20540760

Source:http://linkedlifedata.com/resource/pubmed/id/20540760

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0015576, umls-concept:C0030946, umls-concept:C0038592, umls-concept:C0072114, umls-concept:C0086418, umls-concept:C0444626, umls-concept:C0678594, umls-concept:C1418873, umls-concept:C1704788
pubmed:dateCreated	2010-6-30
pubmed:abstractText	The unique S28 family of proteases is comprised of the carboxypeptidase PRCP and the aminopeptidase DPP7. The structural basis of the different substrate specificities of the two enzymes is not understood nor has the structure of the S28 fold been described.
pubmed:commentsCorrections	http://linkedlifedata.com/resource/pubmed/commentcorrection/20540760-10477574, http://linkedlifedata.com/resource/pubmed/commentcorrection/20540760-10570924, http://linkedlifedata.com/resource/pubmed/commentcorrection/20540760-10607665, http://linkedlifedata.com/resource/pubmed/commentcorrection/20540760-11173530, http://linkedlifedata.com/resource/pubmed/commentcorrection/20540760-12483204, http://linkedlifedata.com/resource/pubmed/commentcorrection/20540760-12690074, http://linkedlifedata.com/resource/pubmed/commentcorrection/20540760-1409539, http://linkedlifedata.com/resource/pubmed/commentcorrection/20540760-14514675, http://linkedlifedata.com/resource/pubmed/commentcorrection/20540760-14996700, http://linkedlifedata.com/resource/pubmed/commentcorrection/20540760-15487984, http://linkedlifedata.com/resource/pubmed/commentcorrection/20540760-17149884, http://linkedlifedata.com/resource/pubmed/commentcorrection/20540760-17452350, http://linkedlifedata.com/resource/pubmed/commentcorrection/20540760-18396440, http://linkedlifedata.com/resource/pubmed/commentcorrection/20540760-19620781, http://linkedlifedata.com/resource/pubmed/commentcorrection/20540760-20382998, http://linkedlifedata.com/resource/pubmed/commentcorrection/20540760-28321, http://linkedlifedata.com/resource/pubmed/commentcorrection/20540760-4297812, http://linkedlifedata.com/resource/pubmed/commentcorrection/20540760-4620382, http://linkedlifedata.com/resource/pubmed/commentcorrection/20540760-4969969, http://linkedlifedata.com/resource/pubmed/commentcorrection/20540760-6055465, http://linkedlifedata.com/resource/pubmed/commentcorrection/20540760-7451650, http://linkedlifedata.com/resource/pubmed/commentcorrection/20540760-7893686, http://linkedlifedata.com/resource/pubmed/commentcorrection/20540760-8344943, http://linkedlifedata.com/resource/pubmed/commentcorrection/20540760-8377180, http://linkedlifedata.com/resource/pubmed/commentcorrection/20540760-8591035, http://linkedlifedata.com/resource/pubmed/commentcorrection/20540760-9695945
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/101088689
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Carboxypeptidases, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins, http://linkedlifedata.com/resource/pubmed/chemical/lysosomal Pro-X carboxypeptidase
pubmed:status	MEDLINE
pubmed:issn	1472-6807
pubmed:author	pubmed-author:AbeywickremaPravien DPD, pubmed-author:ByrneNoel JNJ, pubmed-author:DiehlRonald ERE, pubmed-author:FordRachael ERE, pubmed-author:HallDawn LDL, pubmed-author:LumbKevin JKJ, pubmed-author:PatelSangita BSB, pubmed-author:ReidJohn CJC, pubmed-author:RickertKeith WKW, pubmed-author:SharmaSujataS, pubmed-author:ShipmanJennifer MJM, pubmed-author:SoissonStephen MSM
pubmed:issnType	Electronic
pubmed:volume	10
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	16
pubmed:dateRevised	2010-9-30
pubmed:meshHeading	pubmed-meshheading:20540760-Amino Acid Sequence, pubmed-meshheading:20540760-Binding Sites, pubmed-meshheading:20540760-Carboxypeptidases, pubmed-meshheading:20540760-Catalytic Domain, pubmed-meshheading:20540760-Crystallography, X-Ray, pubmed-meshheading:20540760-Humans, pubmed-meshheading:20540760-Molecular Sequence Data, pubmed-meshheading:20540760-Protein Structure, Tertiary, pubmed-meshheading:20540760-Recombinant Proteins, pubmed-meshheading:20540760-Sequence Alignment, pubmed-meshheading:20540760-Sequence Homology, Amino Acid, pubmed-meshheading:20540760-Substrate Specificity
pubmed:year	2010
pubmed:articleTitle	Structural definition and substrate specificity of the S28 protease family: the crystal structure of human prolylcarboxypeptidase.
pubmed:affiliation	Global Structural Biology, Merck Research Laboratories, P,O, Box 4, West Point, PA 19486, USA. stephen_soisson@merck.com
pubmed:publicationType	Journal Article