Linked Life Data

18603124

Source:http://linkedlifedata.com/resource/pubmed/id/18603124

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2008-7-8
pubmed:abstractText
Ubiquitin-mediated proteolysis plays a major role in a variety of cellular functions, including cell metabolism, cell cycle progression, cellular response to DNA damage, and programmed cell death. In most cases, the crucial regulators involved in the control of these diverse cellular functions are modified by specific E3 ubiquitin ligases through the attachment of multiple ubiquitin molecules, a signal that triggers the subsequent destruction by the 26S proteasome complex. Recent studies revealed that the proteasomal degradation pathway regulates the cellular apoptosis process on multiple levels. Thus, a better understanding of the molecular mechanisms that underlie the ubiquitination and destruction of these specific regulators of apoptosis will provide us with insight on how apoptosis is properly controlled in normal cells and how tumor cells evade the apoptosis pathways. This chapter provides an overview of the common methods used to examine whether a target protein is ubiquitinated, as well as the protocols to examine how a putative E3 ligase controls the destruction of the target protein.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0076-6879
pubmed:author
pubmed:issnType
Print
pubmed:volume
446
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
205-23
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Experimental approaches to investigate the proteasomal degradation pathways involved in regulation of apoptosis.
pubmed:affiliation
Department of Pathology, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, Massachusetts, USA.
pubmed:publicationType
Journal Article