SGD gene description for MDM12 (yeast)
Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Electronic Gene Ontology annotations created by transferring manual GO annotations between related proteins based on shared sequence features
Automatic assignment of GO terms using logical inference, based on on inter-ontology links
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
A protein complex containing Mdm10p, Mdm12p, and Mmm1p links mitochondrial membranes and DNA to the cytoskeleton-based segregation machinery.
Large-scale identification of yeast integral membrane protein interactions.
Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics.
The morphology proteins Mdm12/Mmm1 function in the major beta-barrel assembly pathway of mitochondria.
An ER-mitochondria tethering complex revealed by a synthetic biology screen.
Mdm10 as a dynamic constituent of the TOB/SAM complex directs coordinated assembly of Tom40.
The conserved GTPase Gem1 regulates endoplasmic reticulum-mitochondria connections.
Composition and topology of the endoplasmic reticulum-mitochondria encounter structure.
Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress.
A phospholipid transfer function of ER-mitochondria encounter structure revealed in vitro.
Structure-function insights into direct lipid transfer between membranes by Mmm1-Mdm12 of ERMES.
Contribution of ERMES subunits to mature peroxisome abundance.
Complementation Assay Using Fusion of Split-GFP and TurboID (CsFiND) Enables Simultaneous Visualization and Proximity Labeling of Organelle Contact Sites in Yeast.
Mdm12p, a component required for mitochondrial inheritance that is conserved between budding and fission yeast.
Conserved SMP domains of the ERMES complex bind phospholipids and mediate tether assembly.
ER-mitochondrial junctions can be bypassed by dominant mutations in the endosomal protein Vps13.
Crystal structure of Mdm12 reveals the architecture and dynamic organization of the ERMES complex.
METALIC reveals interorganelle lipid flux in live cells by enzymatic mass tagging.
In situ architecture of the ER-mitochondria encounter structure.
Comparative analysis of mitochondrial proteomes across the tree of life.
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Comparative proteomic/phylogenetic inference that Saccharomyces mitochondria retained the ERMES complex from the last opisthokont common ancestor, whereas human mitochondria lost it.
"the endoplasmic reticulum (ER)-mitochondria encounter structure (ERMES) complex from LOCA mitochondria, but human mitochondria lost these pathways"
Gem1 and ERMES do not directly affect phosphatidylserine transport from ER to mitochondria or mitochondrial inheritance.
Falcon deep research report for MDM12