| pubmed-article:20937034 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20937034 | lifeskim:mentions | umls-concept:C0001483 | lld:lifeskim |
| pubmed-article:20937034 | lifeskim:mentions | umls-concept:C1304649 | lld:lifeskim |
| pubmed-article:20937034 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:20937034 | lifeskim:mentions | umls-concept:C1948066 | lld:lifeskim |
| pubmed-article:20937034 | lifeskim:mentions | umls-concept:C0030935 | lld:lifeskim |
| pubmed-article:20937034 | lifeskim:mentions | umls-concept:C0018270 | lld:lifeskim |
| pubmed-article:20937034 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:20937034 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:20937034 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:20937034 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:20937034 | lifeskim:mentions | umls-concept:C0337141 | lld:lifeskim |
| pubmed-article:20937034 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:20937034 | pubmed:dateCreated | 2011-2-25 | lld:pubmed |
| pubmed-article:20937034 | pubmed:abstractText | Here we present a study of five analogues of a fragment from the shaft domain of the adenovirus fibre protein that readily form fibrils under a range of conditions. Using atomic force microscopy the fibrillisation of these peptides at the liquid/solid interface utilizing ordered crystalline substrates has been investigated. Our results demonstrate that the assembly pathway at the liquid/solid interface enables only the formation of truncated fibrillar structures, which align along the substrate's underlying atomic lattice during growth. Furthermore, that the concentration and volume of solution applied can be used to directly control the density of fibrillar coverage at the surface. | lld:pubmed |
| pubmed-article:20937034 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20937034 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20937034 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:20937034 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20937034 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20937034 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20937034 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20937034 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20937034 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:20937034 | pubmed:issn | 1875-5305 | lld:pubmed |
| pubmed-article:20937034 | pubmed:author | pubmed-author:AllenStephani... | lld:pubmed |
| pubmed-article:20937034 | pubmed:author | pubmed-author:MitrakiAnnaA | lld:pubmed |
| pubmed-article:20937034 | pubmed:author | pubmed-author:RobertsClive... | lld:pubmed |
| pubmed-article:20937034 | pubmed:author | pubmed-author:TendlerSaul... | lld:pubmed |
| pubmed-article:20937034 | pubmed:author | pubmed-author:SedmanVictori... | lld:pubmed |
| pubmed-article:20937034 | pubmed:author | pubmed-author:ChenXinyongX | lld:pubmed |
| pubmed-article:20937034 | pubmed:author | pubmed-author:KasotakisEmma... | lld:pubmed |
| pubmed-article:20937034 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20937034 | pubmed:volume | 18 | lld:pubmed |
| pubmed-article:20937034 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20937034 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20937034 | pubmed:pagination | 268-74 | lld:pubmed |
| pubmed-article:20937034 | pubmed:meshHeading | pubmed-meshheading:20937034... | lld:pubmed |
| pubmed-article:20937034 | pubmed:meshHeading | pubmed-meshheading:20937034... | lld:pubmed |
| pubmed-article:20937034 | pubmed:meshHeading | pubmed-meshheading:20937034... | lld:pubmed |
| pubmed-article:20937034 | pubmed:meshHeading | pubmed-meshheading:20937034... | lld:pubmed |
| pubmed-article:20937034 | pubmed:meshHeading | pubmed-meshheading:20937034... | lld:pubmed |
| pubmed-article:20937034 | pubmed:meshHeading | pubmed-meshheading:20937034... | lld:pubmed |
| pubmed-article:20937034 | pubmed:meshHeading | pubmed-meshheading:20937034... | lld:pubmed |
| pubmed-article:20937034 | pubmed:meshHeading | pubmed-meshheading:20937034... | lld:pubmed |
| pubmed-article:20937034 | pubmed:meshHeading | pubmed-meshheading:20937034... | lld:pubmed |
| pubmed-article:20937034 | pubmed:year | 2011 | lld:pubmed |
| pubmed-article:20937034 | pubmed:articleTitle | Surface-templated fibril growth of peptide fragments from the shaft domain of the adenovirus fibre protein. | lld:pubmed |
| pubmed-article:20937034 | pubmed:affiliation | Laboratory of Biophysics and Surface Analysis, School of Pharmacy, The University of Nottingham, Nottingham, UK. | lld:pubmed |
| pubmed-article:20937034 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:20937034 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
