation factor 2 controls the fidelity of translation initiation in bacteria.Ensemble and single-molecule FRET studies of protein synthesis.Dynamics of ribosomes and release factors during translation termination in E. coli.A guide to large-scale RNA sample preparation.
P2860
Q26864185-F2D93047-C2FA-494D-B571-72532BA518F8Q27309781-06347FB7-C295-41EA-B8CB-A2AD9D753350Q27681174-DA1A07C5-5836-4A6A-AE6A-A5D074C75217Q27681176-E025666D-1B99-421E-9BB5-1E114E6A138BQ34322508-68CBFC6E-642E-47EA-A985-32930C2F0AEEQ35199307-884593CF-917C-4DE9-B971-1229CAFAA28DQ35616176-D49767B1-299A-4C2C-A857-EED09A0B52AAQ35796219-3AD20E57-CAFE-4BA5-82B2-C009CBF00EF8Q36452412-3E037EFE-51A0-4DD4-9B2C-4C5828CFB323Q36495638-358FF3AA-1E5A-40DB-8EA4-B5DA09DA9631Q36654612-5CA43FCB-76D9-4601-89C0-720739C26815Q36828472-C3919206-7204-4801-9A1D-1CE433BB3B01Q40338352-D4ED4281-2582-4BA0-B7CD-2CBB20523E70Q47131408-25FC9226-8C8C-43E4-B686-42F5FD9F305AQ47286270-CB9D52F7-4070-41CF-AF88-4AF85BCF6B22Q55043309-9F9BAF49-E39F-42EF-B389-256A191C7B2AQ55048841-4ED823C0-92F1-4711-8E35-042107631772
P2860
A highly purified, fluorescently labeled in vitro translation system for single-molecule studies of protein synthesis.
description
2010 nî lūn-bûn
@nan
2010年の論文
@ja
2010年学术文章
@wuu
2010年学术文章
@zh-cn
2010年学术文章
@zh-hans
2010年学术文章
@zh-my
2010年学术文章
@zh-sg
2010年學術文章
@yue
2010年學術文章
@zh
2010年學術文章
@zh-hant
name
A highly purified, fluorescent ...... studies of protein synthesis.
@en
type
label
A highly purified, fluorescent ...... studies of protein synthesis.
@en
prefLabel
A highly purified, fluorescent ...... studies of protein synthesis.
@en
P2093
P2860
P1476
A highly purified, fluorescent ...... studies of protein synthesis.
@en
P2093
Daniel D MacDougall
Dileep K Pulukkunat
Jiangning Wang
Jingyi Fei
Margaret M Elvekrog
Michael T Englander
Ruben L Gonzalez
Samuel H Sternberg
P2860
P304
P356
10.1016/S0076-6879(10)72008-5
P407
P577
2010-01-01T00:00:00Z