Query author contributions in Reactome

Reactome depends on collaboration between our curation team and outside experts to assemble and peer-review its pathway modules. The integration of ORCID within Reactome enables us to meet a key challenge with authoring, curating and reviewing biological information by incentivizing and crediting the external experts that contribute their expertise and time to the Reactome curation process. More information is available at ORCID and Reactome.

If you have an ORCID ID that is not listed on this page, please forward this information to us and we will update your Reactome pathway records.

Details on Person TLR folding by chaperones GP96 and CNPY3

Class:Id	Reaction:1678923
_displayName	TLR folding by chaperones GP96 and CNPY3
_doRelease	TRUE
_timestamp	2012-03-01 11:23:52
authored	[InstanceEdit:1679075] Shamovsky, V, 2011-10-19
compartment	[Compartment:17957] endoplasmic reticulum lumen [Compartment:12045] endoplasmic reticulum membrane
created	[InstanceEdit:1679075] Shamovsky, V, 2011-10-19
edited	[InstanceEdit:2129343] Shamovsky, V, 2012-02-19
input	[CandidateSet:1679009] TLR7/8/9 [endoplasmic reticulum membrane] [Homo sapiens] [SimpleEntity:211579] ATP [endoplasmic reticulum membrane] [EntityWithAccessionedSequence:1678932] CNPY3 [endoplasmic reticulum lumen] [Homo sapiens] [Complex:1678941] Apo-GP96 dimer [endoplasmic reticulum lumen] [Homo sapiens] [SimpleEntity:211579] ATP [endoplasmic reticulum membrane] [CandidateSet:1679009] TLR7/8/9 [endoplasmic reticulum membrane] [Homo sapiens] [EntityWithAccessionedSequence:1678932] CNPY3 [endoplasmic reticulum lumen] [Homo sapiens]
isChimeric	FALSE
literatureReference	[LiteratureReference:1678954] gp96, an endoplasmic reticulum master chaperone for integrins and Toll-like receptors, selectively regulates early T and B lymphopoiesis [LiteratureReference:1679047] Endoplasmic reticulum HSP90b1 (gp96, grp94) optimizes B-cell function via chaperoning integrin and TLR but not immunoglobulin [LiteratureReference:1679041] Heat shock protein gp96 is a master chaperone for toll-like receptors and is important in the innate function of macrophages [LiteratureReference:1679039] Tumor rejection antigen gp96/grp94 is an ATPase: implications for protein folding and antigen presentation [LiteratureReference:1678975] Folding of Toll-like receptors by the HSP90 paralogue gp96 requires a substrate-specific cochaperone [LiteratureReference:2065192] The Molecular Chaperone gp96/GRP94 Interacts With Toll-Like Receptors And Integrins Via Its C-Terminal Hydrophobic Domain
modified	[InstanceEdit:1679571] Shamovsky, V, 2011-10-20 [InstanceEdit:2065193] Shamovsky, V, 2012-01-20 [InstanceEdit:2123509] Shamovsky, V, 2012-02-14 [InstanceEdit:2129010] Shamovsky, V, 2012-02-19 [InstanceEdit:2143409] Shamovsky, V, 2012-02-24 [InstanceEdit:2153489] Shamovsky, V, 2012-02-28 [InstanceEdit:9830342] Matthews, Lisa, 2023-03-08
name	TLR folding by chaperones GP96 and CNPY3
output	[Complex:1679076] ATP-bound Gp96 dimer:CNPY3:TLR7/8/9 [endoplasmic reticulum membrane] [Homo sapiens]
releaseDate	2012-03-13
reviewed	[InstanceEdit:2121211] Gillespie, ME, 2012-02-09 [InstanceEdit:2153487] Leifer, CA, Rose II, WA, 2012-02-28
reviewStatus	[ReviewStatus:9821382] five stars
species	[Species:48887] Homo sapiens
stableIdentifier	[StableIdentifier:2158159] R-HSA-1678923.2
summation	[Summation:1679053] GP96 (also known as GRP94, HSP90b1), a paralogue of HSP90 in...
(hasEvent)	[Pathway:1679131] Trafficking and processing of endosomal TLR [Homo sapiens]
(precedingEvent)	[Reaction:1678944] Folded full-length TLR7/8/9 dissociates from the GP96:CNPY3 complex [Homo sapiens]
[Change default viewing format]

No pathways have been reviewed or authored by TLR folding by chaperones GP96 and CNPY3 (1678923)