Shuttling proteins go both ways.

Goldfarb DS

doi:10.1016/0960-9822(91)90059-6

Shuttling proteins go both ways.

Goldfarb DS ¹

Affiliations

1. Department of Biology, University of Rochester, Rochester, New York 14627, USA.
Authors
Goldfarb DS¹
(1 author)

Current Biology : CB, 01 Aug 1991, 1(4):212-214
https://doi.org/10.1016/0960-9822(91)90059-6 PMID: 15336122

Abstract

No abstract provided.

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Read article at publisher's site: https://doi.org/10.1016/0960-9822(91)90059-6

References

Articles referenced by this article (12)

Internuclear exchange of an inner nuclear membrane protein (p55) in heterokaryons: in vivo evidence for the interaction of p55 with the nuclear lamina.
Powell L, Burke B
J Cell Biol, (6 Pt 1):2225-2234 1990
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Cell, (3):489-497 1991
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Borer RA, Lehner CF, Eppenberger HM, Nigg EA
Cell, (3):379-390 1989
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Identification of two HSP70-related Xenopus oocyte proteins that are capable of recycling across the nuclear envelope.
Mandell RB, Feldherr CM
J Cell Biol, (5 Pt 1):1775-1783 1990
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Mutational analysis of the human HSP70 protein: distinct domains for nucleolar localization and adenosine triphosphate binding.
Milarski KL, Morimoto RI
J Cell Biol, (5):1947-1962 1989
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Karyophilic peptides: applications to the study of nuclear transport.
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Cell Biol Int Rep, (9):809-832 1988
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Mastoparan alters subcellular distribution of profilin and remodels F-actin cytoskeleton in cells of maize root apices.
Baluska F, von Witsch M, Peters M, Hlavacka A, Volkmann D
Plant Cell Physiol, 42(9):912-922, 01 Sep 2001
Cited by: 15 articles | PMID: 11577185
Nucleocytoplasmic transport.
Agutter PS, Prochnow D
Biochem J, 300 ( Pt 3):609-618, 01 Jun 1994
Cited by: 18 articles | PMID: 8010940 | PMCID: PMC1138210
Review Free full text in Europe PMC
The nucleolus: an organelle formed by the act of building a ribosome.
Mélèse T, Xue Z
Curr Opin Cell Biol, 7(3):319-324, 01 Jun 1995
Cited by: 164 articles | PMID: 7662360
Review
Identification of a signal for rapid export of proteins from the nucleus.
Wen W, Meinkoth JL, Tsien RY, Taylor SS
Cell, 82(3):463-473, 01 Aug 1995
Cited by: 770 articles | PMID: 7634336
Hormonal regulation of the nuclear localization signals of the human glucocorticosteroid receptor.
Cadepond F, Gasc JM, Delahaye F, Jibard N, Schweizer-Groyer G, Segard-Maurel I, Evans R, Baulieu EE
Exp Cell Res, 201(1):99-108, 01 Jul 1992
Cited by: 44 articles | PMID: 1612132

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Shuttling proteins go both ways.

Affiliations

Authors

Abstract

Full text links

References

Internuclear exchange of an inner nuclear membrane protein (p55) in heterokaryons: in vivo evidence for the interaction of p55 with the nuclear lamina.

Rapid and reversible translocation of the catalytic subunit of cAMP-dependent protein kinase type II from the Golgi complex to the nucleus.

Distribution of proteins between nucleus and cytoplasm of Amoeba proteus.

Nuclear protein localization.

How proteins enter the nucleus.

Major nucleolar proteins shuttle between nucleus and cytoplasm.

Identification of two HSP70-related Xenopus oocyte proteins that are capable of recycling across the nuclear envelope.

Mutational analysis of the human HSP70 protein: distinct domains for nucleolar localization and adenosine triphosphate binding.

Karyophilic peptides: applications to the study of nuclear transport.

A nuclear localization signal binding protein in the nucleolus.

Citations & impact

Impact metrics

Citations of article over time

Article citations

Mastoparan alters subcellular distribution of profilin and remodels F-actin cytoskeleton in cells of maize root apices.

Nucleocytoplasmic transport.

The nucleolus: an organelle formed by the act of building a ribosome.

Identification of a signal for rapid export of proteins from the nucleus.

Hormonal regulation of the nuclear localization signals of the human glucocorticosteroid receptor.

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Shuttling proteins go both ways.

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