Evidence map›Paper›PMID 25459764›Full record

ArticleJournal of molecular graphics & modelling2014

Homology modeling, molecular dynamics, and site-directed mutagenesis study of AlkB human homolog 1 (ALKBH1).

Pavel Silvestrov, Tina A Müller, Kristen N Clark, Robert P Hausinger, G Andrés Cisneros

Abstract read
In one paragraph

Article in Journal of molecular graphics & modelling, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.7field-weighted citation impact, top 31% 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

10 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Exploring links between 2-oxoglutarate-dependent oxygenases and Alzheimer's disease.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2022
    Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
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

5 authors at 2 institutions in 1 country.

Pavel SilvestrovDepartment of Chemistry, Wayne State University, Detroit, MI 48202, United States.
Tina A MüllerDepartment of Microbiology and Molecular Genetics, Michigan State University, East Lansing, MI 48824, United States.
Kristen N ClarkDepartment of Microbiology and Molecular Genetics, Michigan State University, East Lansing, MI 48824, United States.
Robert P HausingerDepartment of Microbiology and Molecular Genetics, Michigan State University, East Lansing, MI 48824, United States.
G Andrés CisnerosDepartment of Chemistry, Wayne State University, Detroit, MI 48202, United States. Electronic address: andres@chem.wayne.edu.
Michigan State University · USWayne State University · US

Funding

Study of alpha-ketoglutarate-dependent dioxygenasesR01GM063584 · NIGMS · MICHIGAN STATE UNIVERSITY · PI HAUSINGER, ROBERT P · 2002 to 2014
$3.8M
Theory and Simulation of DNA Repair Enzymes; Mechanism, Structure and FunctionR01GM108583 · NIGMS · WAYNE STATE UNIVERSITY · PI CISNEROS, GERARDO ANDRES · 2014 to 2022
$2.9M
NIGMS NIH HHS GM063584NIGMS NIH HHS GM108583-A1NIGMS NIH HHS R01 GM063584NIGMS NIH HHS R01 GM108583
6 · The paper itself

Abstract

The ability to repair DNA is important for the conservation of genetic information of living organisms. Cells have a number of ways to restore damaged DNA, such as direct DNA repair, base excision repair, and nucleotide excision repair. One of the proteins that can perform direct repair of DNA bases is Escherichia coli AlkB. In humans, there are 9 identified AlkB homologs, including AlkB homolog 1 (ALKBH1). Many of these proteins catalyze the direct oxidative dealkylation of DNA and RNA bases and, as such, have an important role in repairing DNA from damage induced by alkylating agents. In addition to the dealkylase activity, ALKBH1 can also function as an apyrimidinic/apurinic lyase and was proposed to have a distinct lyase active site. To our knowledge, no crystal structure or complete homology model of ALKBH1 protein is available. In this study, we have used homology modeling to predict the structure of ALKBH1 based on AlkB and Duffy-binding-like domain crystal structures as templates. Molecular dynamics simulations were subsequently performed on the predicted structure of ALKBH1. The positions of two disulfide bonds or a zinc-finger motif and a disulfide bond were predicted and the importance of these features was tested by mutagenesis. Possible locations for the lyase active site are proposed based on the analysis of our predicted structures and previous experimental results.

Indexed as

Molecular Dynamics SimulationAlkB Homolog 1, Histone H2a DioxygenaseDNA Repair EnzymesHumansMutagenesis, Site-DirectedALKBH1 protein, humanAlkB Homolog 1, Histone H2a DioxygenaseDNA Repair Enzymes

Identifiers

PMID25459764
PMCPMC4268226
OpenAlexW1999157688

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.