Evidence map›Paper›PMID 19587024›Full record

ArticleProtein engineering, design & selection : PEDS2009

Alignment of multiple protein structures based on sequence and structure features.

M S Madhusudhan, Benjamin M Webb, Marc A Marti-Renom, Narayanan Eswar, Andrej Sali

Abstract read
In one paragraph

Article in Protein engineering, design & selection : PEDS, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing 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

36 citing papers in PubMed.

  1. Article
  2. Review
  3. International journal of molecular sciences · 2022
    Article
  4. Article
  5. Article
  6. Benchmarking Methods of Protein Structure Alignment.Journal of molecular evolution · 2020
    Article
  7. Article
  8. Characterization of SPP inhibitors suppressing propagation of HCV and protozoa.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  9. Article
  10. Article
  11. Article
  12. Comparative Protein Structure Modeling Using MODELLER.Current protocols in bioinformatics · 2016
    Article
  13. Article
  14. Article
  15. Article
  16. Consequences of domain insertion on sequence-structure divergence in a superfold.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  17. SLC classification: an update.Clinical pharmacology and therapeutics · 2013
    Article
  18. Article
  19. 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

5 authors.

M S MadhusudhanDepartment of Bioengineering and Therapeutic Sciences, University of California at San Francisco, San Francisco, CA 94158, USA.
Benjamin M Webb
Marc A Marti-Renom
Narayanan Eswar
Andrej Sali

Funding

CENTER FOR STRUCTURAL GENOMICSP50GM062529 · NIGMS · SGX PHARMACEUTICALS, INC. · PI BURLEY, STEPHEN KEVIN · 2000 to 2004
$33.8M
Protein Modeling by Satisfaction of Spatial RestraintsR01GM054762 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI SALI, ANDREJ · 2001 to 2008
$2.1M
NIGMS NIH HHS R01 GM54762-11NIGMS NIH HHS U54 GM62529
6 · The paper itself

Abstract

Comparing the structures of proteins is crucial to gaining insight into protein evolution and function. Here, we align the sequences of multiple protein structures by a dynamic programming optimization of a scoring function that is a sum of an affine gap penalty and terms dependent on various sequence and structure features (SALIGN). The features include amino acid residue type, residue position, residue accessible surface area, residue secondary structure state and the conformation of a short segment centered on the residue. The multiple alignment is built by following the 'guide' tree constructed from the matrix of all pairwise protein alignment scores. Importantly, the method does not depend on the exact values of various parameters, such as feature weights and gap penalties, because the optimal alignment across a range of parameter values is found. Using multiple structure alignments in the HOMSTRAD database, SALIGN was benchmarked against MUSTANG for multiple alignments as well as against TM-align and CE for pairwise alignments. On the average, SALIGN produces a 15% improvement in structural overlap over HOMSTRAD and 14% over MUSTANG, and yields more equivalent structural positions than TM-align and CE in 90% and 95% of cases, respectively. The utility of accurate multiple structure alignment is illustrated by its application to comparative protein structure modeling.

Indexed as

AlgorithmsAmino Acid SequenceDatabases, ProteinProtein ConformationProteinsSequence AlignmentSequence Analysis, ProteinProteins

Identifiers

PMID19587024
PMCPMC2909824

What OpenQuestion holds

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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.