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Search results 101 to 117 out of 117 for Pdia6

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0.022s
Type Details Score
Publication      
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
Publication      
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform
Allele
Name: protein disulfide isomerase associated 6; endonuclease-mediated mutation 2, Shanghai Model Organisms Center
Allele Type: Endonuclease-mediated
Attribute String: Null/knockout
Strain
Attribute String: coisogenic, endonuclease-mediated mutation, mutant strain
Allele
Name: protein disulfide isomerase associated 6; endonuclease-mediated mutation 1, Shanghai Model Organisms Center
Allele Type: Endonuclease-mediated
Attribute String: Conditional ready, No functional change
Strain
Attribute String: coisogenic, endonuclease-mediated mutation, mutant strain
Publication
First Author: Kimura T
Year: 2005
Journal: J Biol Chem
Title: Interactions among yeast protein-disulfide isomerase proteins and endoplasmic reticulum chaperone proteins influence their activities.
Volume: 280
Issue: 36
Pages: 31438-41
Protein Domain
Type: Family
Description: This entry represents a group disulfide-isomerases, including PDIA6 from animals, Mpd1 from yeasts and PDI22/PDI23 from Arabidopsis. Protein-disulfide isomerase (PDI) is a resident of the endoplasmic reticulum (ER) that catalyses the formation, reduction, and isomerization of disulfide bonds. PDIA6 is an active oxidoreductase with similar enzymatic properties to other PDIs; however, it doesn't seem to be involved directly in protein folding. Instead, it regulates the unfolded protein response (UPR) through controlling the decay of IRE1alpha signaling via disulfide-dependent association []. Mpd1 have oxidative refolding activity and interacts with Cne1, an integral membrane ER chaperone involved in folding and quality control of glycoproteins [].
Publication
First Author: Eletto D
Year: 2012
Journal: J Cell Sci
Title: Limitation of individual folding resources in the ER leads to outcomes distinct from the unfolded protein response.
Volume: 125
Issue: Pt 20
Pages: 4865-75
Publication  
First Author: Wen W
Year: 2024
Journal: Front Pharmacol
Title: Sex-specific effects of alcohol on neurobehavioral performance and endoplasmic reticulum stress: an analysis using neuron-specific MANF deficient mice.
Volume: 15
Pages: 1407576
Protein
Organism: Mus musculus/domesticus
Length: 440  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 440  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 445  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 391  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 445  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 445  
Fragment?: false