Evidence map›Paper›PMID 31053642›Full record

ArticleThe Journal of biological chemistry2019

The yeast protein Mam33 functions in the assembly of the mitochondrial ribosome.

Gabrielle A Hillman, Michael F Henry

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

17 citing papers in PubMed, 36 citations in OpenAlex.

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  17. HeterozygousFrontiers in oncology · 2020
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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.

Gabrielle A HillmanFrom the Department of Molecular Biology, Rowan University School of Osteopathic Medicine, Stratford, New Jersey 08084 and.ORCID 0000-0003-1354-9994
Michael F HenryFrom the Department of Molecular Biology, Rowan University School of Osteopathic Medicine, Stratford, New Jersey 08084 and henrymf@rowan.edu.ORCID 0000-0002-8754-9463
Stratford University · US

Funding

Translational control of mitochondrial gene expressionR15GM117483 · NIGMS · ROWAN UNIVERSITY SCHOOL/OSTEOPATHIC MED · PI HENRY, MICHAEL F · 2016 to 2016
$483k
NIGMS NIH HHS R15 GM117483
6 · The paper itself

Abstract

Mitochondrial ribosomes are functionally specialized for the synthesis of several essential inner membrane proteins of the respiratory chain. Although remarkable progress has been made toward understanding the structure of mitoribosomes, the pathways and factors that facilitate their biogenesis remain largely unknown. The long unstructured domains of unassembled ribosomal proteins are highly prone to misfolding and often require dedicated chaperones to prevent aggregation. To date, chaperones that ensure safe delivery to the assembling ribosome have not been identified in the mitochondrion. In this study, a respiratory synthetic lethality screen revealed a role for an evolutionarily conserved mitochondrial matrix protein called Mam33 in

Indexed as

Amino Acid SequenceMitochondrial ProteinsMitochondrial RibosomesProtein BiosynthesisProtein ConformationRibosomal ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence HomologyMAM33 protein, S cerevisiaeMitochondrial ProteinsRibosomal ProteinsSaccharomyces cerevisiae Proteinschaperonecomplement C1q-binding protein (C1QBP)COX1mitochondriamitochondrial respiratory chain complexprotein misfoldingribosome assemblyRNA helicasesynthetic lethality

Identifiers

PMID31053642
PMCPMC6597815
OpenAlexW2943560757

What OpenQuestion holds

Textmetadata
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.