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Literature DB >> 19421156

Nuclear transport comes full circle.

Erik W Debler, Günter Blobel, André Hoelz.

Abstract

Mesh：

Substances：

Year: 2009 PMID： 19421156 DOI： 10.1038/nsmb0509-457

Source DB: PubMed Journal: Nat Struct Mol Biol ISSN： 1545-9985 Impact factor: 15.369

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13 in total

Review 1. Karyopherins and nuclear import.

Authors: Y M Chook; G Blobel
Journal: Curr Opin Struct Biol Date: 2001-12 Impact factor: 6.809

2. GLFG and FxFG nucleoporins bind to overlapping sites on importin-beta.

Authors: Richard Bayliss; Trevor Littlewood; Lisa A Strawn; Susan R Wente; Murray Stewart
Journal: J Biol Chem Date: 2002-10-07 Impact factor: 5.157

3. Cell biology: popping out of the nucleus.

Authors: André Hoelz; Günter Blobel
Journal: Nature Date: 2004-12-16 Impact factor: 49.962

4. Structural basis for the assembly of a nuclear export complex.

Authors: Yoshiyuki Matsuura; Murray Stewart
Journal: Nature Date: 2004-12-16 Impact factor: 49.962

Review 5. Structural biology of nucleocytoplasmic transport.

Authors: Atlanta Cook; Fulvia Bono; Martin Jinek; Elena Conti
Journal: Annu Rev Biochem Date: 2007 Impact factor: 23.643

6. Protein sequence requirements for function of the human T-cell leukemia virus type 1 Rex nuclear export signal delineated by a novel in vivo randomization-selection assay.

Authors: H P Bogerd; R A Fridell; R E Benson; J Hua; B R Cullen
Journal: Mol Cell Biol Date: 1996-08 Impact factor: 4.272

7. Structural basis for m3G-cap-mediated nuclear import of spliceosomal UsnRNPs by snurportin1.

Authors: Anja Strasser; Achim Dickmanns; Reinhard Lührmann; Ralf Ficner
Journal: EMBO J Date: 2005-05-26 Impact factor: 11.598

8. Architecture of CRM1/Exportin1 suggests how cooperativity is achieved during formation of a nuclear export complex.

Authors: Carlo Petosa; Guy Schoehn; Peter Askjaer; Ulrike Bauer; Martine Moulin; Ulrich Steuerwald; Montserrat Soler-López; Florence Baudin; Iain W Mattaj; Christoph W Müller
Journal: Mol Cell Date: 2004-12-03 Impact factor: 17.970

9. Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin alpha.

Authors: E Conti; M Uy; L Leighton; G Blobel; J Kuriyan
Journal: Cell Date: 1998-07-24 Impact factor: 41.582

6. Nucleoporin translocated promoter region (Tpr) associates with dynein complex, preventing chromosome lagging formation during mitosis.

Authors: Hiroshi Nakano; Tatsuyoshi Funasaka; Chieko Hashizume; Richard W Wong
Journal: J Biol Chem Date: 2010-02-04 Impact factor: 5.157

6 in total

Nuclear transport comes full circle.

Review 1. Karyopherins and nuclear import.

2. GLFG and FxFG nucleoporins bind to overlapping sites on importin-beta.

3. Cell biology: popping out of the nucleus.

4. Structural basis for the assembly of a nuclear export complex.

Review 5. Structural biology of nucleocytoplasmic transport.

6. Protein sequence requirements for function of the human T-cell leukemia virus type 1 Rex nuclear export signal delineated by a novel in vivo randomization-selection assay.

7. Structural basis for m3G-cap-mediated nuclear import of spliceosomal UsnRNPs by snurportin1.

8. Architecture of CRM1/Exportin1 suggests how cooperativity is achieved during formation of a nuclear export complex.

9. Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin alpha.

10. Molecular basis for the recognition of snurportin 1 by importin beta.

Review 1. New pathologic mechanisms in nucleotide repeat expansion disorders.

2. Structure of a trimeric nucleoporin complex reveals alternate oligomerization states.

Review 3. Characterization of the membrane-coating Nup84 complex: paradigm for the nuclear pore complex structure.

4. Evidence for an evolutionary relationship between the large adaptor nucleoporin Nup192 and karyopherins.

5. Molecular basis for the anchoring of proto-oncoprotein Nup98 to the cytoplasmic face of the nuclear pore complex.

6. Nucleoporin translocated promoter region (Tpr) associates with dynein complex, preventing chromosome lagging formation during mitosis.