A mitochondrial insertion directs substrate selection and engagement by ClpX

No abstract is available for this paper.

• Publication year

  2026

• Venue

  bioRxiv

• Publication date

  2026-02-23

• Fields of study

  Biology, Chemistry

• Identifiers
  DOI 10.64898/2026.02.23.707539PMCID PMC12970495
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar

• No claims are published for this paper.

• No concepts are published for this paper.

• Genetic determinants of micronucleus formation in vivo

  2024cited by this paper
• Cryo-EM structures of human ClpXP reveal mechanisms of assembly and proteolytic activation

  2024influential reference
• An adaptor for feedback regulation of heme biosynthesis by the mitochondrial protease CLPXP

  2024influential reference
• The AAA+ superfamily: a review of the structural and mechanistic principles of these molecular machines

  2021cited by this paper
• ATP hydrolysis tunes specificity of a AAA+ protease

  2021cited by this paper
• Mitochondrial ClpX activates an essential biosynthetic enzyme through partial unfolding

  2020influential reference
• Polymerase delta-interacting protein 38 (PDIP38) modulates the stability and activity of the mitochondrial AAA+ protease CLPXP

  2020cited by this paper
• Discovery and engineering of enhanced SUMO protease enzymes

  2018cited by this paper
• Regulated Proteolysis in Bacteria.

  2018cited by this paper
• Mutation in human CLPX elevates levels of δ-aminolevulinate synthase and protoporphyrin IX to promote erythropoietic protoporphyria

  2017cited by this paper
• Origins of tmRNA: the missing link in the birth of protein synthesis?

  2016cited by this paper
• Novel Mechanisms for Heme-dependent Degradation of ALAS1 Protein as a Component of Negative Feedback Regulation of Heme Biosynthesis*

  2016cited by this paper
• CLPP coordinates mitoribosomal assembly through the regulation of ERAL1 levels

  2016cited by this paper
• Mitochondrial ClpX Activates a Key Enzyme for Heme Biosynthesis and Erythropoiesis.

  2015influential reference
• AAA+ proteases: ATP-fueled machines of protein destruction.

  2011cited by this paper
• Crystal structures of asymmetric ClpX hexamers reveal nucleotide-dependent motions in a AAA+ protein-unfolding machine

  2009cited by this paper
• Diverse pore loops of the AAA+ ClpX machine mediate unassisted and adaptor-dependent recognition of ssrA-tagged substrates.

  2008cited by this paper
• Clp ATPases and ClpP proteolytic complexes regulate vital biological processes in low GC, Gram‐positive bacteria

  2007cited by this paper
• AAA+ proteins: have engine, will work

  2005cited by this paper
• Communication between ClpX and ClpP during substrate processing and degradation

  2004cited by this paper
• Crystal Structure of ClpX Molecular Chaperone from Helicobacter pylori*

  2003cited by this paper
• Functional Proteolytic Complexes of the Human Mitochondrial ATP-dependent Protease, hClpXP*

  2002cited by this paper
• Disassembly of the Mu transposase tetramer by the ClpX chaperone.

  1995cited by this paper
• Activity and specificity of Escherichia coli ClpAP protease in cleaving model peptide substrates.

  1994cited by this paper
• Isolation and characterization of ClpX, a new ATP-dependent specificity component of the Clp protease of Escherichia coli.

  1993cited by this paper
• THE OCCURRENCE AND DETERMINATION OF δ-AMINOLEVULINIC ACID AND PORPHOBILINOGEN IN URINE

  1956cited by this paper

• No citing papers are available for this paper.