N-linked glycosylation of a subunit isoforms is critical for vertebrate vacuolar H+ -ATPase (V-ATPase) biosynthesis.

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

P2860

Q47223009-6DDF5F89-B4FF-46D5-8997-5C7C6081661E

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N-linked glycosylation of a subunit isoforms is critical for vertebrate vacuolar H+ -ATPase (V-ATPase) biosynthesis.

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2017 nî lūn-bûn

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N-linked glycosylation of a su ...... TPase (V-ATPase) biosynthesis.

@en

N-linked glycosylation of a su ...... vertebrate vacuolar H+ -ATPase

@nl

type

Item

label

N-linked glycosylation of a su ...... TPase (V-ATPase) biosynthesis.

@en

N-linked glycosylation of a su ...... vertebrate vacuolar H+ -ATPase

@nl

prefLabel

N-linked glycosylation of a su ...... TPase (V-ATPase) biosynthesis.

@en

N-linked glycosylation of a su ...... vertebrate vacuolar H+ -ATPase

@nl

P1476

N-linked glycosylation of a su ...... ATPase (V-ATPase) biosynthesis

@en

P2093

Joo Wan Kim

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

Morris F Manolson

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

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P2860

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

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

The amino-terminal domain of the vacuolar proton-translocating ATPase a subunit controls targeting and in vivo dissociation, and the carboxyl-terminal domain affects coupling of proton transport and ATP hydrolysis.

VMA21 deficiency prevents vacuolar ATPase assembly and causes autophagic vacuolar myopathy

ER chaperones in mammalian development and human diseases

On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database

Vacuolar ATPases: rotary proton pumps in physiology and pathophysiology

Structure of the Lipid Nanodisc-reconstituted Vacuolar ATPase Proton Channel: DEFINITION OF THE INTERACTION OF ROTOR AND STATOR AND IMPLICATIONS FOR ENZYME REGULATION BY REVERSIBLE DISSOCIATION.

N-glycosylation efficiency is determined by the distance to the C-terminus and the amino acid preceding an Asn-Ser-Thr sequon

The amino acid at the X position of an Asn-X-Ser sequon is an important determinant of N-linked core-glycosylation efficiency.

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861-875

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P31

scholarly article

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10.1002/JCB.26250

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P433

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

P478

119

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P50

Norbert Kartner

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2017-08-04T00:00:00Z

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P698

28661051

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P921

glycosylation

N-linked glycosylation of a subunit isoforms is critical for vertebrate vacuolar H+ -ATPase (V-ATPase) biosynthesis.

about

P2860

P2860

N-linked glycosylation of a subunit isoforms is critical for vertebrate vacuolar H+ -ATPase (V-ATPase) biosynthesis.

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type

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P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P698

P921

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P698

P921