Complementary interhelical interactions between three buried Glu-Lys pairs within three heptad repeats are essential for Hec1-Nuf2 heterodimerization and mitotic progression. - Test2 - elhamkhani - TriplyDB

Complementary interhelical interactions between three buried Glu-Lys pairs within three heptad repeats are essential for Hec1-Nuf2 heterodimerization and mitotic progression.

Complementary interhelical interactions between three buried Glu-Lys pairs within three heptad repeats are essential for Hec1-Nuf2 heterodimerization and mitotic progression.

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The Elucidation of the Interactome of 16 Arabidopsis bZIP Factors Reveals Three Independent Functional Networks Novel small molecules disrupting Hec1/Nek2 interaction ablate tumor progression by triggering Nek2 degradation through a death-trap mechanism.

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Complementary interhelical interactions between three buried Glu-Lys pairs within three heptad repeats are essential for Hec1-Nuf2 heterodimerization and mitotic progression.

http://www.wikidata.org/entity/Q37348881

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article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 15 October 2013

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vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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Complementary interhelical int ...... ation and mitotic progression.

@en

Complementary interhelical int ...... ation and mitotic progression.

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type

label

Complementary interhelical int ...... ation and mitotic progression.

@en

Complementary interhelical int ...... ation and mitotic progression.

@nl

prefLabel

Complementary interhelical int ...... ation and mitotic progression.

@en

Complementary interhelical int ...... ation and mitotic progression.

@nl

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JBC.M113.490524

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Journal of Biological Chemistry

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Complementary interhelical int ...... ation and mitotic progression.

@en

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Brittany Ngo

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

Bryan Ngo

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

Chun-Mei Hu

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

Randy Wei

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

Wen-Hwa Lee

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

Xuning Emily Guo

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

P2860

Architecture of the human ndc80-hec1 complex, a critical constituent of the outer kinetochore

The vertebrate Ndc80 complex contains Spc24 and Spc25 homologs, which are required to establish and maintain kinetochore-microtubule attachment

HEC binds to the seventh regulatory subunit of the 26 S proteasome and modulates the proteolysis of mitotic cyclins

The human Mis12 complex is required for kinetochore assembly and proper chromosome segregation.

HEC, a novel nuclear protein rich in leucine heptad repeats specifically involved in mitosis

Hec1 sequentially recruits Zwint-1 and ZW10 to kinetochores for faithful chromosome segregation and spindle checkpoint control

Hec1p, an evolutionarily conserved coiled-coil protein, modulates chromosome segregation through interaction with SMC proteins

Implications for kinetochore-microtubule attachment from the structure of an engineered Ndc80 complex.

The coiled-coil trigger site of the rod domain of cortexillin I unveils a distinct network of interhelical and intrahelical salt bridges

Buried polar residues in coiled-coil interfaces

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34403-34413

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scholarly article

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10.1074/JBC.M113.490524

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48

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2013-10-15T00:00:00Z

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3843055

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