Molecular mechanisms of cutis laxa and distal renal tubular acidosis-causing mutations in V-ATPase a subunits, ATP6V0A2 and ATP6V0A4.

about

Molecular mechanisms of cutis laxa and distal renal tubular acidosis-causing mutations in V-ATPase a subunits, ATP6V0A2 and ATP6V0A4.

Item

http://www.wikidata.org/entity/Q47223009

description

2018 nî lūn-bûn

@nan

2018年の論文

@ja

2018年学术文章

@wuu

2018年学术文章

@zh

2018年学术文章

@zh-cn

2018年学术文章

@zh-hans

2018年学术文章

@zh-my

2018年学术文章

@zh-sg

2018年學術文章

@yue

2018年學術文章

@zh-hant

name

Molecular mechanisms of cutis ...... bunits, ATP6V0A2 and ATP6V0A4.

@en

Molecular mechanisms of cutis ...... bunits, ATP6V0A2 and ATP6V0A4.

@nl

type

Item

label

Molecular mechanisms of cutis ...... bunits, ATP6V0A2 and ATP6V0A4.

@en

Molecular mechanisms of cutis ...... bunits, ATP6V0A2 and ATP6V0A4.

@nl

prefLabel

Molecular mechanisms of cutis ...... bunits, ATP6V0A2 and ATP6V0A4.

@en

Molecular mechanisms of cutis ...... bunits, ATP6V0A2 and ATP6V0A4.

@nl

P1476

Molecular mechanisms of cutis ...... bunits, ATP6V0A2 and ATP6V0A4.

@en

P2093

Joo Wan Kim

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

Morris F Manolson

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

Norbert Kartner

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

Reinhart A F Reithmeier

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

Sally Esmail

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

Yeqi Yao

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

P2860

V-ATPase interacts with ARNO and Arf6 in early endosomes and regulates the protein degradative pathway

Human H+ATPase a4 subunit mutations causing renal tubular acidosis reveal a role for interaction with phosphofructokinase-1

Novel ATP6V1B1 and ATP6V0A4 mutations in autosomal recessive distal renal tubular acidosis with new evidence for hearing loss

Role of Vma21p in assembly and transport of the yeast vacuolar ATPase

Mechanisms of protein-folding diseases at a glance

Models for the a subunits of the Thermus thermophilus V/A-ATPase and Saccharomyces cerevisiae V-ATPase enzymes by cryo-EM and evolutionary covariance

Yeast V-ATPase complexes containing different isoforms of the 100-kDa a-subunit differ in coupling efficiency and in vivo dissociation.

Skp1 forms multiple protein complexes, including RAVE, a regulator of V-ATPase assembly.

Voa1p functions in V-ATPase assembly in the yeast endoplasmic reticulum

Mutations in the a3 subunit of the vacuolar H(+)-ATPase cause infantile malignant osteopetrosis

P31

scholarly article

P356

10.1074/JBC.M117.818872

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

P407

English

P577

2018-01-08T00:00:00Z

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

P698

29311258

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

P932

5827428

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