Literature DB >> 10461316

A tail of protein folding.

R J Villafañe1, K Baksi.   

Abstract

This review describes the use of a simple genetic system that has provided important insight into the process of folding and, of its flipside, that of protein aggregation. These studies make use of the tail protein of the bacterial virus P22 which infects Salmonella typhimurium. This folding system serves as a model for a number protein structural elements and may also provide important insights into disease-related protein folding defects at a time when an increasing number of diseases are being shown to be due to protein folding alterations.

Entities:  

Mesh:

Substances:

Year:  1999        PMID: 10461316

Source DB:  PubMed          Journal:  P R Health Sci J        ISSN: 0738-0658            Impact factor:   0.705


  2 in total

1.  Bacteriophage SP6 is closely related to phages K1-5, K5, and K1E but encodes a tail protein very similar to that of the distantly related P22.

Authors:  Dean Scholl; Sankar Adhya; Carl R Merril
Journal:  J Bacteriol       Date:  2002-05       Impact factor: 3.490

2.  Homology between two different Salmonella phages: Salmonella enterica serovar Typhimurium phage P22 and Salmonella enterica serovar Anatum var. 15 + phageepsilon34.

Authors:  Clari J Salgado; Milka Zayas; Robert Villafane
Journal:  Virus Genes       Date:  2004-08       Impact factor: 2.332

  2 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.