Evidence map›Paper›PMID 19859826›Full record

ArticleJournal of structural and functional genomics2009

Structural genomics target selection for the New York consortium on membrane protein structure.

Marco Punta, James Love, Samuel Handelman, John F Hunt, Lawrence Shapiro, Wayne A Hendrickson, Burkhard Rost

Abstract read
In one paragraph

Article in Journal of structural and functional genomics, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing 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

30 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Current research in structural biology · 2021
    Article
  7. Review
  8. Article
  9. Article
  10. Prediction of protein disorder based on IUPred.Protein science : a publication of the Protein Society · 2018
    Article
  11. Article
  12. Article
  13. Article
  14. Unexpected features of the dark proteome.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  15. Article
  16. Trends in structural coverage of the protein universe and the impact of the Protein Structure Initiative.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  17. Article
  18. Article
  19. Structural genomics plucks high-hanging membrane proteins.Current opinion in structural biology · 2012
    Review
  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

7 authors.

Marco PuntaDepartment of Biochemistry and Molecular Biophysics, Columbia University, 630 West 168th Street, New York, NY, 10032, USA. punta@rostlab.org
James Love
Samuel Handelman
John F Hunt
Lawrence Shapiro
Wayne A Hendrickson
Burkhard Rost

Funding

Sub 9 at AECMU54GM075026 · NIGMS · NEW YORK STRUCTURAL BIOLOGY CENTER · PI GOUAUX, JAMES E · 2005 to 2009
$16.8M
MOLECULAR BASIS OF CADHERIN MEDIATED CELL ADHESIONR01GM062270 · NIGMS · MOUNT SINAI SCHOOL OF MEDICINE OF NYU · PI SHAPIRO, LAWRENCE S · 2001 to 2015
$3.4M
NIGMS NIH HHS R01 GM062270NIGMS NIH HHS U54 GM075026NIGMS NIH HHS U54-GM75026-01
6 · The paper itself

Abstract

The New York Consortium on Membrane Protein Structure (NYCOMPS), a part of the Protein Structure Initiative (PSI) in the USA, has as its mission to establish a high-throughput pipeline for determination of novel integral membrane protein structures. Here we describe our current target selection protocol, which applies structural genomics approaches informed by the collective experience of our team of investigators. We first extract all annotated proteins from our reagent genomes, i.e. the 96 fully sequenced prokaryotic genomes from which we clone DNA. We filter this initial pool of sequences and obtain a list of valid targets. NYCOMPS defines valid targets as those that, among other features, have at least two predicted transmembrane helices, no predicted long disordered regions and, except for community nominated targets, no significant sequence similarity in the predicted transmembrane region to any known protein structure. Proteins that feed our experimental pipeline are selected by defining a protein seed and searching the set of all valid targets for proteins that are likely to have a transmembrane region structurally similar to that of the seed. We require sequence similarity aligning at least half of the predicted transmembrane region of seed and target. Seeds are selected according to their feasibility and/or biological interest, and they include both centrally selected targets and community nominated targets. As of December 2008, over 6,000 targets have been selected and are currently being processed by the experimental pipeline. We discuss how our target list may impact structural coverage of the membrane protein space.

Indexed as

GenomeGenomicsProkaryotic CellsMembrane ProteinsProtein Structure, SecondarySequence Homology, Amino AcidMembrane Proteins

Identifiers

PMID19859826
PMCPMC2780672

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.