Evidence map›Paper›PMID 20944205›Full record

ArticleActa crystallographica. Section F, Structural biology and crystallization communications2010

Structure of the first representative of Pfam family PF09410 (DUF2006) reveals a structural signature of the calycin superfamily that suggests a role in lipid metabolism.

Hsiu Ju Chiu, Constantina Bakolitsa, Arne Skerra, Andrei Lomize, Dennis Carlton, Mitchell D Miller, S Sri Krishna, Polat Abdubek, Tamara Astakhova, Herbert L Axelrod and 31 more

Open access · hybridAbstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2010. 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
0.3field-weighted citation impact, top 40% 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, 20 citations in OpenAlex.

  1. Reverse vaccinology for development of vaccine against Aeromonas hydrophila infection in nile tilapia (Oreochromis niloticus).Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2026
    Article
  2. Review
  3. Article
  4. Article
  5. Catalytic mechanism andNature catalysis · 2021
    Article
  6. 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

41 authors at 9 institutions in 2 countries.

Hsiu Ju ChiuJoint Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, CA, USA.
Constantina Bakolitsa
Arne Skerra
Andrei Lomize
Dennis Carlton
Mitchell D Miller
S Sri Krishna
Polat Abdubek
Tamara Astakhova
Herbert L Axelrod
Thomas Clayton
Marc C Deller
Lian Duan
Julie Feuerhelm
Joanna C Grant
Slawomir K Grzechnik
Gye Won Han
Lukasz Jaroszewski
Kevin K Jin
Heath E Klock
Mark W Knuth
Piotr Kozbial
Abhinav Kumar
David Marciano
Daniel McMullan
Andrew T Morse
Edward Nigoghossian
Linda Okach
Jessica Paulsen
Ron Reyes
Christopher L Rife
Henry van den Bedem
Dana Weekes
Qingping Xu
Keith O Hodgson
John Wooley
Marc André Elsliger
Ashley M Deacon
Adam Godzik
Scott A Lesley
Ian A Wilson
Joint Center for Structural Genomics · USSanford Burnham Prebys Medical Discovery Institute · USGenomics Institute of the Novartis Research Foundation · USUniversity of California, San Diego · USScripps Research Institute · USSLAC National Accelerator Laboratory · USStanford Synchrotron Radiation Lightsource · USTechnical University of Munich · DEUniversity of Michigan–Ann Arbor · US

Funding

Technology Evaluation CoreU54GM074898 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI WILSON, IAN A · 2005 to 2009
$50.6M
NCI NIH HHS Y1-CO-1020NIGMS NIH HHS U54 GM074898NIGMS NIH HHS Y1-GM-1104
6 · The paper itself

Abstract

The first structural representative of the domain of unknown function DUF2006 family, also known as Pfam family PF09410, comprises a lipocalin-like fold with domain duplication. The finding of the calycin signature in the N-terminal domain, combined with remote sequence similarity to two other protein families (PF07143 and PF08622) implicated in isoprenoid metabolism and the oxidative stress response, support an involvement in lipid metabolism. Clusters of conserved residues that interact with ligand mimetics suggest that the binding and regulation sites map to the N-terminal domain and to the interdomain interface, respectively.

Indexed as

Databases, GeneticLipid MetabolismAmino Acid SequenceBacterial ProteinsCrystallography, X-RayModels, MolecularMolecular Sequence DataNitrosomonas europaeaOxidative StressProtein Structure, TertiarySequence AlignmentSequence Homology, Amino AcidBacterial Proteins

Identifiers

PMID20944205
PMCPMC2954199
OpenAlexW2150247260

What OpenQuestion holds

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LicenceCC BY
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.