Evidence map›Paper›PMID 8130644›Full record

ArticleThe Plant cell1994

Envelope membrane proteins that interact with chloroplastic precursor proteins.

S E Perry, K Keegstra

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 93 papers.

0numbers the graph read from it
0cells of the map it votes in
93citing papers in PubMed
7.8field-weighted citation impact, top 2% 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

93 citing papers in PubMed, 263 citations in OpenAlex.

  1. Article
  2. Chloroplast import motor subunits FtsHi1 and FtsHi2 are located on opposite sides of the inner envelope membrane.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Coexpressed subunits of dual genetic origin define a conserved supercomplex mediating essential protein import into chloroplasts.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  8. Article
  9. Article
  10. A Protochlorophyllide (Pchlide)Frontiers in plant science · 2019
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. Article
  20. Review

33 more citing papers are in PubMed but not listed here.

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.

S E PerryDepartment of Botany, University of Wisconsin, Madison 53706-1381.
K Keegstra
University of Wisconsin System · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The post-translational transport of cytoplasmically synthesized precursor proteins into chloroplasts requires proteins in the envelope membranes. To identify some of these proteins, label transfer cross-linking was performed using precursor to the small subunit of ribulose-1,5-bisphosphate carboxylase (prSSU) that was blocked at an early stage of the transport process. Two envelope proteins were identified: an 86-kD protein and a 75-kD protein, both present in the outer membrane. Labeling of both proteins required prSSU and could not be accomplished with SSU lacking a transit peptide. Labeling of the 75-kD protein occurred only when low levels of ATP were present, whereas labeling of the 86-kD protein occurred in the absence of exogenous ATP. Although both labeled proteins were identified as proteins of the outer envelope membrane, the labeled form of the 75-kD protein could only be detected in fractions containing mixed envelope membranes. Based on these observations, we propose that prSSU first binds in an ATP-independent fashion to the 86-kD protein. The energy-requiring step is association with the 75-kD protein and assembly of a translocation contact site between the inner and outer membrane of the chloroplastic envelope.

Indexed as

Adenosine TriphosphateBiological TransportCells, CulturedChloroplastsCross-Linking ReagentsElectrophoresis, Gel, Two-DimensionalFabaceaeIntracellular MembranesMembrane ProteinsPlant ProteinsPlants, MedicinalProtein BindingProtein PrecursorsProtein Processing, Post-TranslationalRibulose-Bisphosphate CarboxylaseThermolysinAdenosine TriphosphateCross-Linking ReagentsMembrane ProteinsPlant ProteinsProtein PrecursorsRibulose-Bisphosphate CarboxylaseThermolysin

Identifiers

PMID8130644
PMCPMC160419
OpenAlexW1985296992

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.