BioMed Research International

Helicase and Its Interacting Factors: Regulation Mechanism, Characterization, Structure, and Application for drug design


Publishing date
07 Nov 2014
Status
Published
Submission deadline
20 Jun 2014

1School of Biomedical Sciences, Chung Shan Medical University, Taichung, Taiwan

2Department of Protein Structure, Function and Design, Kyushu University, Fukuoka, Japan

3Department of Biological Sciences, Louisiana State University, Baton Rouge, LA, USA

4Institute of Biomedical Informatics, National Yang-Ming University, Taipei, Taiwan


Helicase and Its Interacting Factors: Regulation Mechanism, Characterization, Structure, and Application for drug design

Description

Helicases are motor proteins that separate nucleic acid duplexes and/or displace protein in reactions fueled by the binding and hydrolysis of adenosine triphosphate (ATP). Because of their essential roles in all aspects of nucleic acid metabolism, helicases encoded by bacteria, viruses, and human cells are widely studied targets for new antiviral, antibiotic, and anticancer drugs. Recent evidence indicates that some accessory proteins can regulate their helicase and/or translocase activities. Knowledge of structure-activity relationships has led to the development of successful therapies, new DNA/protein interacting models, novel inhibitors, and bioinformatics characterization to deeply understand the acting mechanism of helicases and/or their interacting factor. We invite investigators to contribute original research articles as well as review articles that will stimulate the continuing efforts and provide strategies to the information and structure-based development of new antiviral, antibiotic, and anticancer drugs for helicase inhibitions. Drug design of targeting any ATPase and DNA binding protein is also welcome. Potential topics include, but are not limited to:

  • Recent developments and applications in antiviral, antibiotic, and anticancer drugs targeting helicases and the loading factors
  • Anticancer signaling pathway
  • Biochemistry of helicase and its accessory protein(s)
  • New bioinformatics tools in any aspects for DNA binding proteins and ATPases
  • Structure and information-based inhibitor design and screening to helicases and DNA binding proteins
  • Latest technologies to monitor action of helicases and DNA binding proteins
  • Signaling pathway to regulation of helicase expression and activity
  • Potent inhibitor to any ATPase and DNA binding protein

Before submission authors should carefully read over the journal’s Author Guidelines, which are located at http://www.hindawi.com/journals/bmri/guidelines/. Prospective authors should submit an electronic copy of their complete manuscript through the journal Manuscript Tracking System at http://mts.hindawi.com/submit/journals/bmri/bioinformatics/hif/ according to the following timetable:


Articles

  • Special Issue
  • - Volume 2015
  • - Article ID 909047
  • - Editorial

Helicase and Its Interacting Factors: Regulation Mechanism, Characterization, Structure, and Application for Drug Design

Cheng-Yang Huang | Yoshito Abe | ... | I-Fang Chung
  • Special Issue
  • - Volume 2015
  • - Article ID 931857
  • - Review Article

Regulation of DEAH/RHA Helicases by G-Patch Proteins

Julien Robert-Paganin | Stéphane Réty | Nicolas Leulliot
  • Special Issue
  • - Volume 2014
  • - Article ID 171263
  • - Research Article

Crystal Structure of a Conserved Hypothetical Protein MJ0927 from Methanocaldococcus jannaschii Reveals a Novel Quaternary Assembly in the Nif3 Family

Sheng-Chia Chen | Chi-Hung Huang | ... | Yeh Chen
  • Special Issue
  • - Volume 2014
  • - Article ID 549719
  • - Review Article

The Mcm2-7 Replicative Helicase: A Promising Chemotherapeutic Target

Nicholas E. Simon | Anthony Schwacha
  • Special Issue
  • - Volume 2014
  • - Article ID 342725
  • - Research Article

Crystal Structure of Deinococcus radiodurans RecQ Helicase Catalytic Core Domain: The Interdomain Flexibility

Sheng-Chia Chen | Chi-Hung Huang | ... | Yeh Chen
  • Special Issue
  • - Volume 2014
  • - Article ID 573936
  • - Research Article

C-Terminal Domain Swapping of SSB Changes the Size of the ssDNA Binding Site

Yen-Hua Huang | Cheng-Yang Huang
  • Special Issue
  • - Volume 2014
  • - Article ID 285791
  • - Research Article

The N-Terminal Domain of Human DNA Helicase Rtel1 Contains a Redox Active Iron-Sulfur Cluster

Aaron P. Landry | Huangen Ding
  • Special Issue
  • - Volume 2014
  • - Article ID 195162
  • - Review Article

Structural Insight into the DNA-Binding Mode of the Primosomal Proteins PriA, PriB, and DnaT

Yen-Hua Huang | Cheng-Yang Huang
BioMed Research International
 Journal metrics
Acceptance rate31%
Submission to final decision67 days
Acceptance to publication30 days
CiteScore3.600
Impact Factor2.276
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