Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
The protein network of HIV budding.
Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins.
Recycling of ESCRTs by the AAA-ATPase Vps4 is regulated by a conserved VSL region in Vta1.
The ESCRT-III subunit hVps24 is required for degradation but not silencing of the epidermal growth factor receptor.
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hVps24 localizes mainly to late endosomes
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Required for EGFR degradation and transport to lysosomes
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Depletion causes accumulation in small MVEs with impaired lysosome fusion
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Not required for termination of EGF signaling
Structural basis for budding by the ESCRT-III factor CHMP3.
Functional multivesicular bodies are required for autophagic clearance of protein aggregates associated with neurodegenerative disease.
Novel interactions of ESCRT-III with LIP5 and VPS4 and their implications for ESCRT-III disassembly.
Structural basis for autoinhibition of ESCRT-III CHMP3.
Helical structures of ESCRT-III are disassembled by VPS4.
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CHMP2A and CHMP3 assemble into helical tubular structures in vitro
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VPS4 disassembles the tubes upon ATP hydrolysis
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CHMP2A-CHMP3 copolymers expose membrane interaction sites externally
Large-scale proteomics and phosphoproteomics of urinary exosomes.
Membrane scission by the ESCRT-III complex.
Structural basis for ESCRT-III protein autoinhibition.
Membrane budding and scission by the ESCRT machinery: it's all in the neck.
Human ESCRT-III and VPS4 proteins are required for centrosome and spindle maintenance.
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Depletion of any ESCRT-III protein inhibits abscission
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ESCRT-III depletion causes centrosome amplification and multipolar spindles
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CHMP3 and CHMP4 localize to kinetochores
The role of ESCRT proteins in fusion events involving lysosomes, endosomes and autophagosomes.
Mechanism of inhibition of retrovirus release from cells by interferon-induced gene ISG15.
Structural basis for ESCRT-III CHMP3 recruitment of AMSH.
Syndecan-syntenin-ALIX regulates the biogenesis of exosomes.
ESCRT-III CHMP2A and CHMP3 form variable helical polymers in vitro and act synergistically during HIV-1 budding.
Interactions of the human LIP5 regulatory protein with endosomal sorting complexes required for transport.
ESCRT machinery is required for plasma membrane repair.
Structure of cellular ESCRT-III spirals and their relationship to HIV budding.
Spastin and ESCRT-III coordinate mitotic spindle disassembly and nuclear envelope sealing.
ESCRT-III controls nuclear envelope reformation.
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ESCRT-III localizes to nuclear envelope fenestrations during telophase
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CHMP3 depletion impairs NE integrity
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ESCRT-III required for sealing holes in forming NE
Structural basis of CHMP2A-CHMP3 ESCRT-III polymer assembly and membrane cleavage.
Recruitment Of HIV Virion Budding Machinery
VPS4 binds ESCRT-III assemblies at nuclear envelope (NE) fenestrations
CHMP7 binds CHMP4B, which recruits other subunits of the ESCRT-III complex
SPAST (spastin) binds the IST1 subunit of ESCRT-III at the sites of microtubule attachment to chromatin
VPS4 mediates disassembly of ESCRTIII subunits to promote sealing of holes in the nuclear envelope
SPAST (spastin) mediates the severing of microtubules at chromosome attachment sites
Deep research report on CHMP3