Evidence map›Paper›PMID 9012810›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1997

Probing the environment along the protein import pathways in yeast mitochondria by site-specific photocrosslinking.

T Kanamori, S Nishikawa, I Shin, P G Schultz, T Endo

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

28 citing papers in PubMed, 77 citations in OpenAlex.

  1. Article
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  9. Review
  10. Therapeutic applications of an expanded genetic code.Chembiochem : a European journal of chemical biology · 2014
    Review
  11. Article
  12. Article
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  18. Article
  19. Addition of a photocrosslinking amino acid to the genetic code of Escherichiacoli.Proceedings of the National Academy of Sciences of the United States of America · 2002
    Article
  20. Article
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

5 authors at 3 institutions in 2 countries.

T KanamoriDepartment of Chemistry, Faculty of Science, Nagoya University, Japan.
S Nishikawa
I Shin
P G Schultz
T Endo
University of California, Berkeley · USHoward Hughes Medical Institute · USNagoya University · JP

Funding

PROTEIN STUDIES WITH UNNATURAL AMINO ACIDSR01GM049220 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI SCHULTZ, PETER G · 1993 to 2000
$230k
NIGMS NIH HHS GM49220
6 · The paper itself

Abstract

Artificially aminoacylated suppressor tRNAs were used to introduce photoreactive amino acids into model mitochondrial precursor proteins to probe the environment along the protein import pathway. Amino acids with benzophenone side chains of various lengths [DL-2-amino-3-(p-benzoylphenyl)propanoic acid (1) and DL-2-amino-5-(p-benzoylphenyl)pentanoic acid (2)] were incorporated at specific sites throughout the cytochrome b2-dihydrofolate reductase fusion proteins, pb2(220)-DHFR and pb2 delta 19(220)-DHFR, which were destined for the intermembrane space and the matrix in mitochondria, respectively. In vitro import of pb2(220)-DHFR and pb2 delta 19(220)-DHFR bearing 1 or 2 into isolated yeast mitochondria was arrested so that the N terminus reached the intermembrane space or the matrix, respectively, while the DHFR domain remained at the mitochondrial surface. The matrix-targeted pb2 delta 19(220)-DHFR was photocrosslinked to Tom40 in the outer membrane, Tim44 in the inner membrane, and Ssc1p in the matrix, suggesting that the protein has an extended conformation in the import channels. On the other hand, incorporation of 2 at various positions in the 50-residue segment of intermembrane-space-targeted pb2(220)-DHFR gave photocrosslinks only to Tom40, suggesting that the segment is not in an extended conformation, but localized near Tom40. The N-terminal portion of pb2(220)-DHFR, but not pb2 delta 19(220)-DHFR, was photocrosslinked to an as-yet-unidentified mitochondrial component to generate a 95-kDa crosslinked product.

Indexed as

Biological TransportCell CompartmentationCross-Linking ReagentsFungal ProteinsIntracellular MembranesMacromolecular SubstancesMitochondriaPhotochemistrySaccharomyces cerevisiaeStructure-Activity RelationshipTetrahydrofolate DehydrogenaseCross-Linking ReagentsFungal ProteinsMacromolecular SubstancesTetrahydrofolate Dehydrogenase

Identifiers

PMID9012810
PMCPMC19539
OpenAlexW1970338434

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.