Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1989-3-16
pubmed:abstractText
Tryptic digestion has been used to investigate the conformational changes associated with substrate translocation by the human erythrocyte glucose transporter. The effects of substrates and inhibitors of transport on the rates of tryptic cleavage at the cytoplasmic surface of the membrane have confirmed previous observations that this protein can adopt at least two conformations. In the presence of phloretin or 4,6-O-ethylidene-D-glucose, the rate of cleavage is slowed. Because these inhibitors bind preferentially at the extracellular surface of the transporter, their effects must result from a conformational change rather than from steric hindrance. A conformational change must also be responsible for the effect of the physiological substrate D-glucose, which is to increase the rate of cleavage. The regions of the protein involved in the conformational changes include both of the large cytoplasmic regions that are cleaved by trypsin: these are the central hydrophilic region of the sequence (residues 213-269) and the hydrophilic C-terminal region (residues 457-492).
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/3223921-1156368, http://linkedlifedata.com/resource/pubmed/commentcorrection/3223921-13539834, http://linkedlifedata.com/resource/pubmed/commentcorrection/3223921-14067949, http://linkedlifedata.com/resource/pubmed/commentcorrection/3223921-3365399, http://linkedlifedata.com/resource/pubmed/commentcorrection/3223921-3455783, http://linkedlifedata.com/resource/pubmed/commentcorrection/3223921-3473495, http://linkedlifedata.com/resource/pubmed/commentcorrection/3223921-3545294, http://linkedlifedata.com/resource/pubmed/commentcorrection/3223921-3571218, http://linkedlifedata.com/resource/pubmed/commentcorrection/3223921-3597413, http://linkedlifedata.com/resource/pubmed/commentcorrection/3223921-3606595, http://linkedlifedata.com/resource/pubmed/commentcorrection/3223921-3620469, http://linkedlifedata.com/resource/pubmed/commentcorrection/3223921-3689782, http://linkedlifedata.com/resource/pubmed/commentcorrection/3223921-3707948, http://linkedlifedata.com/resource/pubmed/commentcorrection/3223921-3711076, http://linkedlifedata.com/resource/pubmed/commentcorrection/3223921-3718945, http://linkedlifedata.com/resource/pubmed/commentcorrection/3223921-3722192, http://linkedlifedata.com/resource/pubmed/commentcorrection/3223921-3733746, http://linkedlifedata.com/resource/pubmed/commentcorrection/3223921-3778899, http://linkedlifedata.com/resource/pubmed/commentcorrection/3223921-3801473, http://linkedlifedata.com/resource/pubmed/commentcorrection/3223921-3818652, http://linkedlifedata.com/resource/pubmed/commentcorrection/3223921-3839598, http://linkedlifedata.com/resource/pubmed/commentcorrection/3223921-4039316, http://linkedlifedata.com/resource/pubmed/commentcorrection/3223921-4039758, http://linkedlifedata.com/resource/pubmed/commentcorrection/3223921-4041454, http://linkedlifedata.com/resource/pubmed/commentcorrection/3223921-4715343, http://linkedlifedata.com/resource/pubmed/commentcorrection/3223921-4817966, http://linkedlifedata.com/resource/pubmed/commentcorrection/3223921-5432063, http://linkedlifedata.com/resource/pubmed/commentcorrection/3223921-5553320, http://linkedlifedata.com/resource/pubmed/commentcorrection/3223921-5964395, http://linkedlifedata.com/resource/pubmed/commentcorrection/3223921-6421318, http://linkedlifedata.com/resource/pubmed/commentcorrection/3223921-6431970, http://linkedlifedata.com/resource/pubmed/commentcorrection/3223921-6455434, http://linkedlifedata.com/resource/pubmed/commentcorrection/3223921-6541055, http://linkedlifedata.com/resource/pubmed/commentcorrection/3223921-667049, http://linkedlifedata.com/resource/pubmed/commentcorrection/3223921-6890381, http://linkedlifedata.com/resource/pubmed/commentcorrection/3223921-690133, http://linkedlifedata.com/resource/pubmed/commentcorrection/3223921-7126174, http://linkedlifedata.com/resource/pubmed/commentcorrection/3223921-7194337, http://linkedlifedata.com/resource/pubmed/commentcorrection/3223921-7200802, http://linkedlifedata.com/resource/pubmed/commentcorrection/3223921-7295669, http://linkedlifedata.com/resource/pubmed/commentcorrection/3223921-993210
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0264-6021
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
256
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
421-7
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Proteolytic dissection as a probe of conformational changes in the human erythrocyte glucose transport protein.
pubmed:affiliation
Department of Biochemistry and Chemistry, Royal Free Hospital School of Medicine (University of London), U.K.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't