Evidence map›Paper›PMID 15546976›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2004

Unraveling the interface of signal recognition particle and its receptor by using chemical cross-linking and tandem mass spectrometry.

Feixia Chu, Shu-ou Shan, Demetri T Moustakas, Frank Alber, Pascal F Egea, Robert M Stroud, Peter Walter, Alma L Burlingame

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
–field-weighted citation impact
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

40 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Subunit order of eukaryotic TRiC/CCT chaperonin by cross-linking, mass spectrometry, and combinatorial homology modeling.Proceedings of the National Academy of Sciences of the United States of America · 2012
    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

8 authors.

Feixia ChuMass Spectrometry Facility, University of California, San Francisco 94143-0046, USA.
Shu-ou Shan
Demetri T Moustakas
Frank Alber
Pascal F Egea
Robert M Stroud
Peter Walter
Alma L Burlingame

Funding

YEAST THREONINE &SERINE KINASESP41RR001614 · NCRR · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI ORTIZ DE MONTELLANO, PAUL R · 1985 to 2011
$24.1M
MECHANISM OF PROTEIN TRANSLOCATION ACROSS MEMBRANESR01GM032384 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI STROUD, ROBERT M · 1985 to 2023
$7.6M
SIGNAL SEQUENCE RECOGNITION AND PROTEIN TARGETINGR01GM060641 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI STROUD, ROBERT M · 2000 to 2007
$2.4M
MECHANISM OF PROTEIN TRANSLOCATION ACROSS MEMBRANESR37GM032384 · NIGMS · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI WALTER, PETER · 1993 to 2002
$907k
PURCHASE OF MICRO LC/NANO ESIQQTOF MASS SPECTROMETERS10RR015804 · NCRR · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI BURLINGAME, ALMA L · 2001 to 2001
$500k
PURCHASE OF Q TOF MASS SPECTROMETERS10RR012961 · NCRR · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI JAMES, THOMAS L · 1998 to 1998
–
NCRR NIH HHS P41 RR001614NCRR NIH HHS RR 01614NCRR NIH HHS RR 12961NCRR NIH HHS RR 15804NCRR NIH HHS S10 RR015804NIGMS NIH HHS GM 32384NIGMS NIH HHS GM 60641NIGMS NIH HHS R01 GM032384NIGMS NIH HHS R01 GM060641NIGMS NIH HHS R37 GM032384
6 · The paper itself

Abstract

Among the methods used to unravel protein interaction surfaces, chemical cross-linking followed by identification of the cross-linked peptides by mass spectrometry has proven especially useful in dynamic and complex systems. During the signal recognition particle (SRP)-dependent targeting of proteins to the bacterial plasma membrane, the specific interaction between Ffh (the protein component of SRP) and FtsY (the SRP receptor) is known to be essential for the efficiency and fidelity of this process. In this work, we studied the Escherichia coli and Thermus aquaticus Ffh.FtsY complexes by using chemical cross-linking and tandem mass spectrometry to identify nine intermolecular cross-linked peptides. This information was used in conjunction with a previously undescribed model-building approach that combines geometric restraint optimization with macromolecular docking. The resulting model of the Ffh.FtsY complex is in good agreement with the crystal structure solved shortly thereafter. Intriguingly, four of the cross-linked pairs involve the M domain of Ffh, which is absent from the crystal structure, providing previously undocumented experimental evidence that the M domain is positioned in close proximity to the Ffh.FtsY interface in the complex.

Indexed as

Bacterial ProteinsCross-Linking ReagentsEscherichia coliEscherichia coli ProteinsMass SpectrometryModels, MolecularMultiprotein ComplexesProtein Structure, TertiaryReceptors, Cytoplasmic and NuclearReceptors, PeptideRecombinant ProteinsSignal Recognition ParticleThermusBacterial ProteinsCross-Linking ReagentsEscherichia coli ProteinsFfh protein, E coliFtsY protein, BacteriaMultiprotein ComplexesReceptors, Cytoplasmic and NuclearReceptors, PeptideRecombinant Proteinssignal peptide receptorSignal Recognition Particle

Identifiers

PMID15546976
PMCPMC528904

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.