Zobrazeno 1 - 10
of 37
pro vyhledávání: '"Wallace M. LeStourgeon"'
Publikováno v:
Journal of Molecular Biology. 350:319-337
During active cell division, heterogeneous nuclear ribonucleoprotein (hnRNP) C is one of the most abundant proteins in the nucleus. hnRNP C exists as a stable tetramer that binds about 230 nucleotides of pre-mRNA and functions in vivo to package nasc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::36d453b502fed290aabc340acfd48a42
https://doi.org/10.1016/j.jmb.2005.05.002
https://doi.org/10.1016/j.jmb.2005.05.002
Publikováno v:
Biochemistry. 35:1212-1222
Proteins C1 and C2 together comprise about one-third the protein mass of mammalian core 40S heterogeneous nuclear ribonucleoprotein particles (40S hnRNP) and exist as heterotetramers of (C1)3C2. On the basis of nonequilibrium binding studies, it has
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b0bf73b38ad7469cf85660d94f7b1c49
https://doi.org/10.1021/bi951974k
https://doi.org/10.1021/bi951974k
Autor:
Stephanie J. Northington, Wallace M. LeStourgeon, Mei Huang, Akila Mayeda, J E Rech, Adrian R. Krainer, P F Flicker
Publikováno v:
Molecular and Cellular Biology. 14:518-533
A series of in vitro protein-RNA binding studies using purified native (C1)3C2 and (A2)3B1 tetramers, total soluble heterogeneous nuclear ribonucleoprotein (hnRNP), and pre-mRNA molecules differing in length and sequence have revealed that a single C
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8e64c3b39e58261c5c13d5d860cae297
https://doi.org/10.1128/mcb.14.1.518
https://doi.org/10.1128/mcb.14.1.518
Publikováno v:
Molecular and Cellular Biology. 11:864-871
The six "core" proteins of HeLa cell 40S nuclear ribonucleoprotein particles (hnRNP particles) package 700-nucleotide lengths of pre-mRNA into a repeating array of regular particles. We have previously shown that the C proteins exist as anisotropic t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6f95b0f6822788e393f2d08aad870625
https://doi.org/10.1128/mcb.11.2.864
https://doi.org/10.1128/mcb.11.2.864
Autor:
Wallace M. LeStourgeon, Jia-huai Tan
Publikováno v:
eLS
During transcription in higher eukaryotes, the elongating pre-messenger RNA is bound by a unique set of abundant nuclear proteins to form a repeating array of 20–22-nm particles termed 30–40S heterogeneous nuclear ribonucleoprotein (hnRNP) partic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c1157460ccc5ef656ce738ed8d842b16
https://doi.org/10.1038/npg.els.0002603
https://doi.org/10.1038/npg.els.0002603
Publikováno v:
Journal of molecular biology. 305(4)
Previous studies have shown that the C protein of 40 S hnRNP complexes contains a leucine-zipper domain, residues 180-207, and that a 40 residue highly basic domain, immediately preceding the zipper, is responsible for almost all of the free energy o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::197b120fec1581d1f7ad652d3b3d47a5
https://pubmed.ncbi.nlm.nih.gov/11162094
https://pubmed.ncbi.nlm.nih.gov/11162094
Autor:
Lillian Shahied, Jia-huai Tan, Jun Li, Yuji Kajiwara, Wallace M. LeStourgeon, James G. McAfee
Publikováno v:
Journal of molecular biology. 305(4)
The hnRNP C protein tetramer cooperatively binds 230 nt increments of pre-mRNA in vitro in a salt-resistant manner and is located along the length of vertebrate transcripts in vivo . Based on these and other findings it has been suggested that hnRNP
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9640fc4c1e9dd2df3d3b80450f511315
https://pubmed.ncbi.nlm.nih.gov/11162095
https://pubmed.ncbi.nlm.nih.gov/11162095
Publikováno v:
Molecular biology of the cell. 11(5)
The behavior of nuclear pre-mRNA-binding proteins after their nuclease and/or salt-induced release from RNA was investigated. After RNase digestion or salt extraction, two proteins that initially exist as tetramers (A2)3B1 in isolated heterogeneous n
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dcc6de3873ddf33b2b0a5d36c504eed0
https://pubmed.ncbi.nlm.nih.gov/10793134
https://pubmed.ncbi.nlm.nih.gov/10793134
Publikováno v:
The Journal of biological chemistry. 273(33)
Based on UV cross-linking experiments, it has been reported that the C protein tetramer of 40 S heterogeneous nuclear ribonucleoprotein complexes specifically interacts with stem-loop I of U2 small nuclear RNA (snRNA) (Temsamani, J., and Pederson, T.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::87f18eb66a559293b6785c0935602430
https://pubmed.ncbi.nlm.nih.gov/9694897
https://pubmed.ncbi.nlm.nih.gov/9694897
Publikováno v:
Journal of structural biology. 114(2)
In mammalian cells approximately 700 nucleotide lengths of pre-mRNA are packaged during transcription by a unique group of abundant nuclear proteins to form a repeating array of regular ribonucleoprotein complexes termed 30-40S heterogeneous nuclear
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d76eaf49072b00cefc7aeb6ff8ffafd5
https://pubmed.ncbi.nlm.nih.gov/7542018
https://pubmed.ncbi.nlm.nih.gov/7542018