17418086

Source:http://linkedlifedata.com/resource/pubmed/id/17418086

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0002270, umls-concept:C0007625, umls-concept:C0017033, umls-concept:C0086418, umls-concept:C0332185, umls-concept:C0337051, umls-concept:C0376315, umls-concept:C1509144, umls-concept:C1524075, umls-concept:C1706853, umls-concept:C1707271, umls-concept:C1879748
pubmed:issue	1
pubmed:dateCreated	2007-6-12
pubmed:abstractText	Assembly of alpha-globin with translated, full-length and C-terminal truncated human gamma-globin to form Hb F was assessed in a cell-free transcription/translation system. Polysome profiles showed two amino acid C-terminal-truncated gamma-chains retained on polysomes can assemble with unlabeled holo alpha-chains only after puromycin-induced chain release. Two amino acid C-terminal truncated gamma-chains encoded from vectors containing a stop codon at the translation termination site were released from polysomes and assembled with alpha-chains in the absence of puromycin addition, while removal of 11 or more amino acids from the gamma-chain carboxy-terminus inhibited assembly with alpha-chains. These results suggest that amino acids in the HC- and H-helix gamma-chain regions including amino acids 135-144 at the C-terminus in the translated gamma-chains play a key role in assembly with alpha-chains, and that assembly occurs soon after exit of translated gamma-chains from the ribosome tunnel and release from polysomes thereby preventing stable gamma(2) homo-dimer formation.
pubmed:grant	http://linkedlifedata.com/resource/pubmed/grant/DK61692, http://linkedlifedata.com/resource/pubmed/grant/HL58879, http://linkedlifedata.com/resource/pubmed/grant/HL69256, http://linkedlifedata.com/resource/pubmed/grant/HL70585, http://linkedlifedata.com/resource/pubmed/grant/HL70596, http://linkedlifedata.com/resource/pubmed/grant/R01 HL058879-07, http://linkedlifedata.com/resource/pubmed/grant/R01 HL058879-08
pubmed:commentsCorrections	http://linkedlifedata.com/resource/pubmed/commentcorrection/17418086-10512867, http://linkedlifedata.com/resource/pubmed/commentcorrection/17418086-10772884, http://linkedlifedata.com/resource/pubmed/commentcorrection/17418086-10777526, http://linkedlifedata.com/resource/pubmed/commentcorrection/17418086-10937990, http://linkedlifedata.com/resource/pubmed/commentcorrection/17418086-11233172, http://linkedlifedata.com/resource/pubmed/commentcorrection/17418086-11827978, http://linkedlifedata.com/resource/pubmed/commentcorrection/17418086-12066189, http://linkedlifedata.com/resource/pubmed/commentcorrection/17418086-12706346, http://linkedlifedata.com/resource/pubmed/commentcorrection/17418086-12939154, http://linkedlifedata.com/resource/pubmed/commentcorrection/17418086-15545996, http://linkedlifedata.com/resource/pubmed/commentcorrection/17418086-1694572, http://linkedlifedata.com/resource/pubmed/commentcorrection/17418086-1943802, http://linkedlifedata.com/resource/pubmed/commentcorrection/17418086-3539223, http://linkedlifedata.com/resource/pubmed/commentcorrection/17418086-3957922, http://linkedlifedata.com/resource/pubmed/commentcorrection/17418086-4528029, http://linkedlifedata.com/resource/pubmed/commentcorrection/17418086-6173568, http://linkedlifedata.com/resource/pubmed/commentcorrection/17418086-6504915, http://linkedlifedata.com/resource/pubmed/commentcorrection/17418086-6602634, http://linkedlifedata.com/resource/pubmed/commentcorrection/17418086-6646230, http://linkedlifedata.com/resource/pubmed/commentcorrection/17418086-6863236, http://linkedlifedata.com/resource/pubmed/commentcorrection/17418086-723949, http://linkedlifedata.com/resource/pubmed/commentcorrection/17418086-7622554, http://linkedlifedata.com/resource/pubmed/commentcorrection/17418086-766070, http://linkedlifedata.com/resource/pubmed/commentcorrection/17418086-7907594, http://linkedlifedata.com/resource/pubmed/commentcorrection/17418086-7980567, http://linkedlifedata.com/resource/pubmed/commentcorrection/17418086-8995292, http://linkedlifedata.com/resource/pubmed/commentcorrection/17418086-9619585
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/0372430
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Blood Proteins, http://linkedlifedata.com/resource/pubmed/chemical/ERAF protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Fetal Hemoglobin, http://linkedlifedata.com/resource/pubmed/chemical/Globins, http://linkedlifedata.com/resource/pubmed/chemical/Molecular Chaperones
pubmed:status	MEDLINE
pubmed:month	Jul
pubmed:issn	0003-9861
pubmed:author	pubmed-author:AdachiKazuhikoK, pubmed-author:LakkaVinaysagarV, pubmed-author:SurreySaulS, pubmed-author:WeissMitchell JMJ, pubmed-author:ZhaoYiY
pubmed:issnType	Print
pubmed:day	1
pubmed:volume	463
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	60-7
pubmed:dateRevised	2009-11-18
pubmed:meshHeading	pubmed-meshheading:17418086-Blood Proteins, pubmed-meshheading:17418086-Cell-Free System, pubmed-meshheading:17418086-Fetal Hemoglobin, pubmed-meshheading:17418086-Globins, pubmed-meshheading:17418086-Humans, pubmed-meshheading:17418086-Molecular Chaperones, pubmed-meshheading:17418086-Polyribosomes, pubmed-meshheading:17418086-Triticum
pubmed:year	2007
pubmed:articleTitle	Assembly of recently translated full-length and C-terminal truncated human gamma-globin chains with a pool of alpha-globin chains to form Hb F in a cell-free system.
pubmed:affiliation	The Children's Hospital of Philadelphia, Division of Hematology, University of Pennsylvania School of Medicine, 34th Street & Civic Center Boulevard, Philadelphia, PA 19104, USA. adachi@email.chop.edu
pubmed:publicationType	Journal Article, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural