Home| About us| My LA: login/register| For authors| For reviewers| Submit a paper
(close)

(Ctrl-click to select multiple journals)


How should we address you?

Your email address


 Yes, sign up now
 Sign up for general news too

Privacy Statement
 
 
 

Biochemistry Insights

Synopsis: An open access, peer reviewed electronic journal that covers biochemistry.


Indexing: Two major databases. Pubmed indexing for NIH-funded research.

Processing time: Decision in 2 weeks for 90% of papers.

Visibility: Most popular article read 800+ times.

View factor
for journal
26333


About this journal

ISSN: 1178-6264


Aims and scope:

Biochemistry Insights is a peer-reviewed, open-access online journal encompassing all topics within the field of biochemistry. This includes the chemistry, structure and functionality of proteins, carbohydrates, lipids, nucleic acids and smaller molecular components of cells and tissues. Cell metabolism, genomes, protein synthesis, cell signalling, transportation, and signal transduction are included but are not exclusive subjects. The journal also accepts articles on related topics applicable to this area, such as technology, outcomes, techniques and applications.

Editorial standards and procedures:

Submissions, excluding editorials, letters to the editor and dedications, will be peer reviewed by two reviewers.  Reviewers are required to provide fair, balanced and constructive reports.  

Under our Fairness in Peer Review Policy authors may appeal against reviewers' recommendations which are ill-founded, unobjective or unfair.  Appeals are considered by the Editor in Chief or Associate Editor.

Papers are not sent to peer reviewers following submission of a revised manuscript. Editorial decisions on re-submitted papers are based on the author's response to the initial peer review report.

Indexing:

This journal is indexed by:

  • CAS 
  • DOAJ
National Institutes of Health Public Access Policy compliant:

As of April 7 2008, the US NIH Public Access Policy requires that all peer reviewed articles resulting from research carried out with NIH funding be deposited in the Pubmed Central archive.

If you are an NIH employee or grantee Libertas Academica will ensure that you comply with the policy by depositing your paper at Pubmed Central on your behalf. 



Editor in Chief's call for papers
 
 
 


A 20 Residues Motif Delineates the Furin Cleavage Site and its Physical Properties May Influence Viral Fusion

Authors: Sun Tian
Publication Date: 08 Apr 2009
Biochemistry Insights 2009:2 9-20

Sun Tian

Institute of Biomechanics, South China University of Technology, Guangzhou, Guangdong, 510640, China.

Abstract

Furin is a proprotein convertase that proteolytically cleaves protein precursors to yield functional proteins. Efficient cleavage depends on the presence of a specific sequence motif on the substrate. Currently, the cleavage site motif is described as a four amino acid pattern: R-X-[K/R]-R↓. However, not all furin cleavage recognition sites can be described by this pattern and not all R-X-[K/R]-R↓ sites are cleaved by furin. Since many furin substrates are involved in the pathogenesis of viral infection and human diseases, it is important to accurately characterize the furin cleavage site motif. In this study, the furin cleavage site motif was characterized using statistical analysis. The data were interpreted within the 3D crystal structure of the furin catalytic domain. The results indicate that the furin cleavage site motif is comprised of about 20 residues, P14–P6´. Specific physical properties such as volume, charge, and hydrophilicity are required at specific positions. The furin cleavage site motif is divided into two parts: 1) one core region (8 amino acids, positions P6–P2´) packed inside the furin binding pocket; 2) two polar regions (8 amino acids, positions P7–P14; and 4 amino acids, positions P3´–P6´) located outside the furin binding pocket. The physical properties of the core region contribute to the binding strength of the furin substrate, while the polar regions provide a solvent accessible environment and facilitate the accessibility of the core region to the furin binding pocket. This furin cleavage site motif also revealed a dynamic relationship linking the evolution of physical properties in region P1´–P6´ of viral fusion peptides, furin cleavage efficacy, and viral infectivity.

Categories: Biochemistry


Post comment




No comments yet...Be the first to comment.

Bookmark this article

LINKEDIN FACEBOOK

Add to Mixx! MIXX YAHOO! BUZZ

PERMALINK DIGG


Sign up for free journal updates

How should we address you?
Your email address
 Yes, sign up now


Recently published in this journal

Renal Toxicity of Mercuric Chloride at Different Time Intervals in Rats
- 23/Jun/2009

Prolonged Treatment with Free Fatty Acids has Post Receptor Effect in Hepatic Insulin Resistance: Evidence that Fatty Acids, Oleate and Palmitate have Insignificant Effect on the Insulin Receptor Beta In Vivo and Ex Vivo Primary Hepatocytes
- 12/Jun/2009

A Novel Mechanism in Regulating the Alpha-Subunit of the Epithelial Sodium Channel (α ENaC) by the Alternatively Spliced Form α ENaC-b
- 15/Apr/2009

A 20 Residues Motif Delineates the Furin Cleavage Site and its Physical Properties May Influence Viral Fusion
- 08/Apr/2009

Fast and Simple micro-RNA Northern Blots
- 04/Mar/2009

Production of (2R,3S)-2-Benzamidomethyl-3-Hydroxybutanoates by Immobilized Plant Cells of Parthenocissus Tricuspidata
- 06/Jan/2009

Use of a Combined Duplex PCR/Dot Blot Assay for more sensitive genetic characterization
- 06/Nov/2008

The Dual Nature of Metallothioneins in the Metabolism of Heavy Metals and Reactive Oxygen Species in Aquatic Organisms: Implications of Use as a Biomarker of Heavy-Metal Effects in Field Investigations
- 01/Sep/2008

Targeted Cancer Therapy with Tumor Necrosis Factor-Alpha
- 22/Jul/2008

A Changing Research and Publication Landscape for Biochemistry
- 25/Mar/2008



Related journals...