Evidence map›Paper›PMID 20601428›Full record

ArticleThe Journal of biological chemistry2010

Properties of the C-terminal tail of human mitochondrial inner membrane protein Oxa1L and its interactions with mammalian mitochondrial ribosomes.

Md Emdadul Haque, Kevin B Elmore, Ashutosh Tripathy, Hasan Koc, Emine C Koc, Linda L Spremulli

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.0field-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

26 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
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  3. Article
  4. Review
  5. Review
  6. Article
  7. Review
  8. Mechanisms and regulation of protein synthesis in mitochondria.Nature reviews. Molecular cell biology · 2021
    Review
  9. Article
  10. Article
  11. Article
  12. Building the CuThe Journal of biological chemistry · 2018
    Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Structural aspects of mitochondrial translational apparatus.Current opinion in structural biology · 2012
    Review
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

6 authors at 2 institutions in 1 country.

Md Emdadul HaqueDepartment of Chemistry, University of North Carolina, Chapel Hill, North Carolina 27599-3290, USA.
Kevin B Elmore
Ashutosh Tripathy
Hasan Koc
Emine C Koc
Linda L Spremulli
University of North Carolina at Chapel Hill · USPennsylvania State University · US

Funding

MECHANISM OF PROTEIN SYNTHESIS IN MAMMALIAN MITOCHONDRIAR01GM032734 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI SPREMULLI, LINDA L · 1985 to 2009
$2.8M
Structural Studies of Mammalian Mitochondrial RibosomesR01GM071034 · NIGMS · PENNSYLVANIA STATE UNIVERSITY-UNIV PARK · PI KOC, EMINE C · 2005 to 2009
$1.3M
NIGMS NIH HHS GM071034NIGMS NIH HHS GM 32734NIGMS NIH HHS R01 GM032734NIGMS NIH HHS R01 GM071034
6 · The paper itself

Abstract

In humans the mitochondrial inner membrane protein Oxa1L is involved in the biogenesis of membrane proteins and facilitates the insertion of both mitochondrial- and nuclear-encoded proteins from the mitochondrial matrix into the inner membrane. The C-terminal approximately 100-amino acid tail of Oxa1L (Oxa1L-CTT) binds to mitochondrial ribosomes and plays a role in the co-translational insertion of mitochondria-synthesized proteins into the inner membrane. Contrary to suggestions made for yeast Oxa1p, our results indicate that the C-terminal tail of human Oxa1L does not form a coiled-coil helical structure in solution. The Oxa1L-CTT exists primarily as a monomer in solution but forms dimers and tetramers at high salt concentrations. The binding of Oxa1L-CTT to mitochondrial ribosomes is an enthalpy-driven process with a K(d) of 0.3-0.8 microM and a stoichiometry of 2. Oxa1L-CTT cross-links to mammalian mitochondrial homologs of the bacterial ribosomal proteins L13, L20, and L28 and to mammalian mitochondrial specific ribosomal proteins MRPL48, MRPL49, and MRPL51. Oxa1L-CTT does not cross-link to proteins decorating the conventional exit tunnel of the bacterial large ribosomal subunit (L22, L23, L24, and L29).

Indexed as

Amino Acid SequenceAnimalsCattleElectron Transport Complex IVHumansMitochondriaMitochondrial ProteinsModels, MolecularMolecular Sequence DataNuclear ProteinsProtein BindingProtein MultimerizationProtein Structure, QuaternaryProtein Structure, SecondaryRibosomesRibosome Subunits, LargeElectron Transport Complex IVMitochondrial ProteinsNuclear ProteinsOXA1 protein

Identifiers

PMID20601428
PMCPMC2934699
OpenAlexW1992453819

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.