Evidence map›Paper›PMID 18842639›Full record

ArticleNucleic acids research2009

TMFunction: database for functional residues in membrane proteins.

M Michael Gromiha, Yukimitsu Yabuki, M Xavier Suresh, A Mary Thangakani, Makiko Suwa, Kazuhiko Fukui

Abstract read
In one paragraph

Article in Nucleic acids research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Real value prediction of protein folding rate change upon point mutation.Journal of computer-aided molecular design · 2012
    Article
  7. Article
  8. 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

6 authors.

M Michael GromihaComputational Biology Research Center, National Institute of Advanced Industrial Science and Technology, AIST Tokyo Waterfront Bio-IT Research Building, 2-42 Aomi, Koto-ku, Tokyo 135-0064, Japan. michael-gromiha@aist.go.jp
Yukimitsu Yabuki
M Xavier Suresh
A Mary Thangakani
Makiko Suwa
Kazuhiko Fukui

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have developed the database TMFunction, which is a collection of more than 2900 experimentally observed functional residues in membrane proteins. Each entry includes the numerical values for the parameters IC50 (measure of the effectiveness of a compound in inhibiting biological function), V(max) (maximal velocity of transport), relative activity of mutants with respect to wild-type protein, binding affinity, dissociation constant, etc., which are important for understanding the sequence-structure-function relationship of membrane proteins. In addition, we have provided information about name and source of the protein, Uniprot and Protein Data Bank codes, mutational and literature information. Furthermore, TMFunction is linked to related databases and other resources. We have set up a web interface with different search and display options so that users have the ability to get the data in several ways. TMFunction is freely available at http://tmbeta-genome.cbrc.jp/TMFunction/.

Indexed as

Databases, ProteinAmino AcidsInternetMembrane ProteinsMutationAmino AcidsMembrane Proteins

Identifiers

PMID18842639
PMCPMC2686444

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.