Trapping of normal EB1 ligands in aggresomes formed by an EB1 deletion mutant.

about

EB1 is required for spindle symmetry in mammalian mitosis Adenomatous polyposis coli on microtubule plus ends in cell extensions can promote microtubule net growth with or without EB1.MCAK associates with EB1.

P2860

Q27311190-844D783B-F4D4-4682-9470-7418BF3E29F9 Q28594585-FD2A14E2-2070-4404-82CA-0FF59ED3CD4B Q40060454-89BB6C5C-662C-4C65-A300-2D15EA09657E

P2860

Trapping of normal EB1 ligands in aggresomes formed by an EB1 deletion mutant.

Item

http://www.wikidata.org/entity/Q24798968

description

2005 nî lūn-bûn

@nan

2005 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2005 թվականի ապրիլին հրատարակված գիտական հոդված

@hy

2005年の論文

@ja

2005年論文

@yue

2005年論文

@zh-hant

2005年論文

@zh-hk

2005年論文

@zh-mo

2005年論文

@zh-tw

2005年论文

@wuu

name

Trapping of normal EB1 ligands in aggresomes formed by an EB1 deletion mutant

@nl

Trapping of normal EB1 ligands in aggresomes formed by an EB1 deletion mutant.

@ast

Trapping of normal EB1 ligands in aggresomes formed by an EB1 deletion mutant.

@en

type

Item

label

Trapping of normal EB1 ligands in aggresomes formed by an EB1 deletion mutant

@nl

Trapping of normal EB1 ligands in aggresomes formed by an EB1 deletion mutant.

@ast

Trapping of normal EB1 ligands in aggresomes formed by an EB1 deletion mutant.

@en

prefLabel

Trapping of normal EB1 ligands in aggresomes formed by an EB1 deletion mutant

@nl

Trapping of normal EB1 ligands in aggresomes formed by an EB1 deletion mutant.

@ast

Trapping of normal EB1 ligands in aggresomes formed by an EB1 deletion mutant.

@en

P1476

Trapping of normal EB1 ligands in aggresomes formed by an EB1 deletion mutant.

@en

P2093

Ewan E Morrison

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

Jon M Askham

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

Kelly Milward

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

Matthew Adams

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

Nick P Riess

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

Tracy Lee

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

P2860

The APC-associated protein EB1 associates with components of the dynactin complex and cytoplasmic dynein intermediate chain

Regulation and function of the interaction between the APC tumour suppressor protein and EB1

Parkin accumulation in aggresomes due to proteasome impairment

APC binds to the novel protein EB1

Evidence that an interaction between EB1 and p150(Glued) is required for the formation and maintenance of a radial microtubule array anchored at the centrosome

Dynactin is required for bidirectional organelle transport

The microtubule plus-end proteins EB1 and dynactin have differential effects on microtubule polymerization

Crystal structure of the amino-terminal microtubule-binding domain of end-binding protein 1 (EB1)

EB1, a protein which interacts with the APC tumour suppressor, is associated with the microtubule cytoskeleton throughout the cell cycle

EB/RP gene family encodes tubulin binding proteins

P2888

1471-2121-6-17

P304

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

P31

scholarly article

P356

10.1186/1471-2121-6-17

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

P407

English

P433

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

P478

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

P577

2005-04-06T00:00:00Z

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

P5875

7922406

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

P6179

1001705318

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

P6409

81267501

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

P698

15813965

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

P921

cell biology

P932

1090566

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

P953

1058/

Trapping of normal EB1 ligands in aggresomes formed by an EB1 deletion mutant.

about

P2860

P2860

Trapping of normal EB1 ligands in aggresomes formed by an EB1 deletion mutant.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P407

P433

P478

P577

P5875

P6179

P6409

P698

P921

P932

P953

P356

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P407

P433

P478

P577

P5875

P6179

P6409

P698

P921

P932

P953