reference/10608290

http://rdf.ncbi.nlm.nih.gov/pubchem/reference/10608290

Outgoing Links

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contentType	Journal Article\|Research Support, Non-U.S. Gov't
endingPage	118
issn	0022-2836
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pageRange	102-118
publicationName	Journal of molecular biology
startingPage	102
hasFundingAgency	http://rdf.ncbi.nlm.nih.gov/pubchem/organization/MD5_aec4825d20e6536fa94395fa864468ce http://rdf.ncbi.nlm.nih.gov/pubchem/organization/MD5_e4b7799b7b1f11aa93c9c8c1592f6892 http://rdf.ncbi.nlm.nih.gov/pubchem/organization/MD5_f2869a8020d1cfb546b8497c7d0aa646
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bibliographicCitation	Furtado PB, Huang CY, Ihyembe D, Hammond RA, Marsh HC, Perkins SJ. The partly folded back solution structure arrangement of the 30 SCR domains in human complement receptor type 1 (CR1) permits access to its C3b and C4b ligands. J Mol Biol. 2008 Jan 04;375(1):102–18. doi: 10.1016/j.jmb.2007.09.085. PMID: 18028942.
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date	2008-01-04-04:00^^<http://www.w3.org/2001/XMLSchema#date>
identifier	https://pubmed.ncbi.nlm.nih.gov/18028942 https://doi.org/10.1016/j.jmb.2007.09.085
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language	English
source	https://pubmed.ncbi.nlm.nih.gov/ https://www.crossref.org/
title	The Partly Folded Back Solution Structure Arrangement of the 30 SCR Domains in Human Complement Receptor Type 1 (CR1) Permits Access to its C3b and C4b Ligands
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Total number of triples: 43.