The architecture of EMC reveals a path for membrane protein insertion.
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
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
Defining the membrane proteome of NK cells.
Defining human ERAD networks through an integrative mapping strategy.
A human interactome in three quantitative dimensions organized by stoichiometries and abundances.
Architecture of the human interactome defines protein communities and disease networks.
The ER membrane protein complex is a transmembrane domain insertase.
The ER membrane protein complex interacts cotranslationally to enable biogenesis of multipass membrane proteins.
EMC Is Required to Initiate Accurate Membrane Protein Topogenesis.
A reference map of the human binary protein interactome.
Structural basis for membrane insertion by the human ER membrane protein complex.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
EMC is required for biogenesis of Xport-A, an essential chaperone of Rhodopsin-1 and the TRP channel.
OpenCell: Endogenous tagging for the cartography of human cellular organization.
The solute carrier superfamily interactome.
A selectivity filter in the ER membrane protein complex limits protein misinsertion at the ER.
EMC chaperone-Ca(V) structure reveals an ion channel assembly intermediate.
EMC rectifies the topology of multipass membrane proteins.
Structural insights into human EMC and its interaction with VDAC.
The EMC acts as a chaperone for membrane proteins.
Identification of host regulators of Mycobacterium tuberculosis phenotypes uncovers a role for the MMGT1-GPR156 lipid droplet axis in persistence.
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A genome-wide CRISPR screen prioritized MMGT1; MMGT1-deficient macrophages promote a switch of M. tuberculosis toward persistence, with upregulated lipid metabolism and lipid droplet accumulation driven by the orphan GPCR GPR156, and triacylglycerol-synthesis inhibition reduces both droplets and persistence.