The crystal structure of mouse Nup35 reveals atypical RNP motifs and novel homodimerization of the RRM domain
about
Architectural nucleoporins Nup157/170 and Nup133 are structurally related and descend from a second ancestral element.Molecular architecture of the Nup84–Nup145C–Sec13 edge element in the nuclear pore complex latticeStructural basis for the dual RNA-recognition modes of human Tra2- RRMStructure and nucleic acid binding activity of the nucleoporin Nup157Discovering novel interactions at the nuclear pore complex using bead halo: a rapid method for detecting molecular interactions of high and low affinity at equilibrium.Regulation of mRNA trafficking by nuclear pore complexes.Biology and biophysics of the nuclear pore complex and its componentsInteractome Mapping Reveals the Evolutionary History of the Nuclear Pore Complex.The C-terminal RNA binding motif of HuR is a multi-functional domain leading to HuR oligomerization and binding to U-rich RNA targets.Nup53 is required for nuclear envelope and nuclear pore complex assembly.Functional insights from studies on the structure of the nuclear pore and coat protein complexes.Towards reconciling structure and function in the nuclear pore complex.Nuclear pore complex assembly through the cell cycle: regulation and membrane organization.The nuclear pore complex has entered the atomic age.Structural insight into RNA recognition motifs: versatile molecular Lego building blocks for biological systems.The Nuclear Pore Complex as a Flexible and Dynamic GateThe Structure Inventory of the Nuclear Pore Complex.Nucleoporin 35 regulates cardiomyocyte pH homeostasis by controlling Na+-H+ exchanger-1 expression.A Novel Mutation in Nucleoporin 35 Causes Murine Degenerative Colonic Smooth Muscle Myopathy.PAB1 self-association precludes its binding to poly(A), thereby accelerating CCR4 deadenylation in vivo.Dimerization and direct membrane interaction of Nup53 contribute to nuclear pore complex assemblyRapid evolution exposes the boundaries of domain structure and function in natively unfolded FG nucleoporins.
P2860
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P2860
The crystal structure of mouse Nup35 reveals atypical RNP motifs and novel homodimerization of the RRM domain
description
2006 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2006
@ast
im Oktober 2006 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2006/10/13)
@sk
vědecký článek publikovaný v roce 2006
@cs
wetenschappelijk artikel (gepubliceerd op 2006/10/13)
@nl
наукова стаття, опублікована в жовтні 2006
@uk
مقالة علمية (نشرت في 13-10-2006)
@ar
name
The crystal structure of mouse ...... dimerization of the RRM domain
@ast
The crystal structure of mouse ...... dimerization of the RRM domain
@en
The crystal structure of mouse ...... dimerization of the RRM domain
@nl
type
label
The crystal structure of mouse ...... dimerization of the RRM domain
@ast
The crystal structure of mouse ...... dimerization of the RRM domain
@en
The crystal structure of mouse ...... dimerization of the RRM domain
@nl
prefLabel
The crystal structure of mouse ...... dimerization of the RRM domain
@ast
The crystal structure of mouse ...... dimerization of the RRM domain
@en
The crystal structure of mouse ...... dimerization of the RRM domain
@nl
P2093
P50
P1476
The crystal structure of mouse ...... dimerization of the RRM domain
@en
P2093
Akiko Tanaka
Kazutaka Murayama
Makoto Inoue
Naoko Imamoto
Noriko Handa
Ryogo Akasaka
Shingo Kose
Takaho Terada
Takanori Kigawa
P304
P356
10.1016/J.JMB.2006.07.089
P407
P577
2006-10-13T00:00:00Z