Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

NMR Structural and Biophysical Analysis of the Disease-Linked Inner Mitochondrial Membrane Protein MPV17.

Journal of molecular biology - 23 Jul 2021

Sperl Laura E, Hagn Franz

Abstract excerpt

MPV17 is an integral inner mitochondrial membrane protein, whose loss-of-function is linked to the hepatocerebral form of the mitochondrial-DNA-depletion syndrome, leading to a tissue-specific reduction of mitochondrial DNA and organ failure in infants. Several disease-causing mutations in MPV17 have been identified and earlier studies with reconstituted protein suggest that MPV17 forms a high conductivity...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Circular Dichroism
Share to Disulfides
Share to Micelles

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Mitochondrial Proteins

Share to Nuclear Magnetic Resonance, Biomolecular

Share to Protein Engineering

Share to Protein Folding

Share to Protein Multimerization

Source

Identifiers

PMID: 34116124
DOI: 10.1016/j.jmb.2021.167098

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

NMR Structural and Biophysical Analysis of the Disease-Linked Inner Mitochondrial Membrane Protein MPV17.PMID 34116124Read ↗

The Human Mitochondrial DNA Depletion Syndrome Gene MPV17 Encodes a Non-selective Channel That Modulates Membrane Potential.Semantic proximity Read ↗

In-depth study of MPV17: a molecular travel unveiling a mitochondrial calcium regulation functionSemantic proximity Read ↗

The 3.5-Å CryoEM Structure of Nanodisc-Reconstituted Yeast Vacuolar ATPase Vo Proton Channel.Semantic proximity Read ↗

MPV17-associated hepatocerebral mitochondrial DNA depletion syndrome: new patients and novel mutations.Semantic proximity Read ↗

Insights into VPS13 properties and function reveal a new mechanism of eukaryotic lipid transport.Semantic proximity Read ↗

In situ architecture of the lipid transport protein VPS13C at ER-lysosomes membrane contactsSemantic proximity Read ↗

Conformational analysis of membrane-proximal segments of GDAP1 in a lipidic environment using synchrotron radiation suggests a mode of assembly at the mitochondrial outer membraneSemantic proximity Read ↗

VPS13C/PARK23 initiates lipid transfer and membrane remodeling for efficient lysosomal repairSemantic proximity Read ↗

AAV-mediated liver-specific MPV17 expression restores mtDNA levels and prevents diet-induced liver failure.Semantic proximity Read ↗

VPS13C/PARK23 initiates lipid transfer and membrane remodeling for efficient lysosomal repairSemantic proximity Read ↗

Structure of mammalian endolysosomal TRPML1 channel in nanodiscs.Semantic proximity Read ↗

Conformational changes associated with L16P and T118M mutations in the membrane-embedded PMP22 protein, consequential in CMT-1A.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.