ELYS regulates the localization of LBR by modulating its phosphorylation state. - Wikidata - wikimedia - TriplyDB

ELYS regulates the localization of LBR by modulating its phosphorylation state.

ELYS regulates the localization of LBR by modulating its phosphorylation state.

http://www.wikidata.org/entity/Q37425917

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Lamin B Receptor: Interplay between Structure, Function and Localization.Enhancer of rudimentary homologue interacts with scaffold attachment factor B at the nuclear matrix to regulate SR protein phosphorylation.The nucleoporin MEL-28/ELYS: A PP1 scaffold during M-phase exit.Messages from the voices within: regulation of signaling by proteins of the nuclear lamina.

P2860

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ELYS regulates the localization of LBR by modulating its phosphorylation state.

http://www.wikidata.org/entity/Q37425917

description

article científic

@ca

article scientifique

@fr

articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 06 October 2016

@en

vedecký článok

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vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

ELYS regulates the localization of LBR by modulating its phosphorylation state.

@en

ELYS regulates the localization of LBR by modulating its phosphorylation state.

@nl

type

label

ELYS regulates the localization of LBR by modulating its phosphorylation state.

@en

ELYS regulates the localization of LBR by modulating its phosphorylation state.

@nl

prefLabel

ELYS regulates the localization of LBR by modulating its phosphorylation state.

@en

ELYS regulates the localization of LBR by modulating its phosphorylation state.

@nl

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Journal of Cell Science

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ELYS regulates the localization of LBR by modulating its phosphorylation state.

@en

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Masatoshi Takagi

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

Michaela Clever

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

Yasuhiro Mimura

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

P2860

Novel vertebrate nucleoporins Nup133 and Nup160 play a role in mRNA export.

Primary structure analysis and lamin B and DNA binding of human LBR, an integral protein of the nuclear envelope inner membrane

ELYS is a dual nucleoporin/kinetochore protein required for nuclear pore assembly and proper cell division

Interaction between an integral protein of the nuclear envelope inner membrane and human chromodomain proteins homologous to Drosophila HP1

The enzymatic activity of SR protein kinases 1 and 1a is negatively affected by interaction with scaffold attachment factors B1 and 2

Vertebrate Nup53 interacts with the nuclear lamina and is required for the assembly of a Nup93-containing complex

Live imaging and modeling of inner nuclear membrane targeting reveals its molecular requirements in mammalian cells.

Solution Structure and Molecular Interactions of Lamin B Receptor Tudor Domain

SRPK1 and LBR protein kinases show identical substrate specificities

Inner nuclear membrane protein LBR preferentially interacts with DNA secondary structures and nucleosomal linker

P304

4200-4212

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scholarly article

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10.1242/JCS.190678

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22

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129

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2016-10-06T00:00:00Z

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27802161

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phosphorylation

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5117198

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