Linked Life Data

15582399

Source:http://linkedlifedata.com/resource/pubmed/id/15582399

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2004-12-7
pubmed:abstractText
Small peptides have powerful biological activities ranging from antibiotic to immune suppression. These peptides are synthesized by non-ribosomal peptide synthetases (NRPS). Structural understanding of NRPS took a huge leap forward in 2002; this information has led to several detailed biochemical studies and further structural studies. NRPS are complex molecular machines composed of multiple modules and each module contains several autonomously folded catalytic domains. Structural studies have largely focused on individual domains, isolated from the context of the multienzyme. Biochemical studies have looked at individual domains, isolated whole modules and intact NRPS, and the combined data begin to allow us to visualize the process of peptide assembly by NRPS.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0959-440X
pubmed:author
pubmed:issnType
Print
pubmed:volume
14
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
748-56
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Structural aspects of non-ribosomal peptide biosynthesis.
pubmed:affiliation
Department of Chemistry, University of Warwick, Coventry CV4 7AL, UK.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't