Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 5.3.4.1 extracted from

  • Walker, A.
    Protein disulfide isomerase and the endoplasmic reticulum in amyotrophic lateral sclerosis (2010), J. Neurosci., 30, 3865-3867.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.3.4.1

Inhibitors

Inhibitors Comment Organism Structure
additional information although PDI can be protective against mutant SOD1 aggregation and toxicity, aberrant S-nitrosylation of critical active site cysteine residues likely inactivates the normal protective function of PDI in amyotrophic lateral sclerosis spinal cords Homo sapiens
additional information although PDI can be protective against mutant SOD1 aggregation and toxicity, aberrant S-nitrosylation of critical active site cysteine residues likely inactivates the normal protective function of PDI in amyotrophic lateral sclerosis spinal cords Mus musculus
additional information although PDI can be protective against mutant SOD1 aggregation and toxicity, aberrant S-nitrosylation of critical active site cysteine residues likely inactivates the normal protective function of PDI in amyotrophic lateral sclerosis spinal cords Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum
-
 Mus musculus 5783
-
endoplasmic reticulum
-
 Homo sapiens 5783
-
endoplasmic reticulum
-
 Rattus norvegicus 5783
-

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Mus musculus
-
-
-
Rattus norvegicus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
spinal cord
-
 Mus musculus
-
spinal cord
-
 Homo sapiens
-
spinal cord
-
 Rattus norvegicus
-

Synonyms

Synonyms Comment Organism
PDI
-
 Mus musculus
PDI
-
 Homo sapiens
PDI
-
 Rattus norvegicus
protein disulfide isomerase
-
 Mus musculus
protein disulfide isomerase
-
 Homo sapiens
protein disulfide isomerase
-
 Rattus norvegicus

Expression

Organism Comment Expression
Homo sapiens PDI is induced by unfolded protein response, UPR, signaling transduction pathways activated by protein misfolding in the endoplasmic reticulum, overview. PDI is upregulated before symptom onset in spinal cords of ALS postmortem tissue up
Rattus norvegicus PDI is induced by unfolded protein response, UPR, signaling transduction pathways activated by protein misfolding in the endoplasmic reticulum, overview. PDI is upregulated before symptom onset in spinal cords of ALS postmortem tissue up
Mus musculus PDI is induced by unfolded protein response, UPR, signaling transduction pathways activated by protein misfolding in the endoplasmic reticulum, overview. PDI is upregulated before symptom onset in spinal cords of mutant SOD1G93A mice up

General Information

General Information Comment Organism
physiological function PDI is an abundant enzyme that forms, breaks, and isomerizes disulfide bonds and is therefore an important cellular defense against protein misfolding. PDI can be protective against mutant SOD1 aggregation and toxicity Mus musculus
physiological function PDI is an abundant enzyme that forms, breaks, and isomerizes disulfide bonds and is therefore an important cellular defense against protein misfolding. PDI can be protective against mutant SOD1 aggregation and toxicity Homo sapiens
physiological function PDI is an abundant enzyme that forms, breaks, and isomerizes disulfide bonds and is therefore an important cellular defense against protein misfolding. PDI can be protective against mutant SOD1 aggregation and toxicity Rattus norvegicus