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

Structure-function relationships of the C-terminal end of the Saccharomyces cerevisiae ADP/ATP carrier isoform 2.

The Journal of biological chemistry - 25 Apr 2008

Clémençon Benjamin, Rey Martial, Dianoux Anne-Christine, Trézéguet Véronique, Lauquin Guy J-M, Brandolin Gérard, Pelosi Ludovic

Abstract excerpt

The adenine nucleotide carrier (Ancp) catalyzes the transport of ADP and ATP across the mitochondrial inner membrane, thus playing an essential role in the cellular energy metabolism. Two regions of Anc2p from Saccharomyces cerevisiae are specifically photolabeled using a photoactivable ADP derivative; they are the central matrix loop, m2, and the C-terminal end. To get more insights into the structure-function...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Diphosphate
Share to Ligands

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mitochondria

Share to Mitochondrial ADP, ATP Translocases

Share to Protein Isoforms

Share to Saccharomyces cerevisiae Proteins

Share to Spectrometry, Fluorescence

Share to Structure-Activity Relationship

Source

Identifiers

PMID: 18299327
DOI: 10.1074/jbc.M709565200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structure-function relationships of the C-terminal end of the Saccharomyces cerevisiae ADP/ATP carrier isoform 2.PMID 18299327Read ↗

The structure of the second cytosolic loop of the yeast mitochondrial ADP/ATP carrier AAC2 is dependent on the conformational state.Semantic proximity Read ↗

Dominant membrane uncoupling by mutant adenine nucleotide translocase in mitochondrial diseases.Semantic proximity Read ↗

Conserved cardiolipin-mitochondrial ADP/ATP carrier interactions assume distinct structural and functional roles that are clinically relevantSemantic proximity Read ↗

A hybrid model to study pathological mutations of the human ADP/ATP carriers.Semantic proximity Read ↗

Selective profiling of N- and C-terminal nucleotide-binding sites in a TRPM2 channel.Semantic proximity Read ↗

Structure-function relationships of the ADP/ATP carrier.Semantic proximity Read ↗

Functional diversity among cardiolipin binding sites on the mitochondrial ADP/ATP carrier.Semantic proximity Read ↗

Sites of the NUDT9-H domain critical for ADP-ribose activation of the cation channel TRPM2.Semantic proximity Read ↗

Structure-function studies of adenine nucleotide transport in mitochondria. II. Biochemical analysis of distinct AAC1 and AAC2 proteins in yeast.Semantic proximity Read ↗

Ligand-induced activation of human TRPM2 requires the terminal ribose of ADPR and involves Arg1433 and Tyr1349.Semantic proximity Read ↗

Profiling of the ADP‐Ribosylome in Living CellsSemantic proximity Read ↗

Characterization of loops of the yeast mitochondrial ADP/ATP carrier facing the cytosol by site-directed mutagenesis.Semantic proximity Read ↗

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