20948667

Source:http://linkedlifedata.com/resource/pubmed/id/20948667

Download in:

Switch to

Custom View

Named Graph Language Inference

Statements in which the resource exists as a subject.
Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0033625, umls-concept:C0392747, umls-concept:C0443286, umls-concept:C1519751, umls-concept:C1707310
pubmed:dateCreated	2010-10-15
pubmed:abstractText	The structures of enzymes that collectively modify proteins by covalent addition of ubiquitin-like protein moieties have provided significant insights into the regulatory pathways they compose and have highlighted the importance of protein flexibility for the mechanism and regulation of the ubiquitination reaction.
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/101506835
pubmed:status	PubMed-not-MEDLINE
pubmed:issn	1757-594X
pubmed:author	pubmed-author:EndicottJane AJA, pubmed-author:RiedingerChristianeC
pubmed:issnType	Electronic
pubmed:volume	1
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	19
pubmed:year	2009
pubmed:articleTitle	All change: protein conformation and the ubiquitination reaction cascade.
pubmed:affiliation	Laboratory of Molecular Biophysics and Department of Biochemistry South Parks Road, Oxford OX1 3QU UK.
pubmed:publicationType	Journal Article