Affinage

TOMM5

Mitochondrial import receptor subunit TOM5 homolog · UniProt Q8N4H5

Length
51 aa
Mass
6.0 kDa
Annotated
2026-06-10
46 papers in source corpus 26 papers cited in narrative 25 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 7/7 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

TOMM5 (Tom5) is a small C-tail-anchored subunit of the translocase of the outer mitochondrial membrane (TOM complex), where it surrounds the Tom40 β-barrel channel within the dimeric general import pore alongside Tom6, Tom7, and Tom22 (PMID:9774667, PMID:9603986, PMID:28802041, PMID:33083003). Within the assembled complex it behaves as a peripheral, modulatory element: it can be released from the stable Tom40-Tom22 core under stringent detergent conditions while preprotein remains bound, yet its deletion destabilizes the TOM complex and reduces import efficiency in yeast in a species-specific manner (PMID:11259583, PMID:15701639). Beyond steady-state structure, Tom5 acts as an early biogenesis factor that initiates and promotes integration of newly imported Tom40 at the SAM complex, advancing Tom40 from the first to the second SAM-associated assembly stage downstream of Mim1 and antagonized by Tom7 (PMID:11276259, PMID:20026336, PMID:21059357, PMID:20668160). Tom5 confers substrate specificity at the import pore, being required for biogenesis of porin/VDAC and VDAC-like β-barrels, the small Tim intermembrane-space proteins, and Tafazzin, while being dispensable for pathways used by Bcl-2α and cytochrome c (PMID:11266446, PMID:10397776, PMID:16135531, PMID:12419260, PMID:12628251). Its outer-membrane targeting is encoded by a defined C-tail-anchor signal in which transmembrane-segment length, a correctly positioned proline residue, and the relationship of the TMS to the C-terminal segment are the critical determinants (PMID:12006657, PMID:12896971). Tom5 also serves as a physical hub linking mitochondria to other membranes and to quality-control signaling: it binds all ER membrane protein complex (EMC) subunits to support ER–mitochondria tethering and phosphatidylserine transfer (PMID:25313861), and it directly binds the C-lobe of the PINK1 kinase domain, organizing a symmetric TOM–VDAC array that retains and stabilizes PINK1 at the mitochondrial surface for PINK1-Parkin mitophagy signaling (PMID:40080546, PMID:41266657). A Tomm5 knockout mouse develops an organ-restricted lung phenotype of cryptogenic organizing pneumonia (PMID:22688586).

Mechanistic history

Synthesis pass · year-by-year structured walk · 16 steps
  1. 1998 High

    Established that Tom5 is a bona fide constituent of the TOM general import pore that bridges surface receptors and the Tom40 channel, defining its place in the import machinery.

    Evidence Biochemical fractionation, native PAGE and immunoprecipitation of the ~400 kDa GIP complex in yeast

    PMID:9603986 PMID:9774667

    Open questions at the time
    • Did not resolve whether Tom5 is core or peripheral
    • No structural placement relative to Tom40
  2. 1999 Medium

    Showed that Tom5 confers substrate selectivity by being essential for a receptor-independent small Tim import pathway, indicating the pore subunits define distinct import routes.

    Evidence In vitro import assays in yeast strains lacking individual TOM components

    PMID:10397776

    Open questions at the time
    • Single lab
    • Molecular basis of Tom5 selectivity for small Tims not defined
  3. 2000 Medium

    Provided the first structural description of the Tom5 cytosolic domain, establishing a defined helical core.

    Evidence CD and NMR (NOESY) spectroscopy of the cytosolic domain

    PMID:10683449

    Open questions at the time
    • No functional mutagenesis link to the helical structure
    • Isolated domain, not in complex
  4. 2001 High

    Distinguished Tom5 as a peripheral/modulatory subunit while assigning it an active role in Tom40 assembly, showing the protein contributes to biogenesis rather than the core translocation unit.

    Evidence Urea/detergent dissociation, channel reconstitution, and pulse-chase assembly assays with native PAGE in yeast

    PMID:11259583 PMID:11276259

    Open questions at the time
    • Mechanism by which Tom5 promotes Tom40 progression unresolved at this stage
    • Order relative to other assembly factors unknown
  5. 2001 Medium

    Extended Tom5's substrate role to β-barrel biogenesis by showing porin/VDAC import requires Tom5.

    Evidence In vitro import assay using yeast tom5 mutant mitochondria

    PMID:11266446

    Open questions at the time
    • Single lab
    • Does not separate import defect from TOM destabilization
  6. 2002 High

    Defined the C-tail-anchor targeting determinants of Tom5 in a mammalian system, identifying TMS length, a TMS proline, and C-segment charge as the targeting code.

    Evidence Systematic TMS/flanking mutagenesis with GFP reporter, microscopy and fractionation in COS-7 cells

    PMID:12006657

    Open questions at the time
    • Single lab
    • Receptor/insertase machinery for Tom5 targeting not identified
  7. 2002 Medium

    Sharpened pathway specificity by showing some outer-membrane proteins (Bcl-2α) bypass Tom5 and Tom40, demonstrating Tom5 dependence is substrate-class specific.

    Evidence In vitro import into yeast mitochondria lacking individual TOM subunits (negative result for Bcl-2α); PorB import dependent on Tom5

    PMID:11953311 PMID:12419260

    Open questions at the time
    • Single lab
    • Alternative insertion route for Bcl-2α not molecularly mapped
  8. 2003 High

    Refined the targeting signal with functional complementation, showing TMS length and a positioned proline, but not C-segment positive charge, are required for Tom5 assembly into TOM.

    Evidence GFP reporter localization, blue native PAGE and complementation of ts deltaTOM5 yeast

    PMID:12896971

    Open questions at the time
    • Discrepancy with COS-7 charge requirement not reconciled
    • Single lab
  9. 2003 Medium

    Further delineated substrate specificity by showing cytochrome c import is Tom5-independent.

    Evidence In organello import assay in yeast lacking individual Tom proteins (negative result)

    PMID:12628251

    Open questions at the time
    • Single lab
    • Negative result; pathway used by cytochrome c not defined here
  10. 2005 High

    Established Tom5's role in TOM structural integrity and added Tafazzin to its substrate repertoire, while revealing species-specific dependence on Tom5 for complex stability.

    Evidence Cross-species complementation, native PAGE and import assays in yeast and N. crassa; Taz1 import assays in mutant backgrounds

    PMID:15701639 PMID:16135531

    Open questions at the time
    • Basis for yeast vs Neurospora difference unexplained
    • Taz1 import single lab
  11. 2010 High

    Resolved the mechanistic order of TOM assembly, placing Tom5 as the initiating step of Tom40 integration at SAM, downstream of Mim1 and antagonized by Tom7.

    Evidence Pulse-chase assembly assays, native PAGE and genetic epistasis/suppression in yeast deletion strains

    PMID:20026336 PMID:20668160 PMID:21059357

    Open questions at the time
    • Structural basis of Tom5-Tom40 SAM intermediate unknown
    • How Tom7 antagonizes Tom5 not defined
  12. 2014 High

    Revealed an inter-organelle function by showing Tom5 physically links the ER EMC to mitochondria to enable lipid transfer, expanding its role beyond import.

    Evidence Yeast genetic screen, reciprocal Co-IP of EMC with Tom5, PS transfer assay and rescue by artificial tether

    PMID:25313861

    Open questions at the time
    • Which EMC subunit contacts Tom5 directly not mapped
    • Structural detail of the tether absent
  13. 2017 High

    Placed Tom5 structurally around the Tom40 pore in the dimeric TOM core complex.

    Evidence Cryo-EM structure of the N. crassa TOM core complex

    PMID:28802041

    Open questions at the time
    • No bound substrate captured
    • Human complex not resolved here
  14. 2020 High

    Resolved the human TOM core complex and linked Tom5 to the Tom40 N-terminal segment that serves as an exit/recruitment site for presequence-lacking preproteins.

    Evidence Single-particle cryo-EM of the human TOM core complex

    PMID:33083003

    Open questions at the time
    • No trapped substrate at the Tom5 site
    • Functional test of the recruitment role not in this study
  15. 2025 High

    Connected Tom5 to mitophagy quality control by showing it directly binds the PINK1 kinase C-lobe and organizes the TOM-VDAC array to retain PINK1 at the mitochondrial surface.

    Evidence Cryo-EM at 3.1 Å of PINK1 at the TOM-VDAC array plus TOMM5 genetic ablation/knockdown in PINK1 retention assays; HSP90-CDC37 overlap shown by preprint cryo-EM

    PMID:40080546 PMID:41266657 PMID:bio_10.1101_2025.10.17.682828

    Open questions at the time
    • TOM5-PINK1 interface not validated by TOM5 mutagenesis (HSP90 overlap is preprint)
    • How Tom5 import role and PINK1-binding role are coordinated unclear
  16. 2012 Medium

    Showed an organism-level consequence of TOMM5 loss with an organ-restricted lung phenotype.

    Evidence Tomm5(-/-) knockout mice with lung histopathology (cryptogenic organizing pneumonia)

    PMID:22688586

    Open questions at the time
    • No molecular mechanism for lung specificity
    • Link to import or PINK1 functions not established

Open questions

Synthesis pass · forward-looking unresolved questions
  • How Tom5's distinct roles—pore subunit, Tom40 assembly initiator, substrate-selectivity factor, EMC tether, and PINK1 retention platform—are mechanistically coordinated, and how loss of these activities produces the tissue-specific in vivo phenotype, remains unresolved.
  • No integrated model linking import and signaling roles
  • Mechanism of lung-restricted phenotype unknown
  • TOM5-PINK1 interface not validated by direct mutagenesis

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0005198 structural molecule activity 3 GO:0060090 molecular adaptor activity 2
Pathway
R-HSA-9609507 Protein localization 4 R-HSA-392499 Metabolism of proteins 2 R-HSA-9612973 Autophagy 2
Partners
EMCPINK1TOMM22TOMM40TOMM6TOMM7VDAC2
Complex memberships
SAM-Tom5/Tom40 assembly intermediateTOM complexTOM-VDAC array

Evidence

Reading pass · 25 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1998 Tom5 is a component of the general import pore (GIP) complex of the TOM translocase, where it participates in preprotein transfer from surface receptors (Tom20, Tom70) to the channel protein Tom40. The GIP complex (~400 kDa) contains Tom40, Tom22, Tom5, Tom6, and Tom7. Biochemical fractionation, native PAGE, immunoprecipitation, yeast genetics Molecular and cellular biology High 9603986 9774667
2001 Tom5 associates with the precursor of Tom40 during the first assembly intermediate (~250 kDa) at the sorting and assembly machinery (SAM complex), forming a step prior to the 100 kDa and 400 kDa mature TOM complex. Tom5 is required for progression of Tom40 assembly from the SAM complex to the mature TOM complex. Pulse-chase assembly assays, native PAGE, yeast mutant analysis Nature structural biology High 11276259
2001 The Tom40-Tom22 core is the stable unit retaining preproteins in the GIP complex; Tom5 (along with Tom6 and Tom7) is released under stringent detergent conditions while preprotein remains bound, indicating Tom5 is a peripheral/modulatory component rather than part of the core translocation unit. Urea/detergent dissociation assays, native PAGE, channel activity reconstitution Molecular and cellular biology High 11259583
2001 Tom5 is required for the import and assembly of porin (VDAC) into the mitochondrial outer membrane, as shown by reduced import in tom5 mutant mitochondria. Porin biogenesis requires Tom5 in addition to Tom20, Tom22, Tom40, and Tom7. In vitro import assay with yeast tom5 mutant mitochondria The Journal of cell biology Medium 11266446
1999 Tom5 of the GIP complex is crucial for the import of small Tim proteins of the intermembrane space, representing a third novel import pathway in which surface receptors (Tom20, Tom70) are dispensable but Tom5 is essential. In vitro import assays using yeast strains lacking individual TOM components Molecular biology of the cell Medium 10397776
2002 Tom5 is required for import of bacterial PorB (a VDAC-like beta-barrel protein) into the mitochondrial outer membrane in vitro; insertion is dependent on Tom5, Tom20, and Tom40 but independent of Tom70. In vitro import assay into isolated mitochondria with antibody inhibition of specific TOM subunits The EMBO journal Medium 11953311
2002 The transmembrane segment (TMS) length, proline residue position in the TMS, and positive charges in the C-terminal segment (C-segment) together constitute the mitochondrial targeting signal of Tom5 as a C-tail-anchored protein. Reduction of net positive charge in the C-segment causes mislocalization to intracellular membranes; elongation of the TMS or separation of TMS and C-segment impairs targeting. Systematic deletion/mutation analysis of Tom5 TMS and flanking regions with GFP reporter, confocal microscopy, cell fractionation in COS-7 cells Molecular biology of the cell High 12006657
2003 Correct targeting and assembly of Tom5 into the TOM complex requires an appropriate TMS length (not merely hydrophobicity), a proline residue at the correct position in the TMS with specific flanking residues, but unlike other C-tail-anchored outer membrane proteins, does not require positive charges in the C-terminal segment. A minimal targeting signal (Ser-Pro-Met in Leu-Ala repeat context) is sufficient for mitochondrial targeting and functional complementation. In vivo GFP reporter assays, blue native PAGE, complementation of temperature-sensitive deltaTOM5 yeast cells The Journal of biological chemistry High 12896971
2000 The cytosolic domain of Tom5 forms a stable helical core between residues E11 and R15, with a less structurally rigid helix extending to the C-terminus, as determined by CD and NMR spectroscopy. Circular dichroism (CD) and NMR (NOESY) spectroscopy FEBS letters Medium 10683449
2005 Tom5 is required for maintaining the structural integrity of the TOM complex in yeast; deletion of TOM5 destabilizes the TOM complex and reduces protein import efficiency. In Neurospora crassa, Tom5 deletion does not affect TOM stability or import efficiency, indicating a species-specific structural role. Tom5 crosses the outer membrane with its C-terminus facing the IMS. Identification of Neurospora Tom5 by sequence homology; TOM complex stability assessed by native PAGE; import assays in deltaTOM5 yeast and N. crassa; complementation assays The Journal of biological chemistry High 15701639
2005 Transport of Tafazzin (Taz1) into mitochondria depends on the receptor Tom5 of the TOM complex and the small Tim proteins of the IMS, but is independent of the SAM complex. This establishes Tom5 as required for import of this outer membrane IMS-exposed protein. In vitro import assays into yeast mitochondria lacking individual TOM/SAM/Tim components Molecular biology of the cell Medium 16135531
2009 A Tom5-Tom40 subcomplex associates with the SAM core complex to form a large SAM-Tom5/Tom40 assembly that binds the alpha-helical precursor of Tom6 after its Mim1-dependent membrane insertion, functioning in the biogenesis of alpha-helical TOM subunits. Native PAGE, co-immunoprecipitation, pulse-chase assembly assays in yeast mutants Journal of molecular biology High 20026336
2010 Tom5 plays a stimulatory role in TOM complex biogenesis at an early stage of Tom40 assembly at the SAM complex; Tom5 promotes progression of Tom40 from the first SAM stage to the second SAM stage, and Tom5 assembly with Tom40 at the SAM complex is the direct initiation step of newly imported Tom40 assembly. This function is antagonized by Tom7. Pulse-chase assembly assays, native PAGE, yeast genetic analysis of deletion strains Journal of molecular biology High 20668160 21059357
2010 Tom5 is required for the second stage of Tom40 interaction with the SAM complex during TOM biogenesis. Mim1-deficient mitochondria accumulate Tom40 at the first SAM stage similarly to Tom5-deficient mitochondria, and Tom5 overexpression suppresses the Tom40 assembly defect in mim1Δ cells, placing Mim1 function upstream of Tom5 in Tom40 biogenesis. Pulse-chase assembly assay, native PAGE, genetic epistasis in yeast deletion strains Molecular biology of the cell High 20668160
2017 Cryo-EM structure of the Neurospora crassa TOM core complex reveals Tom5 transmembrane segment surrounds the Tom40 β-barrel pore within a symmetrical dimeric complex (148 kDa), together with Tom6, Tom7, and Tom22. Cryo-electron microscopy (cryo-EM) structure determination Cell High 28802041
2020 Cryo-EM structure of the human TOM core complex at near-atomic resolution shows Tom5 surrounds the Tom40 channel as part of the dimeric complex; the N-terminal segment of Tom40 spans the channel to interact with Tom5 at the periphery of the dimer, and this region serves as an exit/recruitment site for presequence-lacking preproteins. Single-particle cryo-EM structure determination Cell discovery High 33083003
2025 Cryo-EM structure of PINK1 at the TOM-VDAC array shows Tom5 facilitates the symmetric arrangement of two TOM core complexes around a central VDAC2 dimer, and Tom5 directly binds the C-lobe of PINK1 kinase domain, stabilizing PINK1 at the mitochondrial surface. Tom5 (as part of TOM) is required for PINK1 retention on the mitochondrial surface. Cryo-EM structure determination (3.1 Å resolution), genetic ablation of TOMM5 in cell-based PINK1 retention assays Science (New York, N.Y.) High 40080546
2025 TOM (including subunit TOMM5) is required for PINK1 retention on the mitochondrial surface. Loss of MMP stalls PINK1 during transfer from TOM to TIM23, causing accumulation at TOM; ablation of TOMM5 abrogates PINK1 retention. Genome-wide screen with Parkin reporter, siRNA knockdown of TOMM5, cell-based PINK1 localization assays The EMBO journal Medium 41266657
2014 All EMC (ER membrane protein complex) proteins interact with the mitochondrial TOM complex protein Tom5, and this interaction is important for phosphatidylserine (PS) transfer from ER to mitochondria and for cell growth. The EMC-TOM5 interaction supports ER-mitochondria tethering, required for phospholipid synthesis. Yeast genetic screen for lipid exchange mutants, co-immunoprecipitation of EMC with Tom5, PS transfer assay, growth assays in EMC/ERMES double mutants PLoS biology High 25313861
2002 Bcl-2alpha insertion into the mitochondrial outer membrane does not require Tom5 or Tom40, indicating Bcl-2alpha bypasses the general import pore and follows a distinct pathway from Tom20 into the outer membrane. In vitro import assay into yeast mitochondria lacking individual TOM subunits (negative result for Tom5 requirement) Journal of molecular biology Medium 12419260
2003 Tom5 is not required for cytochrome c import into the mitochondrial IMS; neither Tom5, Tom6, nor Tom7 are needed for cytochrome c import, establishing that cytochrome c uses a Tom5-independent pathway. In organello import assay in yeast mutants lacking individual Tom proteins Journal of molecular biology Medium 12628251
2012 Tomm5 knockout mice develop a lung-specific phenotype of cryptogenic organizing pneumonia (COP/BOOP), characterized by intra-alveolar fibrosis with fibroblasts/myofibroblasts, macrophage and eosinophil infiltration, while performing normally in other broad phenotyping assays. Tomm5(-/-) knockout mouse generation; histopathological analysis of lung tissue Veterinary pathology Medium 22688586
2024 TOM5 regulates mitochondrial membrane potential in alveolar epithelial cells; TOM5 reduces early apoptosis and promotes cell proliferation in vitro. TOM5 expression is increased in lung tissue of organizing pneumonia patients and correlates with collagen deposition. In vitro knockdown/overexpression in alveolar epithelial cells with mitochondrial membrane potential assay; bleomycin-induced murine OP model Redox report Low 38794801
2011 A fusion protein of wild-type p53 with the mitochondrial transmembrane domain of Tom5 (p53-Tom5) localizes exclusively to mitochondria in ARF-null A549 lung cancer cells, induces mitochondrial dysfunction and cytochrome c release, and suppresses cell proliferation, whereas wild-type p53 alone does not. This demonstrates Tom5's TMS is sufficient to direct a cytosolic protein to mitochondria and cause direct mitochondrial dysfunction. Plasmid transfection, confocal microscopy for localization, cell proliferation assay, cytochrome c release assay, mitochondrial function assay Biological & pharmaceutical bulletin Low 21467644
2025 HSP90-CDC37 chaperone complex covers the C-terminal extension (CTE) of PINK1, which overlaps with interaction sites for TOM5 and TOM20. This structural finding indicates that HSP90 and TOM5 binding to PINK1 are mutually exclusive, providing mechanistic insight into how PINK1 transitions from cytosolic chaperone to TOM complex engagement. Cryo-EM structure of PINK1-HSP90-CDC37 complex bioRxivpreprint Low bio_10.1101_2025.10.17.682828

Source papers

Stage 0 corpus · 46 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2014 A conserved endoplasmic reticulum membrane protein complex (EMC) facilitates phospholipid transfer from the ER to mitochondria. PLoS biology 263 25313861
1993 Identification and genetic analysis of normal and mutant phytoene synthase genes of tomato by sequencing, complementation and co-suppression. Plant molecular biology 214 8343597
1998 Preprotein translocase of the outer mitochondrial membrane: molecular dissection and assembly of the general import pore complex. Molecular and cellular biology 212 9774667
2005 Taz1, an outer mitochondrial membrane protein, affects stability and assembly of inner membrane protein complexes: implications for Barth Syndrome. Molecular biology of the cell 174 16135531
2001 Multistep assembly of the protein import channel of the mitochondrial outer membrane. Nature structural biology 165 11276259
2001 Protein import channel of the outer mitochondrial membrane: a highly stable Tom40-Tom22 core structure differentially interacts with preproteins, small tom proteins, and import receptors. Molecular and cellular biology 147 11259583
2017 Cryo-EM Structure of the TOM Core Complex from Neurospora crassa. Cell 142 28802041
2001 Biogenesis of porin of the outer mitochondrial membrane involves an import pathway via receptors and the general import pore of the TOM complex. The Journal of cell biology 134 11266446
1998 Mitochondria-targeting sequence, a multi-role sorting sequence recognized at all steps of protein import into mitochondria. Journal of biochemistry 131 9603986
2002 Characterization of signal that directs C-tail-anchored proteins to mammalian mitochondrial outer membrane. Molecular biology of the cell 128 12006657
2020 Atomic structure of human TOM core complex. Cell discovery 110 33083003
1999 Biogenesis of Tim proteins of the mitochondrial carrier import pathway: differential targeting mechanisms and crossing over with the main import pathway. Molecular biology of the cell 101 10397776
2009 Two modular forms of the mitochondrial sorting and assembly machinery are involved in biogenesis of alpha-helical outer membrane proteins. Journal of molecular biology 86 20026336
2010 Biogenesis of mitochondria: dual role of Tom7 in modulating assembly of the preprotein translocase of the outer membrane. Journal of molecular biology 76 21059357
2002 VDAC and the bacterial porin PorB of Neisseria gonorrhoeae share mitochondrial import pathways. The EMBO journal 74 11953311
2002 Bcl-2 and porin follow different pathways of TOM-dependent insertion into the mitochondrial outer membrane. Journal of molecular biology 65 12419260
2023 Intratumoral microbial heterogeneity affected tumor immune microenvironment and determined clinical outcome of HBV-related HCC. Hepatology (Baltimore, Md.) 60 37114494
2010 Assembly of the mitochondrial protein import channel: role of Tom5 in two-stage interaction of Tom40 with the SAM complex. Molecular biology of the cell 57 20668160
2005 Role of Tom5 in maintaining the structural stability of the TOM complex of mitochondria. The Journal of biological chemistry 51 15701639
2003 Targeting and assembly of mitochondrial tail-anchored protein Tom5 to the TOM complex depend on a signal distinct from that of tail-anchored proteins dispersed in the membrane. The Journal of biological chemistry 48 12896971
2025 Structure of human PINK1 at a mitochondrial TOM-VDAC array. Science (New York, N.Y.) 44 40080546
2000 The transport machinery for the import of preproteins across the outer mitochondrial membrane. The international journal of biochemistry & cell biology 33 10661891
2021 The receptor subunit Tom20 is dynamically associated with the TOM complex in mitochondria of human cells. Molecular biology of the cell 32 34347503
2003 Biogenesis of yeast mitochondrial cytochrome c: a unique relationship to the TOM machinery. Journal of molecular biology 32 12628251
1995 Isolation and characterisation of a melon cDNA clone encoding phytoene synthase. Plant molecular biology 25 7766896
2016 Nucleo-mitochondrial interaction of yeast in response to cadmium sulfide quantum dot exposure. Journal of hazardous materials 23 27890358
2008 Dynamics of the preprotein translocation channel of the outer membrane of mitochondria. Biophysical journal 22 18456827
2020 Structural snapshot of the mitochondrial protein import gate. The FEBS journal 19 33305524
2017 Pharmacogenetic meta-analysis of baseline risk factors, pharmacodynamic, efficacy and tolerability endpoints from two large global cardiovascular outcomes trials for darapladib. PloS one 18 28753643
2024 Ribosome Profiling and Mass Spectrometry Reveal Widespread Mitochondrial Translation Defects in a Striatal Cell Model of Huntington Disease. Molecular & cellular proteomics : MCP 15 38447791
2011 An insulator loop resides between the synthetically interacting elements of the human/rat conserved breast cancer susceptibility locus MCS5A/Mcs5a. Nucleic acids research 15 21914726
2010 LILBID-mass spectrometry of the mitochondrial preprotein translocase TOM. Journal of physics. Condensed matter : an Institute of Physics journal 14 21339618
2011 Genetic and epigenetic variations contributed by Alu retrotransposition. BMC genomics 13 22185517
2022 Structural overview of the translocase of the mitochondrial outer membrane complex. Biophysics and physicobiology 12 35859989
2012 Alterations in metabolism-related genes induced in SHSY5Y cells by okadaic acid exposure. Journal of toxicology and environmental health. Part A 12 22788371
2012 Cryptogenic organizing pneumonia in Tomm5(-/-) mice. Veterinary pathology 9 22688586
2025 A unified mechanism for mitochondrial damage sensing in PINK1-Parkin-mediated mitophagy. The EMBO journal 7 41266657
2024 Identification of MAP1LC3A as a promising mitophagy-related gene in polycystic ovary syndrome. Scientific reports 7 39043888
2000 Structure of the cytosolic domain of TOM5, a mitochondrial import protein. FEBS letters 7 10683449
2023 Diagnostic model based on key autophagy-related genes in intervertebral disc degeneration. BMC musculoskeletal disorders 6 38041088
2011 Proapoptotic action of p53-Tom5 in p53-resistant A549 human non-small cell lung cancer cells through direct mitochondrial dysfunction. Biological & pharmaceutical bulletin 5 21467644
2025 Structure of an ex vivoDrosophila TOM complex determined by single-particle cryoEM. IUCrJ 2 39575538
2024 TOM5 regulates the mitochondrial membrane potential of alveolar epithelial cells in organizing pneumonia. Redox report : communications in free radical research 1 38794801
2024 Identification of new therapeutic targets related to endoplasmic reticulum stress and mitochondrial dysfunction to reduce the risk of rupture in degenerative ascending aortic aneurysm. Clinica e investigacion en arteriosclerosis : publicacion oficial de la Sociedad Espanola de Arteriosclerosis 1 39424523
2022 Isolation of Plant Mitochondria Using Affinity Purification. Methods in molecular biology (Clifton, N.J.) 0 34545483
2022 In Vivo Epitope Tagging of Plant Mitochondria. Methods in molecular biology (Clifton, N.J.) 0 35188666

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