Evidence map›Paper›PMID 20801163›Full record

ArticleMolecular and biochemical parasitology2010

Crystal structure of Leishmania major ADP-ribosylation factor-like 1 and a classification of related GTPase family members in this Kinetoplastid.

Jennifer R Fleming, Alice Dawson, William N Hunter

Abstract read
In one paragraph

Article in Molecular and biochemical parasitology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.2field-weighted citation impact, top 39% 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

5 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Structure of Plasmodium falciparum ADP-ribosylation factor 1.Acta crystallographica. Section F, Structural biology and crystallization communications · 2010
    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

3 authors at 1 institution in 1 country.

Jennifer R FlemingDivision of Biological Chemistry and Drug Discovery, College of Life Sciences, University of Dundee, Dundee, UK.
Alice Dawson
William N Hunter
University of Dundee · GB

Funding

Biotechnology and Biological Sciences Research Council BBS/B/14434Biotechnology and Biological Sciences Research Council WT082596Wellcome Trust 082596Wellcome Trust 083481
6 · The paper itself

Abstract

ADP-ribosylation factor-like (ARL) proteins are small GTPases that undergo conformational changes upon nucleotide binding, and which regulate the affinity of ARLs for binding other proteins, lipids or membranes. There is a paucity of structural data on this family of proteins in the Kinetoplastida, despite studies implicating them in key events related to vesicular transport and regulation of microtubule-dependent processes. The crystal structure of Leishmania major ARL1 in complex with GDP has been determined to 2.1 Å resolution and reveals a high degree of structural conservation with human ADP-ribosylation factor 1 (ARF1). Putative L. major and Trypanosoma brucei ARF/ARL family members have been classified based on structural considerations, amino acid sequence conservation combined with functional data on Kinetoplastid and human orthologues. This classification may guide future studies designed to elucidate the function of specific family members.

Indexed as

ADP-Ribosylation Factor 1AnimalsCrystallizationCrystallographyGTP PhosphohydrolasesHumansKinetoplastidaLeishmania majorModels, MolecularProtozoan ProteinsADP-Ribosylation Factor 1GTP PhosphohydrolasesProtozoan Proteins

Identifiers

PMID20801163
PMCPMC3065712
OpenAlexW2014126652

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.