Evidence map›Paper›PMID 19256528›Full record

ArticleBiochemistry2009

Development and evaluation of a structural model for SF1B helicase Dda.

Lauren P Blair, Alan J Tackett, Kevin D Raney

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2009. 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
0.7field-weighted citation impact, top 30% 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, 8 citations in OpenAlex.

  1. Article
  2. A maternal high-fat diet modulates fetal SIRT1 histone and protein deacetylase activity in nonhuman primates.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2012
    Article
  3. Article
  4. Article
  5. 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

3 authors at 1 institution in 1 country.

Lauren P BlairDepartment of Biochemistry and Molecular Biology, University of Arkansas for Medical Sciences, Little Rock, Arkansas 72205, USA.
Alan J Tackett
Kevin D Raney
University of Arkansas for Medical Sciences · US

Funding

VIRULENCE MECHANISMS IN ESCHERICHIA COLIP20RR016460 · NCRR · UNIV OF ARKANSAS FOR MED SCIS · PI HENSLEY, LORI · 2001 to 2011
$33.1M
Structure based drug discoveryP20RR015569 · NCRR · UNIVERSITY OF ARKANSAS AT FAYETTEVILLE · PI MILLETT, FRANCIS S · 2000 to 2009
$21.4M
UNWINDING AND TRANSLOCATION OF DNA BY HELICASESR01GM059400 · NIGMS · UNIV OF ARKANSAS FOR MED SCIS · PI RANEY, KEVIN D · 1999 to 2007
$1.8M
REGULATION OF SALMONELLA VIRULENCE BY THE PHOP PROTEINR01GM054900 · NIGMS · WASHINGTON UNIVERSITY · PI GROISMAN, EDUARDO A. · 1996 to 1999
–
NCRR NIH HHS P20 RR015569NCRR NIH HHS P20 RR016460NCRR NIH HHS P20RR016460NCRR NIH HHS P20RR15569NIGMS NIH HHS R01GM054900NIGMS NIH HHS R01 GM059400
6 · The paper itself

Abstract

Helicases are proteins that unwind double-stranded nucleic acids. Dda helicase from bacteriophage T4 has served as an excellent model for understanding the molecular mechanism of this class of enzymes. Study of the structure of Dda may reveal why some helicases translocate in a 5' to 3' direction on DNA, while others translocate in a 3' to 5' direction. Attaining a structure of Dda has proven difficult because the protein fails to readily form crystals and is too large for current NMR technologies. We have developed a homology model of the enzyme which will serve to guide studies that examine the structural and functional significance of the interaction between Dda and DNA and how this interaction affects translocation and unwinding of DNA. We have tested the structural model by using methods for mapping protein domains and for examining protein surfaces that interact with DNA.

Indexed as

Amino Acid SequenceBacteriophage T4DNADNA HelicasesModels, MolecularMolecular ConformationMolecular Sequence DataProtein BindingSequence AlignmentViral ProteinsDNADNA HelicasesViral Proteins

Identifiers

PMID19256528
PMCPMC2664552
OpenAlexW2088659033

What OpenQuestion holds

Textmetadata
LicenceTDM
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.