Evidence map›Paper›PMID 22080505›Full record

ArticleNucleic acids research2012

PSCDB: a database for protein structural change upon ligand binding.

Takayuki Amemiya, Ryotaro Koike, Akinori Kidera, Motonori Ota

Abstract read
In one paragraph

Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. "Protein" no longer means what it used to.Current research in structural biology · 2021
    Review
  8. An intrinsic FRET sensor of protein-ligand interactions.Organic & biomolecular chemistry · 2020
    Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. CCProf: exploring conformational change profile of proteins.Database : the journal of biological databases and curation · 2016
    Article
  15. Article
  16. Article
  17. ChSeq: A database of chameleon sequences.Protein science : a publication of the Protein Society · 2015
    Review
  18. Article
  19. Principles of allosteric interactions in cell signaling.Journal of the American Chemical Society · 2014
    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

4 authors.

Takayuki AmemiyaGraduate School of Information Science, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8601, Japan.
Ryotaro Koike
Akinori Kidera
Motonori Ota

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteins are flexible molecules that undergo structural changes to function. The Protein Data Bank contains multiple entries for identical proteins determined under different conditions, e.g. with and without a ligand molecule, which provides important information for understanding the structural changes related to protein functions. We gathered 839 protein structural pairs of ligand-free and ligand-bound states from monomeric or homo-dimeric proteins, and constructed the Protein Structural Change DataBase (PSCDB). In the database, we focused on whether the motions were coupled with ligand binding. As a result, the protein structural changes were classified into seven classes, i.e. coupled domain motion (59 structural changes), independent domain motion (70), coupled local motion (125), independent local motion (135), burying ligand motion (104), no significant motion (311) and other type motion (35). PSCDB provides lists of each class. On each entry page, users can view detailed information about the motion, accompanied by a morphing animation of the structural changes. PSCDB is available at http://idp1.force.cs.is.nagoya-u.ac.jp/pscdb/.

Indexed as

Databases, ProteinLigandsProtein ConformationMotionUser-Computer InterfaceLigands

Identifiers

PMID22080505
PMCPMC3245091

What OpenQuestion holds

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LicenceCC BY-NC
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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.