Literature DB >> 1991319

How proteins enter the nucleus.

P A Silver1.   

Abstract

Nuclear protein import is a selective process. Proteins destined for the nucleus contain NLSs. These short stretches of amino acids interact with proteins located in the cytoplasm, on the nuclear envelope, and/or at the nuclear pore complex. Following binding at the pore complex, proteins are translocated through the pore into the nucleus in a manner requiring ATP. The biochemical dissection of the nuclear pore complex has begun. Alteration of protein import into the nucleus is emerging as a new and complex form of regulation. However, we are left with the following problems: How do proteins move through the cytoplasm to reach the nuclear pore? How does the nuclear pore complex open and close in a selective manner? How is ATP utilized during import? And finally, how is bi-directional traffic of both proteins and RNA through the pore regulated?

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Year:  1991        PMID: 1991319     DOI: 10.1016/0092-8674(91)90233-o

Source DB:  PubMed          Journal:  Cell        ISSN: 0092-8674            Impact factor:   41.582


  192 in total

1.  Influence of metallothionein-1 localization on its function.

Authors:  M Levadoux-Martin; J E Hesketh; J H Beattie; H M Wallace
Journal:  Biochem J       Date:  2001-04-15       Impact factor: 3.857

2.  Different dynamics in nuclear entry of subunits of the repair/transcription factor TFIIH.

Authors:  F Santagati; E Botta; M Stefanini; A M Pedrini
Journal:  Nucleic Acids Res       Date:  2001-04-01       Impact factor: 16.971

3.  Restriction of viral replication by mutation of the influenza virus matrix protein.

Authors:  Teresa Liu; Zhiping Ye
Journal:  J Virol       Date:  2002-12       Impact factor: 5.103

Review 4.  Peroxisome biogenesis in Saccharomyces cerevisiae.

Authors:  W H Kunau; A Hartig
Journal:  Antonie Van Leeuwenhoek       Date:  1992-08       Impact factor: 2.271

5.  Identification of a sporulation-specific promoter regulating divergent transcription of two novel sporulation genes in Saccharomyces cerevisiae.

Authors:  J G Coe; L E Murray; I W Dawes
Journal:  Mol Gen Genet       Date:  1994-09-28

6.  Decreased expression of Mac-2 (carbohydrate binding protein 35) and loss of its nuclear localization are associated with the neoplastic progression of colon carcinoma.

Authors:  M M Lotz; C W Andrews; C A Korzelius; E C Lee; G D Steele; A Clarke; A M Mercurio
Journal:  Proc Natl Acad Sci U S A       Date:  1993-04-15       Impact factor: 11.205

7.  Cytolocalization of zeatin O-xylosyltransferase in Phaseolus.

Authors:  R C Martin; M C Mok; D W Mok
Journal:  Proc Natl Acad Sci U S A       Date:  1993-02-01       Impact factor: 11.205

8.  The maize abscisic acid-responsive protein Rab17 is located in the nucleus and interacts with nuclear localization signals.

Authors:  A Goday; A B Jensen; F A Culiáñez-Macià; M Mar Albà; M Figueras; J Serratosa; M Torrent; M Pagès
Journal:  Plant Cell       Date:  1994-03       Impact factor: 11.277

9.  Introduction of a temperature-sensitive phenotype into influenza A/WSN/33 virus by altering the basic amino acid domain of influenza virus matrix protein.

Authors:  Teresa Liu; Zhiping Ye
Journal:  J Virol       Date:  2004-09       Impact factor: 5.103

10.  Human carbon catabolite repressor protein (CCR4)-associative factor 1: cloning, expression and characterization of its interaction with the B-cell translocation protein BTG1.

Authors:  J A Bogdan; C Adams-Burton; D L Pedicord; D A Sukovich; P A Benfield; M H Corjay; J K Stoltenborg; I B Dicker
Journal:  Biochem J       Date:  1998-12-01       Impact factor: 3.857

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