Predicate |
Object |
contentType |
Journal Article|Research Support, Non-U.S. Gov't|Review |
endingPage |
2204 |
issn |
1570-9639 |
issueIdentifier |
10 |
pageRange |
2195-2204 |
publicationName |
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics |
startingPage |
2195 |
hasFundingAgency |
http://rdf.ncbi.nlm.nih.gov/pubchem/organization/MD5_32251e7d20111da744eec1a3a0207631 |
bibliographicCitation |
Niemann HH. Structural basis of MET receptor dimerization by the bacterial invasion protein InlB and the HGF/SF splice variant NK1. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 2013 Oct;1834(10):2195–204. doi: 10.1016/j.bbapap.2012.10.012. |
creator |
http://rdf.ncbi.nlm.nih.gov/pubchem/author/MD5_bc46c180446d4cc75f1e1945a9609f4d |
date |
201310 |
identifier |
https://pubmed.ncbi.nlm.nih.gov/23123275 https://doi.org/10.1016/j.bbapap.2012.10.012 |
isPartOf |
http://rdf.ncbi.nlm.nih.gov/pubchem/journal/47985 https://portal.issn.org/resource/ISSN/1570-9639 |
language |
English |
source |
https://www.crossref.org/ https://pubmed.ncbi.nlm.nih.gov/ |
title |
Structural basis of MET receptor dimerization by the bacterial invasion protein InlB and the HGF/SF splice variant NK1 |
discusses |
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