Reactome: A Curated Pathway Database

Query author contributions in Reactome

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Pathways reviewed by Cowan, Nicholas J (389981)

DB_ID Name
389957 Prefoldin mediated transfer of substrate to CCT/TriC
389958 Cooperation of Prefoldin and TriC/CCT in actin and tubulin folding
389960 Formation of tubulin folding intermediates by CCT/TriC
389977 Post-chaperonin tubulin folding pathway
390450 Folding of actin by CCT/TriC
390471 Association of TriC/CCT with target proteins during biosynthesis
390466 Chaperonin-mediated protein folding
391251 Protein folding

Details on Person Cowan, Nicholas J

Class:IdPerson:389981
_displayNameCowan, Nicholas J
_timestamp2017-08-22 20:40:46
affiliation[Affiliation:69324] NYU School of Medicine, Department of Biochemistry
created[InstanceEdit:389975] Matthews, L, 2009-01-21 19:24:07
firstnameNicholas J
initialNJ
modified[InstanceEdit:1237444] D'Eustachio, P, 2011-03-30
[InstanceEdit:8932050] D'Eustachio, Peter, 2016-07-20
surnameCowan
(author)[LiteratureReference:389962] The alpha- and beta-tubulin folding pathways
[LiteratureReference:391406] Prefoldin, a chaperone that delivers unfolded proteins to cytosolic chaperonin
[LiteratureReference:391413] A cytoplasmic chaperonin that catalyzes beta-actin folding
[LiteratureReference:391419] Two cofactors and cytoplasmic chaperonin are required for the folding of alpha- and beta-tubulin
[LiteratureReference:391451] Chaperonin-mediated folding of vertebrate actin-related protein and gamma-tubulin
[LiteratureReference:391508] Pathway leading to correctly folded beta-tubulin
[LiteratureReference:391523] Type II chaperonins, prefoldin, and the tubulin-specific chaperones
[LiteratureReference:391536] Tubulin subunits exist in an activated conformational state generated and maintained by protein cofactors
[LiteratureReference:391553] Prefoldin-nascent chain complexes in the folding of cytoskeletal proteins
[LiteratureReference:391789] Facilitated folding of actins and tubulins occurs via a nucleotide-dependent interaction between cytoplasmic chaperonin and distinctive folding intermediates
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