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, accompanied by conservative changes to GO terms applied by UniProt
Increased expression of Hsp40 chaperones, transcriptional factors, and ribosomal protein Rpp0 can cure yeast prions.
Global analysis of protein localization in budding yeast.
The proteome of Saccharomyces cerevisiae mitochondria.
Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics.
Structure-templated predictions of novel protein interactions from sequence information.
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Apj1 was experimentally recovered with the Hsp70 proteins Ssa1 and Ssa2.
"Another confirmed interaction is between a member of the HSP40 family (Apj1) with two HSP70 proteins (Ssa1, Ssa2)."
Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress.
Sequential duplications of an ancient member of the DnaJ-family expanded the functional chaperone network in the eukaryotic cytosol.
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Apj1 is a specialized class A J-domain cochaperone involved in degradation of sumoylated proteins and genetically cooperative with the Slx5 STUbL pathway.
"Apj1's specialized role is related to degradation of sumolyated proteins."
Cmr1/WDR76 defines a nuclear genotoxic stress body linking genome integrity and protein quality control.
The cellular economy of the Saccharomyces cerevisiae zinc proteome.
Chaperone-Mediated Protein Disaggregation Triggers Proteolytic Clearance of Intra-nuclear Protein Inclusions.
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Apj1 is recruited to nuclear inclusions and promotes proteasomal turnover of insoluble nuclear clients, while its loss accelerates refolding of nuclear luciferase.
"In summary, we conclude that Apj1 is recruited to nuclear protein inclusions upon stress and supports the turnover of misfolded nuclear-targeted proteins."
Network of general and specialty J protein chaperones of the yeast cytosol.
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Cytosolic J proteins are obligate Hsp70 cochaperones, and many functions require only J-domain stimulation of Hsp70 ATPase activity.
"J proteins are obligate cochaperones of Hsp70s, stimulating their ATPase activity and thus allowing them to function in multiple cellular processes."
Unique characteristics of the J-domain proximal regions of Hsp70 cochaperone Apj1 in prion propagation/elimination and its overlap with Sis1 function.
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A 90-residue Apj1 fragment containing the J domain and adjacent Q/A segment is sufficient for Hsp104-driven curing of strong [PSI+] in the tested system.
"we found that a 90-residue fragment that includes the 70-residue J-domain and the adjacent 12-residue glutamine/alanine (Q/A) segment is sufficient for curing."
Nuclear and cytosolic J-domain proteins provide synergistic control of Hsf1 at distinct phases of the heat shock response.
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Apj1 promotes Hsf1 displacement from heat-shock elements and is required for normal attenuation of the heat-shock response.
"Here, we show that the yeast nuclear JDP Apj1 primarily controls the attenuation phase of the HSR by promoting Hsf1's displacement from heat shock elements in target DNA."
OpenScientist hypothesis report for APJ1 GO:0042026
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The focused report finds protein refolding weakly supported and partially over-annotated as a direct APJ1 function because the target-specific study routes nuclear aggregates to turnover instead.
"Weakly supported / partially over-annotated (as a *direct* function)."
Falcon deep research report for APJ1