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Global mitochondrial protein import proteomics reveal distinct regulation by translation and translocation machinery

Molecular Cell(2022)10.1016/j.molcel.2021.11.004Source: DataRank Database

Global mitochondrial protein import proteomics reveal distinct regulation by translation and translocation machinery is a research paper published in Molecular Cell (2022). On theSindex it has a DataRank of 0.668. It has been cited 85 times.

N/A

0.668DataRank · unranked

Scored on demand from live citation data

85 citations

Cite:

Linked data & code

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DataRank reads this dataset's downstream impact straight off the citation graph — no black box, no proprietary weighting. How is this computed?

›Methodology & internals

datarank_citation_only_1hop_v6· scope data_onlyMethodology

Pipeline:MetadataData-paper checkEnrichmentCitation networkScoring

Enrichment:Funding (10 grants)Impact (FWCI 4.07)OA: hybridTopics (71)IDs (PubMed, PMC, OpenAlex)Annotations (3)

FAIR Checklist

Context only (not used in score)

Findable (1/2)

Has DOI

Accessible (0/2)

Interoperable (0/2)

Reusable (0/3)

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DataRank Breakdown

Base Score 100%Citation Network 0%

Base Score Contribution

0.668

From this paper's citation signal

Citation Network Contribution

0

Citation network not refreshed for this result

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Authors (5)

Süleyman Bozkurt ORCID,Jonas B. Michaelis ORCID,Kevin Klann ORCID,Christian Münch ORCID,Jasmin Adriana Schäfer

Live enrichment

PubMed:34847359 PMC:PMC8791276 OpenAlex:https://openalex.org/W3215151924

Deutsche Forschungsgemeinschaft

Grant: 259130777

Deutsche Forschungsgemeinschaft

Grant: 403765277

Deutsche Forschungsgemeinschaft

Grant: 390339347

Elucidation of the mammalian mitochondrial unfolded protein response network

Deutsche Forschungsgemeinschaft

Grant: MU 4216/1-1

Deutsche Forschungsgemeinschaft

Grant: SFB 1177

European Research Council

Grant: 803565

Cellular modulation by the mitochondrial unfolded protein response

Deutsche Forschungsgemeinschaft

Grant: unidentified

unidentified

Deutsche Forschungsgemeinschaft

Grant: 259130777/SFB 1177

Molecular and Functional Characterization of Selective Autophagy

European Research Council

Seventh Framework Programme

FWCI

4.07

Citation Percentile

1.0%

Citation Trend

2021

2022

2023

2024

2025

2026

hybridLicense: cc-by

journalhttps://doi.org/10.1016/j.molcel.2021.11.004

publisherhttps://doi.org/10.1016/j.molcel.2021.11.004

publisherhttps://api.elsevier.com/content/article/PII:S1097276521009540?httpAccept=text/xml

publisherhttps://api.elsevier.com/content/article/PII:S1097276521009540?httpAccept=text/plain

repositoryhttps://pubmed.ncbi.nlm.nih.gov/34847359

Fields of Study

Mitochondrial Function and PathologyATP Synthase and ATPases ResearchRNA and protein synthesis mechanisms0301 basic medicine0303 health sciences03 medical and health sciencesCarbonyl Cyanide m-Chlorophenyl HydrazoneElectron Transport Complex IFemaleHeLa CellsHumansKineticsMitochondriaMitochondrial Membrane Transport ProteinsMitochondrial ProteinsProtein BiosynthesisProtein TransportProteomeProteomicsUncoupling Agents

MeSH Terms

Carbonyl Cyanide m-Chlorophenyl HydrazoneFemaleHeLa CellsHumansKineticsMitochondriaProtein BiosynthesisUncoupling AgentsProteomeProtein TransportMitochondrial ProteinsMitochondrial Membrane Transport ProteinsProteomicsElectron Transport Complex IHela Cells

Keywords

BiologyMitochondrionCell biologyProteomicsTransport proteinStable isotope labeling by amino acids in cell cultureTranslation (biology)ProteomeMitochondrial membrane transport proteinCytosolQuantitative proteomicsInner mitochondrial membraneBiochemistryMessenger RNAEnzymeMitochondriaTranslationProtein translocationDiseaseintegrated stress responseRespiratory Chain ComplexesProteostasisSILACTmtResourceCarbonyl Cyanide m-Chlorophenyl HydrazoneElectron Transport Complex IUncoupling AgentsMitochondrial Membrane Transport ProteinsMitochondrial ProteinsKineticsProtein TransportProtein BiosynthesisHumansFemaleHeLa Cells