Dataset Information

The interaction between NLRP1 and oxidized TRX1 involves a transient disulfide bond: LC-MS/MS Dataset

ABSTRACT: LC-MS/MS analysis of a gel slice containing a disulfide-cross-linked peptide chains between thioredoxin-1 and the NACHT-LRR domains of NLRP1

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Michael Geeson

LAB HEAD: Daniel A. Bachovchin

PROVIDER: PXD047547 | Pride | 2025-05-26

REPOSITORIES: Pride

ACCESS DATA

Dataset's files

Source:

			Action	DRS
	2143CH_S1_Sample_1_25cm_i40_DBachovchin.raw	Raw
	2143CH_S1_Sample_2_25cm_i40_DBachovchin.raw	Raw
	NLRP1_TRX1.fasta	Fasta
	SEARCH.zip	Other
	allSpectra.HCD.FTMS.iso_0.apl	Other

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Publications

The interaction between NLRP1 and oxidized TRX1 involves a transient disulfide bond.

Geeson Michael B MB Hsiao Jeffrey C JC Tsamouri Lydia P LP Ball Daniel P DP Bachovchin Daniel A DA

Cell chemical biology 20240111 5

NLRP1 is an innate immune receptor that detects pathogen-associated signals, assembles into a multiprotein structure called an inflammasome, and triggers a proinflammatory form of cell death called pyroptosis. We previously discovered that the oxidized, but not the reduced, form of thioredoxin-1 directly binds to NLRP1 and represses inflammasome formation. However, the molecular basis for NLRP1's selective association with only the oxidized form of TRX1 has not yet been established. Here, we lev ...[more]

PMID: 38215746

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