Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Alec E, Hodel"'
Publikováno v:
Journal of Biological Chemistry. 282:33968-33976
The vertebrate nucleoporin Nup98 can be expressed in two distinct forms from differentially spliced mRNAs, either as a 98-kDa protein or as the 195-kDa Nup98/Nup96 polyprotein. Both forms undergo autoproteolytic processing to generate the 90-kDa Nup9
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b05c8ed5e196546e0341d221711100cb
https://doi.org/10.1074/jbc.m707911200
https://doi.org/10.1074/jbc.m707911200
Autor:
Mary Elizabeth Harben, Alec E. Hodel, Kanika F. Pulliam, Keith M. Berland, Mary R. Hodel, Jordan S. Holmes, Michelle T. Harreman, Anita H. Corbett
Publikováno v:
Journal of Biological Chemistry. 281:23545-23556
Nuclear localization signals (NLSs) target proteins into the nucleus through mediating interactions with nuclear import receptors. Here, we perform a quantitative analysis of the correlation between NLS receptor affinity and the steady-state distribu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1646cfaca8f883db765450e362041260
https://doi.org/10.1074/jbc.m601718200
https://doi.org/10.1074/jbc.m601718200
Publikováno v:
Journal of Biological Chemistry. 278:41947-41953
Classical protein import, mediated by the binding of a classical nuclear localization signal (NLS) to the NLS receptor, karyopherin/importin alpha, is the most well studied nuclear transport process. Classical NLSs are either monopartite sequences th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c07d3e4372ef363e6f4b29d65ad061f5
https://doi.org/10.1074/jbc.m307162200
https://doi.org/10.1074/jbc.m307162200
Publikováno v:
Journal of Biological Chemistry. 278:5854-5863
Proteins that contain a classical nuclear localization signal (NLS) are recognized in the cytoplasm by a heterodimeric import receptor composed of importin/karyopherin alpha and beta. The importin alpha subunit recognizes classical NLS sequences, and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::988ca25281a4f09be33c23b3909606a1
https://doi.org/10.1074/jbc.m210951200
https://doi.org/10.1074/jbc.m210951200
Autor:
Mary R. Hodel, Krista M. Hennig, Maureen A. Powers, Alec E. Hodel, Eric R. Griffis, Songli Xu, Gary A. Ratner
Publikováno v:
Molecular Cell. 10:347-358
Nup98 is a component of the nuclear pore that plays its primary role in the export of RNAs. Nup98 is expressed in two forms, derived from alternate mRNA splicing. Both forms are processed into two peptides through autoproteolysis mediated by the C-te
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::be5fe1c38f4d4f51930f99742eca1539
https://doi.org/10.1016/s1097-2765(02)00589-0
https://doi.org/10.1016/s1097-2765(02)00589-0
Autor:
Jordan W. Thomas, Pi-Chen Hsu, Mary R. Hodel, Curt H. Hagedorn, Alec E. Hodel, Laura J. Taylor
Publikováno v:
Biochemistry. 39:13730-13736
7-Methylguanosine (m(7)G), also known as the mRNA "cap", is used as a molecular tag in eukaryotic cells to mark the 5' end of messenger RNAs. The mRNA cap is required for several key events in gene expression in which the m(7)G moiety is specifically
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7df8c5c41a0119c30330442daf9aa5e2
https://doi.org/10.1021/bi000623p
https://doi.org/10.1021/bi000623p
Publikováno v:
Cell. 85:247-256
VP39 is a bifunctional vaccinia virus protein that acts as both an mRNA cap–specific RNA 2′-O-methyltransferase and a poly(A) polymerase processivity factor. Here, we report the 1.85 A crystal structure of a VP39 variant complexed with its AdoMet
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cddb6a3b0578092dbe1f630059cec477
https://doi.org/10.1016/s0092-8674(00)81101-0
https://doi.org/10.1016/s0092-8674(00)81101-0
Autor:
M. Beth Harben, Trisha M. Kline, Michelle T. Harreman, Anita H. Corbett, Alec E. Hodel, Heidi G. Milford
Publikováno v:
The Journal of biological chemistry. 279(20)
Many important regulatory proteins, including cell cycle regulators and transcription factors, contain a phosphorylation site within or adjacent to a classic nuclear localization signal (NLS) sequence. Previous studies show that the nuclear localizat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::87232233d5c3d459b5dfc8c52bd18e8c
https://pubmed.ncbi.nlm.nih.gov/14998990
https://pubmed.ncbi.nlm.nih.gov/14998990
Publikováno v:
The Journal of biological chemistry. 278(43)
Classical protein import, mediated by the binding of a classical nuclear localization signal (NLS) to the NLS receptor, karyopherin/importin alpha, is the most well studied nuclear transport process. Classical NLSs are either monopartite sequences th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::9004a11a325d1dcb93aca2ad5cfc9e9b
https://pubmed.ncbi.nlm.nih.gov/12917403
https://pubmed.ncbi.nlm.nih.gov/12917403
Autor:
Michelle T. Harreman, Alec E. Hodel, Glyn J. Truscott, Mary R. Hodel, Pamela E. Cohen, Anita H. Corbett
Publikováno v:
The Journal of biological chemistry. 278(24)
Protein cargoes that contain a classic nuclear localization signal (NLS) are transported into the nucleus through binding to a heterodimeric receptor comprised of importin/karyopherin alpha and beta. An evolutionarily conserved auto-inhibitory sequen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::81cf7b16249f088ca7c3625fa9420d77
https://pubmed.ncbi.nlm.nih.gov/12672802
https://pubmed.ncbi.nlm.nih.gov/12672802