Unfolding of DNA quadruplexes induced by HIV-1 nucleocapsid protein.Crystal structure of tetrameric form of human lysyl-tRNA synthetase: Implications for multisynthetase complex formationEvolutionary conservation of a functionally important backbone phosphate group critical for aminoacylation of histidine tRNAs.Pre-transfer editing by class II prolyl-tRNA synthetase: role of aminoacylation active site in "selective release" of noncognate amino acids.The interaction between HIV-1 Gag and human lysyl-tRNA synthetase during viral assemblyAn isolated class II aminoacyl-tRNA synthetase insertion domain is functional in amino acid editingInability of human immunodeficiency virus type 1 produced in murine cells to selectively incorporate primer formula.Insights on the role of nucleic acid/protein interactions in chaperoned nucleic acid rearrangements of HIV-1 reverse transcription.Cyclic peptide inhibitors of HIV-1 capsid-human lysyl-tRNA synthetase interactionA capillary electrophoretic method for monitoring the presence of alpha-tubulin in nuclear preparations.Electrophoretic behavior of individual nuclear species as determined by capillary electrophoresis with laser-induced fluorescence detection.RiboCAT: a new capillary electrophoresis data analysis tool for nucleic acid probing.Capillary electrophoretic separation of nuclei released from single cells.Nuclear localization of aminoacyl-tRNA synthetases using single-cell capillary electrophoresis laser-induced fluorescence analysis.C-terminal domain modulates the nucleic acid chaperone activity of human T-cell leukemia virus type 1 nucleocapsid protein via an electrostatic mechanism.The Arabidopsis thaliana tandem zinc finger 1 (AtTZF1) protein in RNA binding and decay.Distinct nucleic acid interaction properties of HIV-1 nucleocapsid protein precursor NCp15 explain reduced viral infectivity.Mechanistic differences between nucleic acid chaperone activities of the Gag proteins of Rous sarcoma virus and human immunodeficiency virus type 1 are attributed to the MA domain.Specific zinc-finger architecture required for HIV-1 nucleocapsid protein's nucleic acid chaperone function.Resampling and editing of mischarged tRNA prior to translation elongation.Secondary structure and secondary structure dynamics of DNA hairpins complexed with HIV-1 NC proteinComparative analysis of RNA/protein dynamics for the arginine-rich-binding motif and zinc-finger-binding motif proteins encoded by HIV-1.Single-molecule FRET studies of important intermediates in the nucleocapsid-protein-chaperoned minus-strand transfer step in HIV-1 reverse transcription.Retrovirus-specific packaging of aminoacyl-tRNA synthetases with cognate primer tRNAs.Efficient aminoacylation of the tRNA(Ala) acceptor stem: dependence on the 2:71 base pairRetrovirus-specific differences in matrix and nucleocapsid protein-nucleic acid interactions: implications for genomic RNA packagingMatrix domain modulates HIV-1 Gag's nucleic acid chaperone activity via inositol phosphate binding.Features of double-stranded RNA-binding domains of RNA helicase A are necessary for selective recognition and translation of complex mRNAsSingle aromatic residue location alters nucleic acid binding and chaperone function of FIV nucleocapsid protein.Role of HIV-1 nucleocapsid protein in HIV-1 reverse transcription.Diverse interactions of retroviral Gag proteins with RNAs.Substrate-mediated fidelity mechanism ensures accurate decoding of proline codons.Zinc finger-dependent HIV-1 nucleocapsid protein-TAR RNA interactions.Ancestral AlaX editing enzymes for control of genetic code fidelity are not tRNA-specific.FRET analysis reveals distinct conformations of IN tetramers in the presence of viral DNA or LEDGF/p75.Homologous trans-editing factors with broad tRNA specificity prevent mistranslation caused by serine/threonine misactivation.Substrate specificity of bacterial prolyl-tRNA synthetase editing domain is controlled by a tunable hydrophobic pocketRestoring species-specific posttransfer editing activity to a synthetase with a defunct editing domainRole of coupled dynamics in the catalytic activity of prokaryotic-like prolyl-tRNA synthetases.Probing nucleation, reverse annealing, and chaperone function along the reaction path of HIV-1 single-strand transfer
P50
Q24816887-E736DE38-2F74-470D-911E-323D8789A9E8Q27649847-447F405A-C07D-4628-A0B7-8DD35370E07AQ27934571-4F636F6F-E955-4EDC-8EF3-1C0161B67D54Q27939503-07460D6B-C5A1-45C5-B6C1-366F2037A014Q28205104-97119A94-A1FE-4664-B37D-C6B7C749703BQ28484984-48A47765-7176-471C-AB7C-212FF6474921Q30439541-763465C2-33B0-4269-8F51-5A68B4A5C06FQ30499332-BCEAA251-FE53-474A-AFCF-67B5083E7791Q31046491-81340C7B-28B4-4EBE-A384-798714D8B240Q31073847-7FB8B556-C716-47D0-9360-B225D9FDDE90Q31107795-DE347F84-8FDE-4100-8D18-FC40E1D3DFB1Q31141309-4153F275-B671-424C-9497-1372F9E144CBQ33197244-3DC2020D-D657-4FD2-914D-55E61F957580Q33205879-3EE28FD6-A8D4-4D4E-B927-91C207020AA9Q33581258-1CD7104F-7DB2-4636-93C6-575A34F275BEQ33631175-28A5DC6B-D502-4CB3-9416-168D1F2A8616Q33791156-1EF0261B-57D3-4DF7-9958-869BF41B3BF7Q33900316-2DEFC61A-A51C-4AE1-A4D9-F292D3882BADQ34065314-D5C600D5-FD47-44ED-843E-4CFAE1DE9042Q34151351-9054D29B-A660-46EA-B0FC-AB028A7AE7B6Q34187402-85A3B40B-AA4B-44F3-9394-6FEBEC76D856Q34306859-210CA2FC-C7C2-402C-9B7B-CE06E0FE5002Q34351841-4F2E0DF1-1AC4-4716-96D8-AF32B4DA0468Q34353288-9A6C615E-8925-46DC-887E-A3E17365049AQ34364445-CDC1287F-B3FB-46B6-AB5A-C60CFA066102Q34384875-EC9E7DAA-11F9-44ED-A813-BE757A3897ADQ34529887-B00B8235-1132-4C6C-A47E-D346F9577B8FQ34568434-5400FDE7-03E5-4B06-9D67-817E0EB9DBBCQ34614790-4AEBC8F0-0A84-4C44-A4DE-703F657209F1Q34775658-319A840A-D90D-4B4B-91B5-A74BC8887D6BQ35087489-427D1348-FB60-402A-ADA3-45AA1C7DF4D8Q35213173-7356D89D-E0F9-4F0C-B18E-F705BEBEE963Q35222868-F322270E-FF5C-4BE8-8FF4-55F4966DAFDBQ35451324-021A802E-7B62-4A2D-95E5-F5E928532D16Q35468454-062571F4-30B4-423C-9492-E93C80F14CF7Q35616247-C1A7DA19-016E-4C6F-A59F-2BF1FA7F7E9FQ35728198-DA1EC1F8-B42A-426C-9013-82B4E0F772EFQ35844603-A2628704-218C-45A9-B71E-FA3020F69AF7Q35915716-155B3849-DB2E-4433-B002-2A10BA177299Q35921612-530BBC87-F2B0-42F8-A658-C78CAD10DDC2
P50
description
American biochemist and researcher
@en
wetenschapper
@nl
name
Karin Musier-Forsyth
@ast
Karin Musier-Forsyth
@en
Karin Musier-Forsyth
@es
Karin Musier-Forsyth
@nl
Karin Musier-Forsyth
@sl
type
label
Karin Musier-Forsyth
@ast
Karin Musier-Forsyth
@en
Karin Musier-Forsyth
@es
Karin Musier-Forsyth
@nl
Karin Musier-Forsyth
@sl
altLabel
Karin M. Musier-Forsyth
@en
prefLabel
Karin Musier-Forsyth
@ast
Karin Musier-Forsyth
@en
Karin Musier-Forsyth
@es
Karin Musier-Forsyth
@nl
Karin Musier-Forsyth
@sl
P185
P101
P21
P2381
P31
P4012
P496
0000-0002-0354-4172