MDR1 function is sensitive to the phosphorylation state of myosin regulatory light chain - Wikidata - awgldk - TriplyDB

MDR1 function is sensitive to the phosphorylation state of myosin regulatory light chain

MDR1 function is sensitive to the phosphorylation state of myosin regulatory light chain

http://www.wikidata.org/entity/Q34198760

about

Release of nonmuscle myosin II from the cytosolic domain of tumor necrosis factor receptor 2 is required for target gene expression.Reversal effect of adenovirus-mediated human interleukin 24 transfection on the cisplatin resistance of A549/DDP lung cancer cells.

P2860

Q37334658-E81A75F6-9D62-411E-B97D-569C0EFB4028 Q47430166-628C74EA-4AA6-4355-BDD6-4CB63C0CC095

P2860

MDR1 function is sensitive to the phosphorylation state of myosin regulatory light chain

http://www.wikidata.org/entity/Q34198760

description

2010 nî lūn-bûn

@nan

2010 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի մայիսին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年学术文章

@wuu

2010年学术文章

@zh-cn

2010年学术文章

@zh-hans

2010年学术文章

@zh-my

2010年学术文章

@zh-sg

2010年學術文章

@yue

name

MDR1 function is sensitive to the phosphorylation state of myosin regulatory light chain

@ast

MDR1 function is sensitive to the phosphorylation state of myosin regulatory light chain

@en

MDR1 function is sensitive to the phosphorylation state of myosin regulatory light chain

@nl

type

label

MDR1 function is sensitive to the phosphorylation state of myosin regulatory light chain

@ast

MDR1 function is sensitive to the phosphorylation state of myosin regulatory light chain

@en

MDR1 function is sensitive to the phosphorylation state of myosin regulatory light chain

@nl

prefLabel

MDR1 function is sensitive to the phosphorylation state of myosin regulatory light chain

@ast

MDR1 function is sensitive to the phosphorylation state of myosin regulatory light chain

@en

MDR1 function is sensitive to the phosphorylation state of myosin regulatory light chain

@nl

P1433

Q34198760-32A4252B-9824-48AA-814F-18CCE1DF670A

P1476

Q34198760-6EB12A8D-F93A-4FD5-8FC3-8A717295FD2B

P2093

Q34198760-54280C90-6117-4A21-8DF7-19F8CE03AEA5

Q34198760-71F0477A-FC52-4B7C-9CA8-EE64204DD3FD

Q34198760-C41B6FA3-4BE0-4F8F-A085-588876BE5966

Q34198760-CC933794-3852-4241-91F4-8CB5DC225023

Q34198760-F7344E1D-934E-4B56-8590-5F4FEB22DCD2

P2860

Q34198760-0A5BF98C-0D99-4718-AD4C-572C80F6F597

Q34198760-0B96E986-86E0-4795-87DD-2D88B1B5154B

Q34198760-1513508A-BDEE-4A57-9E80-C53205A46DBB

Q34198760-1CF289D7-0D67-477C-92CD-51C164FFEDD8

Q34198760-2BFB8E05-56E5-4811-81B4-B92A819F532A

Q34198760-37BCFFDE-5410-4F7F-862D-CBD1A33123F8

Q34198760-3DB90A68-490F-460D-A38B-9A987BB4923F

Q34198760-52A03CBF-E427-44CA-A54C-F5F14F427907

Q34198760-534371C5-6102-4340-AD67-D984449302D4

Q34198760-555C7734-D88D-4B72-AE55-BFD4D0F82953

P304

Q34198760-A16E8899-DB6B-43E0-8B44-95B85F0FDBCE

P31

Q34198760-02437322-F7D4-46BA-9165-31C003178087

P356

Q34198760-47A9441A-D66F-4511-A70B-E3A9F6FAB2D6

P407

Q34198760-582B0CA9-F760-453E-A6BE-2A1C7BC37A35

P433

Q34198760-CA174BD1-7C2C-4217-B6E1-A3452D61B7F1

P478

Q34198760-0BB79553-AF5B-4265-B4D1-3F2FD73E6AC7

P50

Q34198760-83BF4789-F2A4-4DB1-813D-8D0AEAE3E26A

P577

Q34198760-BDD3251E-5FD0-4420-B82A-B2CD6F28E062

P5875

Q34198760-A5634525-C4E6-4C6B-AA49-96851F9AD2D1

P698

Q34198760-31761FC6-DD7E-4026-BF78-0E146E996DA6

P921

Q34198760-A9A02AAE-64B1-4C24-825D-F1F2F77720C0

P932

Q34198760-4F551751-DF25-45E9-AF5E-7FD7F7944537

P356

J.BBRC.2010.05.084

P1433

Biochemical and Biophysical Research Communications

P1476

MDR1 function is sensitive to the phosphorylation state of myosin regulatory light chain

@en

P2093

Anand Venkataraman

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

Gaurav Bajaj

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

Jane E Ishmael

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

Rosita Rodriguez-Proteau

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

Ying Fan

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

P2860

MIR is a novel ERM-like protein that interacts with myosin regulatory light chain and inhibits neurite outgrowth

RNF2 interacts with the linker region of the human P-glycoprotein

Two distinct myosin light chain structures are induced by specific variations within the bound IQ motifs-functional implications

Three-dimensional structure of myosin subfragment-1: a molecular motor

Structure of the regulatory domain of scallop myosin at 2 A resolution: implications for regulation

Yeast myosin light chain, Mlc1p, interacts with both IQGAP and class II myosin to effect cytokinesis.

Nonmuscle myosin II moves in new directions

Direct interaction of myosin regulatory light chain with the NMDA receptor

Identification of HAX-1 as a protein that binds bile salt export protein and regulates its abundance in the apical membrane of Madin-Darby canine kidney cells

N-methyl-D-aspartate receptor subunits are non-myosin targets of myosin regulatory light chain

P304

7-12

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

P31

scholarly article

P356

10.1016/J.BBRC.2010.05.084

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

P407

P433

1

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

P478

398

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

P50

Chrissa Kioussi

P577

2010-05-25T00:00:00Z

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

P5875

44637717

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

P698

20510202

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

P921

phosphorylation

P932

2954888

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