Structural similarity in the absence of sequence homology of the messenger RNA export factors Mtr2 and p15. - Test2 - elhamkhani - TriplyDB

Structural similarity in the absence of sequence homology of the messenger RNA export factors Mtr2 and p15.

Structural similarity in the absence of sequence homology of the messenger RNA export factors Mtr2 and p15.

http://www.wikidata.org/entity/Q27641540

about

The Mtr2-Mex67 NTF2-like domain complex. Structural insights into a dual role of Mtr2 for yeast nuclear export Molecular Basis for Bre5 Cofactor Recognition by the Ubp3 Deubiquitylating Enzyme Structural and Functional Study of Yer067w, a New Protein Involved in Yeast Metabolism Control and Drug Resistance The Structure of the NXF2/NXT1 Heterodimeric Complex Reveals the Combined Specificity and Versatility of the NTF2-Like Fold A versatile interaction platform on the Mex67-Mtr2 receptor creates an overlap between mRNA and ribosome export.Role of Mex67-Mtr2 in the nuclear export of 40S pre-ribosomes.Nuclear export of messenger RNA Agrobacterium tumefaciens VirB8 structure reveals potential protein-protein interaction sites.Domain organization within the nuclear export factor Mex67:Mtr2 generates an extended mRNA binding surface Comparative genomics of proteins involved in RNA nucleocytoplasmic export.Nucleo-cytoplasmic transport of proteins and RNA in plants.Clustering evolving proteins into homologous families Nuclear transporters in a multinucleated organism: functional and localization analyses in Aspergillus nidulans.Evolutionary development of redundant nuclear localization signals in the mRNA export factor NXF1.Nucleocytoplasmic transport: integrating mRNA production and turnover with export through the nuclear pore Targeted cross-linking-mass spectrometry determines vicinal interactomes within heterogeneous RNP complexes.mRNA journey to the cytoplasm: attire required.Flexible gates: dynamic topologies and functions for FG nucleoporins in nucleocytoplasmic transport.Assembly and nuclear export of pre-ribosomal particles in budding yeast.Structural characterization of the principal mRNA-export factor Mex67-Mtr2 from Chaetomium thermophilum.The principal mRNA nuclear export factor NXF1:NXT1 forms a symmetric binding platform that facilitates export of retroviral CTE-RNA Atomic resolution structures in nuclear transport Homology, similarity, and identity in peptide epitope immunodefinition.Structural basis for interaction between the Ubp3 deubiquitinating enzyme and its Bre5 cofactor.

P2860

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P2860

Structural similarity in the absence of sequence homology of the messenger RNA export factors Mtr2 and p15.

http://www.wikidata.org/entity/Q27641540

description

2003 nî lūn-bûn

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2003 թուականի Յուլիսին հրատարակուած գիտական յօդուած

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2003 թվականի հուլիսին հրատարակված գիտական հոդված

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2003年の論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年论文

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Structural similarity in the a ...... NA export factors Mtr2 and p15

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Structural similarity in the a ...... A export factors Mtr2 and p15.

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Structural similarity in the a ...... A export factors Mtr2 and p15.

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Structural similarity in the a ...... NA export factors Mtr2 and p15

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Structural similarity in the a ...... A export factors Mtr2 and p15.

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Structural similarity in the a ...... A export factors Mtr2 and p15.

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Structural similarity in the a ...... NA export factors Mtr2 and p15

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Structural similarity in the a ...... A export factors Mtr2 and p15.

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Structural similarity in the a ...... A export factors Mtr2 and p15.

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Elena Conti

http://www.w3.org/2001/XMLSchema#string

Sébastien Fribourg

http://www.w3.org/2001/XMLSchema#string

P2860

Structural basis for the recognition of a nucleoporin FG repeat by the NTF2-like domain of the TAP/p15 mRNA nuclear export factor

TAP binds to the constitutive transport element (CTE) through a novel RNA-binding motif that is sufficient to promote CTE-dependent RNA export from the nucleus

The Mex67p-mediated nuclear mRNA export pathway is conserved from yeast to human

Formation of Tap/NXT1 heterodimers activates Tap-dependent nuclear mRNA export by enhancing recruitment to nuclear pore complexes

The C-terminal domain of TAP interacts with the nuclear pore complex and promotes export of specific CTE-bearing RNA substrates

Improved methods for building protein models in electron density maps and the location of errors in these models

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

The structure of the mRNA export factor TAP reveals a cis arrangement of a non-canonical RNP domain and an LRR domain

Structural basis for the interaction between NTF2 and nucleoporin FxFG repeats.

Structural basis for the interaction between the Tap/NXF1 UBA domain and FG nucleoporins at 1A resolution

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699-703

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scholarly article

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10.1038/SJ.EMBOR.EMBOR883

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7

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