Evidence map›Paper›PMID 35346689›Full record

ReviewThe Journal of biological chemistry2022

Mitochondrial protein translocation machinery: From TOM structural biogenesis to functional regulation.

Ulfat Mohd Hanif Sayyed, Radhakrishnan Mahalakshmi

Open access · goldAbstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
3.6field-weighted citation impact, top 6% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

31 citing papers in PubMed, 42 citations in OpenAlex.

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  13. Serotonergic Regulation in Alzheimer's Disease.International journal of molecular sciences · 2025
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Ulfat Mohd Hanif SayyedMolecular Biophysics Laboratory, Indian Institute of Science Education and Research, Bhopal, India.
Radhakrishnan MahalakshmiMolecular Biophysics Laboratory, Indian Institute of Science Education and Research, Bhopal, India. Electronic address: maha@iiserb.ac.in.
Indian Institute of Science Education and Research, Bhopal · IN

Funding

DBT-Wellcome Trust India Alliance IA/I/14/1/501305DBT-Wellcome Trust India Alliance IA/S/20/2/505182Wellcome Trust IA/I/14/1/501305Wellcome Trust IA/S/20/2/505182
6 · The paper itself

Abstract

The human mitochondrial outer membrane is biophysically unique as it is the only membrane possessing transmembrane β-barrel proteins (mitochondrial outer membrane proteins, mOMPs) in the cell. The most vital of the three mOMPs is the core protein of the translocase of the outer mitochondrial membrane (TOM) complex. Identified first as MOM38 in Neurospora in 1990, the structure of Tom40, the core 19-stranded β-barrel translocation channel, was solved in 2017, after nearly three decades. Remarkably, the past four years have witnessed an exponential increase in structural and functional studies of yeast and human TOM complexes. In addition to being conserved across all eukaryotes, the TOM complex is the sole ATP-independent import machinery for nearly all of the ∼1000 to 1500 known mitochondrial proteins. Recent cryo-EM structures have provided detailed insight into both possible assembly mechanisms of the TOM core complex and organizational dynamics of the import machinery and now reveal novel regulatory interplay with other mOMPs. Functional characterization of the TOM complex using biochemical and structural approaches has also revealed mechanisms for substrate recognition and at least five defined import pathways for precursor proteins. In this review, we discuss the discovery, recently solved structures, molecular function, and regulation of the TOM complex and its constituents, along with the implications these advances have for alleviating human diseases.

Indexed as

Mitochondrial ProteinsSaccharomyces cerevisiae ProteinsHumansMembrane ProteinsMitochondriaMitochondrial MembranesMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsProtein TransportSaccharomyces cerevisiaeMembrane ProteinsMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsMitochondrial ProteinsSaccharomyces cerevisiae ProteinsTom40 protein, S cerevisiaemitochondrial outer membraneneurodegenerationprotein import pathwaysTom40TOM complextransmembrane β-barrels

Identifiers

PMID35346689
PMCPMC9052162
OpenAlexW4221097514

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.