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ProteomicsIn vivo trapping of proteins interacting with the chloroplast CLPC1 chaperone
The chloroplast stromal CLP protease system is essential for growth and development. It consists of a proteolytic CLP core complex that likely dynamically interacts with oligomeric rings of CLPC1, CLPC2 or CLPD AAA+ chaperones. These ATP-dependent chaperones are predicted to bind and unfold CLP prot...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2019-05-14 | PXD013494 | Pride
In vivo trapping-proteins interaction- chloroplast - clpc1 chaperone 
ProteomicsIn vivo trapping of proteins interacting with the chloroplast CLPC1 chaperone; potential substrates and adaptors
The chloroplast stromal CLP protease system is essential for growth and development. It consists of a proteolytic CLP core complex that likely dynamically interacts with oligomeric rings of CLPC1, CLPC2 or CLPD AAA+ chaperones. These ATP-dependent chaperones are predicted to bind and unfold CLP prot...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2019-04-10 | PXD013424 | Pride
Clpc1 chaperone in vivo trapping adaprotr substrate 
ProteomicsInteractome analysis of chloroplast ClpC1 chaperone in Arabidopsis thaliana
The chloroplast stromal CLP protease system is essential for growth and development, consisting of a proteolytic core complex that interacts with ClpC1, ClpC2, or ClpD AAA+ chaperones. In this study, an in vivo ClpC1 substrate trap with a C-terminal STREPII affinity tag was generated, and MS/MS anal...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2020-02-05 | PXD017400 | Pride
Clpc1 arabidopsis interactome chloroplast chaperone 
ProteomicsCLPC1 maintains chloroplast proteome and RNA homeostasis
In chloroplasts, homeostasis of the proteome maintained by protein synthesis, importation, and degradation is critical to the development of chloroplasts. The caseinolytic protease complex component CLPC1, a member of the HSP100 family of chaperones, not only facilitates the translocation of pre-pro...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2018-10-19 | PXD000869 | Pride
Clpc1 Rna Chloroplast Proteome Homeostasis 
ProteomicsEffect of depletion of clpP2, clpX and clpC1 genes on whole cell proteome profile of Mycobacterium tuberculosis H37Rv
Global protein alteration in Mycobacterium tuberculosis H37 RV ( Mtb-H37RV) having depletion of Clpx ,Clp2 and ClpC1 were accessed using 4 plex iTRAQ label.
ORGANISM(S): Mycobacterium tuberculosis H37Rv Mycobacterium tuberculosis 
2020-05-14 | PXD013589 | Pride
Mycobacterium clp 
ProteomicsInteractome analysis by shotgun proteomics identifies a novel substrate for Mycolicibacterium smegmatis unfoldase ClpC1
Tuberculosis remains a leading cause of worldwide infectious mortality and one of the top ten leading causes of death overall. While advances in public health have contributed to a reduction in tuberculosis cases, the prevalence of multidrug-resistant Mycobacterium tuberculosis (Mtb) (MDR-TB) infect...
ORGANISM(S): Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155) 
2022-12-12 | PXD030385 | Pride
Clp protease Unfoldase clpc1 Shotgun proteomics Tuberculosis Mycolicibacterium smegmatis 
TranscriptomicsClpC1-targeting peptide natural products differentially dysregulate the proteome of Mycobacterium tuberculosis.
Targeting the protein quality control system in Mycobacterium tuberculosis offers a powerful and largely untapped opportunity for antibiotic development. The ClpC1:ClpP1P2 protease is an essential component of the system and is involved in both regulatory and stress-related protein degradation. Seve...
ORGANISM(S): Mycobacterium tuberculosis H37Rv 
2025-11-20 | GSE310713 | GEO
ProteomicsProteomic analysis of WT, gun1-101, clpc1 and gun1clpc1
To understand the differences of the wild type, gun1, clpc1 and gun1clpc1 on the proteome level.
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2019-04-23 | PXD010730 | Pride
Clpc1 Gun1-101 Chloroplast Retrograde signaling 
UnknownRufomycin Targets ClpC1 Proteolysis in Mycobacterium tuberculosis and M. abscessus.
Not available
S-EPMC6395927 | biostudies-literature
UnknownInteractome Analysis Identifies MSMEI_3879 as a Substrate of Mycolicibacterium smegmatis ClpC1.
Not available
S-EPMC10433963 | biostudies-literature
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