PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 23937531-1 2013 Colloid particle deposition was applied to characterize bovine and human fibrinogen (Fb) monolayers on mica produced by controlled adsorption under diffusion transport at pH 3.5. mica 103-107 fibrinogen beta chain Homo sapiens 85-87 23937531-1 2013 Colloid particle deposition was applied to characterize bovine and human fibrinogen (Fb) monolayers on mica produced by controlled adsorption under diffusion transport at pH 3.5. mica 103-107 fibrinogen beta chain Homo sapiens 73-83 23937531-4 2013 It was shown that Fb adsorbs irreversibly on mica for a broad range of ionic strength of 4 x 10(-4) to 0.15 M, NaCl. mica 45-49 fibrinogen beta chain Homo sapiens 18-20 23937531-5 2013 The overcharging of initially negative mica surface occurred for fibrinogen surface concentrations higher than 1400 mum(-2). mica 39-43 fibrinogen beta chain Homo sapiens 65-75 23937531-9 2013 This confirms that, at this pH, fibrinogen molecules adsorb end-on on mica assuming extended conformations with the positive charge located mostly in the end part of the alphaA chains. mica 70-74 fibrinogen beta chain Homo sapiens 32-42 23621148-11 2013 Also, streaming potential measurements of fibrinogen adsorption kinetics on mica were successfully interpreted in terms of this model. mica 76-80 fibrinogen beta chain Homo sapiens 42-52 18937403-1 2008 We prepared amyloid-like fibrinogen (Fg) fibrils at pH 2.0 in the absence of thrombin; furthermore, we prepared uniform 2-D Fg fibril networks on a hydrophilic mica matrix. mica 160-164 fibrinogen beta chain Homo sapiens 124-126 21621181-7 2011 Results are discussed, obtained for cationic polyelectrolytes (PEI, PAH) and fibrinogen adsorbing on mica, interpreted quantitatively in terms of the theoretical approach postulating a heterogeneous 3D charge distribution. mica 101-105 fibrinogen beta chain Homo sapiens 77-87 21766803-3 2011 In this work, we measure the effects of solution concentration, residence time, and protein competition with BSA on the time-dependent functional changes in adsorbed fibrinogen on mica surface. mica 180-184 fibrinogen beta chain Homo sapiens 166-176 23421850-7 2013 The residual protein concentration after making contact with latex particles was determined by electrokinetic measurements and AFM imaging where the surface coverage of fibrinogen on mica was quantitatively determined. mica 183-187 fibrinogen beta chain Homo sapiens 169-179 21192636-3 2011 The conformational analysis of a large population of fibrinogen molecules on mica revealed the two most energetically favorable conformations characterized by bending angles of ~100 and 160 degrees. mica 77-81 fibrinogen beta chain Homo sapiens 53-63 21192636-5 2011 Imaging in different environments supports the expected hydration of the fibrinogen molecules in buffer, whereas imaging in humid air suggests the 2D spreading of fibrinogen on mica induced by an adsorbed water layer. mica 177-181 fibrinogen beta chain Homo sapiens 163-173 15666410-10 2005 Additionally, protein conformation and assembly orientation on these surfaces were documented where fibrinogen on HOPG formed a network-like structure, whereas fibrinogen on mica was more random. mica 174-178 fibrinogen beta chain Homo sapiens 160-170 18616311-3 2008 These probes were used to collect force measurements between the antibody and fibrinogen on mica substrates and the probability of antigen recognition was calculated. mica 92-96 fibrinogen beta chain Homo sapiens 78-88 18616311-5 2008 Macroscale platelet adhesion measurements on these mica substrates were determined to be greatest at fibrinogen residence times of approximately 45 min, which correlated well with the functional activity of adsorbed fibrinogen as measured by the modified AFM probes. mica 51-55 fibrinogen beta chain Homo sapiens 101-111 18616311-5 2008 Macroscale platelet adhesion measurements on these mica substrates were determined to be greatest at fibrinogen residence times of approximately 45 min, which correlated well with the functional activity of adsorbed fibrinogen as measured by the modified AFM probes. mica 51-55 fibrinogen beta chain Homo sapiens 216-226 20408656-0 2008 Measurement of interaction forces between fibrinogen coated probes and mica surface with the atomic force microscope: The pH and ionic strength effect. mica 71-75 fibrinogen beta chain Homo sapiens 42-52 20408656-2 2008 The authors have used atomic force microscopy (AFM) to directly measure the force of attraction/adhesion of fibrinogen coated tips to mica surfaces and reveal the effect of the surrounding solution pH and ionic strength on this interaction. mica 134-138 fibrinogen beta chain Homo sapiens 108-118 17337166-0 2007 pH and ionic strength effect on single fibrinogen molecule adsorption on mica studied with AFM. mica 73-77 fibrinogen beta chain Homo sapiens 39-49 17337166-2 2007 We have used atomic force microscopy to image, in phosphate buffer, single fibrinogen molecules adsorbed on mica and compare the surface coverage at variable pH (7.4, 5.8, 3.5) or ionic strength (15, 150, 500 mM) conditions. mica 108-112 fibrinogen beta chain Homo sapiens 75-85 15379516-1 2004 Tapping-mode atomic force microscopy was used to study the time-dependent changes in the structure of fibrinogen under aqueous conditions following adsorption on two model surfaces: hydrophobic graphite and hydrophilic mica. mica 219-223 fibrinogen beta chain Homo sapiens 102-112 9768470-6 1997 Purified human fibrinogen, together with 15-nm colloidal gold particles serving as an internal calibration standard, were adhered to a poly-L-lysine substrate on freshly cleaved mica. mica 178-182 fibrinogen beta chain Homo sapiens 15-25 12757384-3 2003 After adhesion to the mica surface, both liposomes without fibrinogen and liposomes with attached fibrinogen collapsed into patches. mica 22-26 fibrinogen beta chain Homo sapiens 59-69 12757384-3 2003 After adhesion to the mica surface, both liposomes without fibrinogen and liposomes with attached fibrinogen collapsed into patches. mica 22-26 fibrinogen beta chain Homo sapiens 98-108 10494763-8 1999 Quantitative dimensional analysis, which yielded structural information in three dimensions, indicates that surface-dependent structural deformation or spreading of fibrinogen increases according to the order: mica < APTES < OTS. mica 210-214 fibrinogen beta chain Homo sapiens 165-175 870006-1 1977 A mica adsorption technique was used to prepare fibrinogen and early fibrin polymers for examination in the transmission electron microscope. mica 2-6 fibrinogen beta chain Homo sapiens 48-58 960051-0 1976 Fibrinogen structure after spraying on mica: assessing the electron microscopic basis for a trinodular model. mica 39-43 fibrinogen beta chain Homo sapiens 0-10 4327023-1 1971 I. Competetive adsorption of fibrinogen and heparin on mica. mica 55-59 fibrinogen beta chain Homo sapiens 29-39