Evidence map›Paper›PMID 17277440›Full record

ArticleActa crystallographica. Section F, Structural biology and crystallization communications2007

Structure of cyclophilin from Leishmania donovani at 1.97 A resolution.

V Venugopal, Banibrata Sen, Alok K Datta, Rahul Banerjee

Open access · bronzeAbstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.1field-weighted citation impact, top 47% of its field
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

6 citing papers in PubMed, 13 citations in OpenAlex.

  1. Review
  2. Review
  3. Insights into Peptidyl-ProlylPathogens (Basel, Switzerland) · 2024
    Review
  4. Article
  5. Article
  6. Functional analysis of Leishmania major cyclophilin.International journal for parasitology · 2008
    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 at 2 institutions in 1 country.

V VenugopalCrystallography and Molecular Biology Division, Saha Institute of Nuclear Physics, Sector 1, Block AF, Bidhan Nagar, Kolkata 700 064, India.
Banibrata Sen
Alok K Datta
Rahul Banerjee
Indian Institute of Chemical Biology · INSaha Institute of Nuclear Physics · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The crystal structure of cyclophilin from Leishmania donovani (LdCyp) has been determined and refined at 1.97 A resolution to a crystallographic R factor of 0.178 (R(free) = 0.197). The structure was solved by molecular replacement using cyclophilin from Trypanosoma cruzi as the search model. LdCyp exhibits complete structural conservation of the cyclosporin-binding site with respect to the homologous human protein, as anticipated from LdCyp-cyclosporin binding studies. Comparisons with other cyclophilins show deviations primarily in the loop regions. The solvent structure encompassing the molecule has also been analyzed in some detail.

Indexed as

AnimalsBinding SitesCrystallography, X-RayCyclophilinsEscherichia coliLeishmania donovaniModels, MolecularProtein Structure, SecondaryRecombinant ProteinsWaterCyclophilinsRecombinant ProteinsWater

Identifiers

PMID17277440
PMCPMC2330116
OpenAlexW2046639604

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.