Journal: Cells

Article Title: Inactivity of Peptidase ClpP Causes Primary Accumulation of Mitochondrial Disaggregase ClpX with Its Interacting Nucleoid Proteins, and of mtDNA

doi: 10.3390/cells10123354

Figure Lengend Snippet: Mitochondrial proteins (UniProt-IDs) with significant downregulation (upper part) and upregulation (lower part) in ClpP-null MEFs versus WT (3 versus 3). Factors with special relevance for this manuscript are highlighted in bold letters. Previously reported candidate ClpP cleavage substrates in mouse are identified at the right margin with citations of the relevant PubMed-ID number.

Article Snippet: PMPCB , mitochondrial targeting sequence cleavage , proteostasis , - , hetero-dimer with PMPCA , 56 , 0.02 , 1.4.

Techniques:

Journal: Cells

Article Title: Inactivity of Peptidase ClpP Causes Primary Accumulation of Mitochondrial Disaggregase ClpX with Its Interacting Nucleoid Proteins, and of mtDNA

doi: 10.3390/cells10123354

Figure Lengend Snippet: Significant accumulations of the above eleven mitochondrial matrix proteins were consistent between both PRLTS3 fibroblasts and ClpP-null MEFs, and partially consistent with ClpP-null brains (highlighted by gray background), although they are not known as interactors of ClpX or ClpB. All of them show a multimerized quaternary structure, and they partly associate with cofactors.

Article Snippet: PMPCB , mitochondrial targeting sequence cleavage , proteostasis , - , hetero-dimer with PMPCA , 56 , 0.02 , 1.4.

Techniques: Sequencing