PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 11777392-0 2001 Fibrinogen-conjugated albumin polymers and their interaction with platelets under flow conditions. Polymers 30-38 fibrinogen beta chain Homo sapiens 0-10 10346888-3 1999 The binding ability of each sulfated polymer was estimated by having each polymer-containing buffer interact with the sensor chip surfaces that had immobilized fibrinogen. Polymers 37-44 fibrinogen beta chain Homo sapiens 160-170 11263807-9 2000 Blood compatibility of the polymer alloy was evaluated by observation of fibrinogen adsorption and platelet adhesion from human plasma. Polymers 27-34 fibrinogen beta chain Homo sapiens 73-83 9465033-3 1998 At later times, long flexible polymers made up of 30 or more fibrinogen and fragment E units, with a tendency for lateral aggregation and tangle formation, were seen. Polymers 30-38 fibrinogen beta chain Homo sapiens 61-71 10397958-4 1999 Thus fibrinogen bound to droplets of PDMS renders an adhesive potential to the surface of the droplets, a potential that may have relevance to the biologic processing of the polymer in vivo. Polymers 174-181 fibrinogen beta chain Homo sapiens 5-15 9616708-1 1997 The role of fibrinogen in the adherence of macrophages to polymer surfaces was studied using a human cell line (THP-1 cells) and polystyrene-divinylbenzene beads coated with poly(ethylene oxide)/poly(propylene oxide) copolymers of the form PEO alpha PPO beta PEO alpha. Polymers 58-65 fibrinogen beta chain Homo sapiens 12-22 9493069-2 1998 Water soluble polymer (PEG Mw = 20 KD) beads of 100-150 microns were added (12% by volume) to the fibrinogen to obtain a porous and rough structure. Polymers 14-21 fibrinogen beta chain Homo sapiens 98-108 9056289-0 1997 Competitive Protein Adsorption at Plasma Polymer Surfaces Competitive adsorption from a ternary mixture of human serum albumin (HSA), human IgG, and human fibrinogen (Fgn) at concentrations corresponding to blood plasma diluted 1/100 was investigated with the combination of Total Internal Reflection Fluorescence spectroscopy (TIRF) and ellipsometry. Polymers 41-48 fibrinogen beta chain Homo sapiens 155-165 9299092-0 1997 Sequential Adsorption of Human Serum Albumin (HSA), Immunoglobulin G (IgG), and Fibrinogen (Fgn) at HMDSO Plasma Polymer Surfaces The sequential adsorption of human serum albumin (HSA), immunoglobulin G (IgG), and fibrinogen (Fgn) at hexamethyldisiloxane (HMDSO) plasma polymer surfaces was investigated with ellipsometry and total internal reflection fluorescence spectroscopy (TIRF) as a function of adsorption time, pH, and excess electrolyte concentration. Polymers 113-120 fibrinogen beta chain Homo sapiens 80-90 9299092-0 1997 Sequential Adsorption of Human Serum Albumin (HSA), Immunoglobulin G (IgG), and Fibrinogen (Fgn) at HMDSO Plasma Polymer Surfaces The sequential adsorption of human serum albumin (HSA), immunoglobulin G (IgG), and fibrinogen (Fgn) at hexamethyldisiloxane (HMDSO) plasma polymer surfaces was investigated with ellipsometry and total internal reflection fluorescence spectroscopy (TIRF) as a function of adsorption time, pH, and excess electrolyte concentration. Polymers 113-120 fibrinogen beta chain Homo sapiens 92-95 9056289-0 1997 Competitive Protein Adsorption at Plasma Polymer Surfaces Competitive adsorption from a ternary mixture of human serum albumin (HSA), human IgG, and human fibrinogen (Fgn) at concentrations corresponding to blood plasma diluted 1/100 was investigated with the combination of Total Internal Reflection Fluorescence spectroscopy (TIRF) and ellipsometry. Polymers 41-48 fibrinogen beta chain Homo sapiens 167-170 8996693-9 1996 The Ka was higher for M1 binding to fibrinogen adsorbed to Immulon I than to Biomer, Biospan or poly(ethylene terephthalate), suggesting that fibrinogen adsorbed to Immulon I is more platelet adhesive than fibrinogen adsorbed to the other polymers. Polymers 239-247 fibrinogen beta chain Homo sapiens 36-46 8922606-13 1996 The ellipsometric results show that the adsorption of HSA and Fg at HMS surfaces containing preadsorbed amphiphilic polymer was significantly reduced as compared to the bare HMS surface. Polymers 116-123 fibrinogen beta chain Homo sapiens 62-64 8922606-15 1996 Both polymers gave more than a 20-fold reduction of the Fg adsorption and a 10-fold reduction of the HSA adsorption. Polymers 5-13 fibrinogen beta chain Homo sapiens 56-58 9163070-7 1996 Our present and previous findings suggest that soluble fibrinogen aggregates possess a fibrin-like structure, and that fibrin or fibrinogen polymer formation is a prerequisite for the enhancing effect on t-PA-mediated plasminogen to plasmin conversion which is seen even with the polymers in the soluble state. Polymers 280-288 fibrinogen beta chain Homo sapiens 55-65 9163070-7 1996 Our present and previous findings suggest that soluble fibrinogen aggregates possess a fibrin-like structure, and that fibrin or fibrinogen polymer formation is a prerequisite for the enhancing effect on t-PA-mediated plasminogen to plasmin conversion which is seen even with the polymers in the soluble state. Polymers 280-288 fibrinogen beta chain Homo sapiens 129-139 8996693-9 1996 The Ka was higher for M1 binding to fibrinogen adsorbed to Immulon I than to Biomer, Biospan or poly(ethylene terephthalate), suggesting that fibrinogen adsorbed to Immulon I is more platelet adhesive than fibrinogen adsorbed to the other polymers. Polymers 239-247 fibrinogen beta chain Homo sapiens 142-152 8996693-9 1996 The Ka was higher for M1 binding to fibrinogen adsorbed to Immulon I than to Biomer, Biospan or poly(ethylene terephthalate), suggesting that fibrinogen adsorbed to Immulon I is more platelet adhesive than fibrinogen adsorbed to the other polymers. Polymers 239-247 fibrinogen beta chain Homo sapiens 142-152 2149071-0 1990 Plasma gas discharge deposited fluorocarbon polymers exhibit reduced elutability of adsorbed albumin and fibrinogen. Polymers 44-52 fibrinogen beta chain Homo sapiens 105-115 8608089-3 1995 Investigation of the protein adsorption of these polymer surfaces showed that copolymers with higher DMAA content adsorbed more albumin than fibrinogen. Polymers 49-56 fibrinogen beta chain Homo sapiens 141-151 1484067-3 1992 In this study fibrinogen adsorption to several polymers was examined to ascertain the influence of controlled changes in surface chemistry on the Vroman effect. Polymers 47-55 fibrinogen beta chain Homo sapiens 14-24 1484067-9 1992 The more hydrophobic polymers exhibited greater retention of adsorbed fibrinogen. Polymers 21-29 fibrinogen beta chain Homo sapiens 70-80 1610956-3 1992 These polymers were shown to delay clotting times in the following ways: by direct complex formation between the polymer and thrombin; by interference with fibrin polymerization; and by complex interactions between polymer, thrombin, plasma antiproteases and fibrinogen in plasma. Polymers 6-14 fibrinogen beta chain Homo sapiens 259-269 2035620-5 1991 Our data suggest that different methacrylate polymers induce different changes in adsorbed fibrinogen, which may interfere with its interaction with platelets, and that platelet retention in a methacrylate bead column involves interaction of the COOH-terminal end of the gamma-chain of adsorbed fibrinogen with platelet GpIIb/IIIa receptors. Polymers 45-53 fibrinogen beta chain Homo sapiens 91-101 1926582-1 1991 Fibrinogen-NDSK complex is a model of protofibril having some features of the fibrin polymer structure. Polymers 85-92 fibrinogen beta chain Homo sapiens 0-10 2283349-0 1990 Postadsorptive transitions in fibrinogen: influence of polymer properties. Polymers 55-62 fibrinogen beta chain Homo sapiens 30-40 2283349-4 1990 In this study, we have examined the effects of polymer structure and composition, chain mobility, and hydrophobicity on the postadsorptive transitions of fibrinogen. Polymers 47-54 fibrinogen beta chain Homo sapiens 154-164 2283349-5 1990 Glassy, rigid polymers showed high fibrinogen adsorption, regardless of whether the polymer was hydrophilic or hydrophobic. Polymers 14-22 fibrinogen beta chain Homo sapiens 35-45 2283349-5 1990 Glassy, rigid polymers showed high fibrinogen adsorption, regardless of whether the polymer was hydrophilic or hydrophobic. Polymers 14-21 fibrinogen beta chain Homo sapiens 35-45 2203794-5 1990 On hydrophobic polymers like polyethylene, the low amounts of adsorbed fibrinogen and HMW kininogen from plasma and concentrated plasma solutions may be due to a preferential adsorption of HDL. Polymers 15-23 fibrinogen beta chain Homo sapiens 71-81 7622528-4 1995 In some experiments the test polymers were adsorbed with fibrinogen or IgG prior to the addition of monocytes. Polymers 29-37 fibrinogen beta chain Homo sapiens 57-67 34765272-0 2021 Engineered polymer nanoparticles incorporating l-amino acid groups as affinity reagents for fibrinogen. Polymers 11-18 fibrinogen beta chain Homo sapiens 92-102 34684880-0 2021 Deposition of Polymer Particles with Fibrinogen Corona at Abiotic Surfaces under Flow Conditions. Polymers 14-21 fibrinogen beta chain Homo sapiens 37-47 34902868-5 2021 Upon conversion of fibrinogen into fibrin, the alphaC-domains switch from intra- to intermolecular interactions to form ordered alphaC polymers. Polymers 135-143 fibrinogen beta chain Homo sapiens 19-29 34765272-1 2021 Synthetic polymer hydrogel nanoparticles (NPs) were developed to function as abiotic affinity reagents for fibrinogen. Polymers 10-17 fibrinogen beta chain Homo sapiens 107-117 4005267-8 1985 These studies suggest a specific but weak interaction of the solubilizing fibrinogen with the soluble fibrin polymers as demonstrated by a rapid exchange of both macromolecules. Polymers 109-117 fibrinogen beta chain Homo sapiens 74-84 35252131-6 2022 Currently, tissue engineering has employed several synthetic polymers to design bioactive scaffolds to mimic the native ECM, by combining biopolymers with growth factors including collagen and fibrinogen. Polymers 61-69 fibrinogen beta chain Homo sapiens 180-203 2559918-0 1989 Preadsorption of polymers on glass and silica to reduce fibrinogen adsorption. Polymers 17-25 fibrinogen beta chain Homo sapiens 56-66 3730606-1 1986 Platelet activation by polymer surfaces is thought to require preliminary adsorption of fibrinogen and perhaps changes in fibrinogen conformation. Polymers 23-30 fibrinogen beta chain Homo sapiens 88-98 3730606-1 1986 Platelet activation by polymer surfaces is thought to require preliminary adsorption of fibrinogen and perhaps changes in fibrinogen conformation. Polymers 23-30 fibrinogen beta chain Homo sapiens 122-132 3568326-2 1987 The formation of factor XIIIa-catalyzed fibrin polymers during clotting of plasma and purified fibrinogen in vivo was followed by a sodium dodecyl sulfate agarose gel technique, and an increase in both amount and size of gamma-chain cross-linked polymers was demonstrated before visible clot formation. Polymers 47-55 fibrinogen beta chain Homo sapiens 95-105 3593791-6 1987 It is concluded that the formation of the regular polymer structure during fibrinogen and fibrin N-DSK complex formation requires the participation of two types of complementary centers, namely: D1-E1 and D2-E2. Polymers 50-57 fibrinogen beta chain Homo sapiens 75-85 3730606-5 1986 Tests of platelet retention and fibrinogen binding to four polyalkyl acrylates and to three unrelated polymers (polystyrene, polymethyl methacrylate, and a polyether polyurethane) indicated that platelet retention correlated positively with both total fibrinogen binding and with the amount of antibody-recognizable fibrinogen bound. Polymers 102-110 fibrinogen beta chain Homo sapiens 32-42 3976012-1 1985 Investigation of fibrin N-terminal disulphide knot (N-DSK) binding with fibrinogen (F) showed, that the F-N-DSK-complex represents growing polymer structure which is soluble at early polymerization stage and forms a solid phase during the further growth. Polymers 139-146 fibrinogen beta chain Homo sapiens 72-82 140169-3 1977 Adsorption, and possible conformational changes of fibrinogen, were found to be more substantial on polymer surfaces having a higher content of polyether segments. Polymers 100-107 fibrinogen beta chain Homo sapiens 51-61 6437004-1 1984 Early work on the purification of factor VIII using polyethylene glycol (PEG) indicated that other polymers might also be used to precipitate factor VIII leaving fibrinogen in solution. Polymers 99-107 fibrinogen beta chain Homo sapiens 162-172 7378042-13 1980 This mechanism accounts for the clinical observations of stable fibrinogen-derived polymers in the plasma from patients undergoing thrombotic processes. Polymers 83-91 fibrinogen beta chain Homo sapiens 64-74 6640056-2 1983 The adhesion force between a reference surface (glass) and different polymers (polyurethanes and cellulose derivatives) was found to be dependent on the immersion time of polymers in electrolyte and on the formation of adsorption layers of serum albumin and fibrinogen. Polymers 69-77 fibrinogen beta chain Homo sapiens 258-268 7348274-4 1981 Previous studies have indicated differences in the affinity of various proteins for a given polymer, and differences in the affinity of fibrinogen for a series of polymers varying in hydrophilicity. Polymers 163-171 fibrinogen beta chain Homo sapiens 136-146 33352490-1 2021 An excellent blood-compatible polymer, poly(2-methoxyethyl acrylate) (PMEA), exhibits nanometer-scale phase-separated structures at the interface with water or phosphate-buffered saline (PBS), and fibrinogen adsorption is suppressed, especially on the water-rich region. Polymers 30-37 fibrinogen beta chain Homo sapiens 197-207 33752337-0 2021 Fibrinogen, collagen, and transferrin adsorption to poly(3,4-ethylenedioxythiophene)-xylorhamno-uronic glycan composite conducting polymer biomaterials for wound healing applications. Polymers 131-138 fibrinogen beta chain Homo sapiens 0-10 29317059-7 2018 Also, limited reduction of human serum albumin (HSA) generates hydrophobic polymers that form huge insoluble complexes with fibrinogen. Polymers 75-83 fibrinogen beta chain Homo sapiens 124-134 30326361-3 2019 Adsorption of the proteins fibrinogen, albumin (HSA) and lysozyme on these functionalised plasma polymer surfaces was studied by XPS and quartz crystal microbalance with dissipation (QCM-D). Polymers 97-104 fibrinogen beta chain Homo sapiens 27-37 30467540-8 2018 Furthermore, the FNG molecules adsorbed on the surface of PMEA were easily desorbed, even in the polymer-rich domains. Polymers 97-104 fibrinogen beta chain Homo sapiens 17-20 30193463-8 2018 The NO-releasing polymer films were found to increase Fb adsorption, but decrease platelet adhesion and activation on the surface when compared to plasticized PVC control films. Polymers 17-24 fibrinogen beta chain Homo sapiens 54-56 30193463-9 2018 Further, to eliminate the effects of NO on platelets, NO-releasing polymer films were first exposed to Fb and then incubated until all NO was released. Polymers 67-74 fibrinogen beta chain Homo sapiens 103-105 31257890-4 2019 On films of poly(desaminotyrosyl-tyrosine-co-PEG carbonate) with high (20 wt %) PEG content, in which very little protein adsorption is expected, quartz crystal microbalance data showed significant adsorption of fibrinogen and bovine serum albumin at 8 C. The surface became protein-repellent at 37.5 C. When the same polymer was iodinated, the polymer was protein-adsorbent, even when 37 wt % PEG was incorporated into the polymer backbone. Polymers 320-327 fibrinogen beta chain Homo sapiens 212-222 31070898-1 2019 This work describes the interaction of the human blood plasma proteins albumin, fibrinogen, and gamma-globulins with micro- and nanopatterned polymer interfaces. Polymers 142-149 fibrinogen beta chain Homo sapiens 80-90 28276243-8 2017 For larger proteins like fibrinogen, adsorption is expected to occur mainly "on top" of the polymer brush, and brush thickness determines whether protein is located in the "detectable zone". Polymers 92-99 fibrinogen beta chain Homo sapiens 25-35 28548908-9 2017 We also investigated protein adsorption behavior in terms of the amount and deformation of fibrinogen adsorbed on the polymer surface. Polymers 118-125 fibrinogen beta chain Homo sapiens 91-101 29134801-4 2017 The most protein-resistant copolymer layers, eliminating fibrinogen and lysozyme adsorption within detectible limits of 0.01 mg/m2, had metrics (the amount of pMPC at the surface and the reduced tether footprint) consistent with the formation of an interfacial polymer brush. Polymers 29-36 fibrinogen beta chain Homo sapiens 57-67 28263863-3 2017 We exposed polymers with different surface chemistries to protease-free human fibrinogen. Polymers 11-19 fibrinogen beta chain Homo sapiens 78-88 33465887-0 2016 Interfacial Structures and Fibrinogen Adsorption at Blood-Compatible Polymer/Water Interfaces. Polymers 69-76 fibrinogen beta chain Homo sapiens 27-37 23911741-4 2013 This study proposed to investigate the application of these two polymers, based on their potential for globular protein adsorption (BSA and fibrinogen). Polymers 64-72 fibrinogen beta chain Homo sapiens 140-150 25025547-11 2014 The most effective surface for preventing fibrinogen adsorption was the polymer brush surface with phosphorylcholine (PC) groups, that is, poly(2-methacryloyloxyethyl phosphorylcholine) brush. Polymers 72-79 fibrinogen beta chain Homo sapiens 42-52 26007735-10 2015 The adsorption of the plasma proteins human serum albumin (HSA) and fibrinogen onto the polymer-coated surfaces were monitored. Polymers 88-95 fibrinogen beta chain Homo sapiens 44-78 25770497-2 2015 The effect of the heterogeneity of the polymer film surface on the nonspecific adsorption of the protein human plasma fibrinogen (FBN, 5.0 x 5.0 x 47.5 nm(3)) was investigated. Polymers 39-46 fibrinogen beta chain Homo sapiens 118-128 25770497-7 2015 These interesting findings can be attributed to the enhancement of the spread FBN molecule in a mobile state by the heterogeneity of polymer film surface before irreversible adsorption occurs. Polymers 133-140 fibrinogen beta chain Homo sapiens 78-81 25462849-2 2015 A precursor solution of cells in photoreactive poly(ethylene glycol) (PEG)-fibrinogen (PF) polymer was transported through a transparent injector exposed to light irradiation before being atomized in a jet-in-air nozzle. Polymers 91-98 fibrinogen beta chain Homo sapiens 75-85 24444156-5 2014 Adsorption kinetics of fibrinogen at hydrophilic and hydrophobic (polymer modified) substrates determined by various techniques is described. Polymers 66-73 fibrinogen beta chain Homo sapiens 23-33 23151385-5 2013 The results show that the adsorbed mass of fibrinogen decreased linearly with increasing CF(3)/CF(2) ratio on the fluorinated polymer surfaces. Polymers 126-133 fibrinogen beta chain Homo sapiens 43-53 19366199-0 2009 Fibrinogen adsorption and conformational change on model polymers: novel aspects of mutual molecular rearrangement. Polymers 57-65 fibrinogen beta chain Homo sapiens 0-10 20571633-0 2010 Conformational behavior of fibrinogen on topographically modified polymer surfaces. Polymers 66-73 fibrinogen beta chain Homo sapiens 27-37 20383582-3 2010 The increased rate of fibrinogen turnover has been traced to generation of fibrin by labeling the polymers with glycine C14 ethyl esters in the presence of activated fibrin stabilizing factor. Polymers 98-106 fibrinogen beta chain Homo sapiens 22-32 22503950-5 2012 The biological properties of the polymer were probed by fibrinogen adsorption, human umbilical vein endothelial cell adhesion and growth, and platelet adhesion. Polymers 33-40 fibrinogen beta chain Homo sapiens 56-66 21417688-1 2011 Ingested, inhaled or injected particles come into contact with biological fluids containing polymers, such as the protein fibrinogen. Polymers 92-100 fibrinogen beta chain Homo sapiens 122-132 19366199-1 2009 By combining quartz crystal microbalance with dissipation monitoring (QCM-D) and surface plasmon resonance (SPR), the organic mass, water content, and corresponding protein film structure of fibrinogen adsorbed to acrylic polymeric substrates with varying polymer chain flexibility was investigated. Polymers 222-229 fibrinogen beta chain Homo sapiens 191-201 19366199-3 2009 For fibrinogen, the QCM-D model resulted in decreased adsorbed mass with increased polymer chain flexibility. Polymers 83-90 fibrinogen beta chain Homo sapiens 4-14 19366199-6 2009 Fibrinogen maintained a more native conformation on the flexible polymer, probably due to polymer chain rearrangement rather than protein conformational change. Polymers 65-72 fibrinogen beta chain Homo sapiens 0-10 19366199-6 2009 Fibrinogen maintained a more native conformation on the flexible polymer, probably due to polymer chain rearrangement rather than protein conformational change. Polymers 90-97 fibrinogen beta chain Homo sapiens 0-10 19568328-0 2007 Prediction of Fibrinogen Adsorption for Biodegradable Polymers: Integration of Molecular Dynamics and Surrogate Modeling. Polymers 54-62 fibrinogen beta chain Homo sapiens 14-24 19718794-7 2009 The ability of the polymer coating to prevent the adsorption of human serum albumin (HSA) and fibrinogen (FBG) was evaluated. Polymers 19-26 fibrinogen beta chain Homo sapiens 70-104 17597372-1 2008 The present work focus on the adsorption of fibrinogen (Fgn) on to the semi-interpenetrating polymer networks (IPNs) of polyethylene glycol (PEG) and poly(2-hydroxyethyl methacrylate-co-acrylonitrile) and attempts to correlate the adsorption behaviour of proteins to the blood compatible aspects of the polymeric surfaces. Polymers 93-100 fibrinogen beta chain Homo sapiens 44-54 17597372-1 2008 The present work focus on the adsorption of fibrinogen (Fgn) on to the semi-interpenetrating polymer networks (IPNs) of polyethylene glycol (PEG) and poly(2-hydroxyethyl methacrylate-co-acrylonitrile) and attempts to correlate the adsorption behaviour of proteins to the blood compatible aspects of the polymeric surfaces. Polymers 93-100 fibrinogen beta chain Homo sapiens 56-59 19568328-1 2007 This work is a part of a series of publications devoted to the development of surrogate (semi-empirical) models for the prediction of fibrinogen adsorption onto polymer surfaces. Polymers 161-168 fibrinogen beta chain Homo sapiens 134-144 19568328-10 2007 The significance of the newly developed 3D model is that it allows high accuracy prediction of fibrinogen adsorption without the need for experimentally derived descriptors and it has better predictive quality than the original 2D surrogate model due to utilization of realistic polymer representations. Polymers 279-286 fibrinogen beta chain Homo sapiens 95-105 12462462-0 2002 Fibrinogen adsorption and platelet interactions on polymer membranes. Polymers 51-58 fibrinogen beta chain Homo sapiens 0-10 16555112-6 2006 The results showed that PEGylated surfaces adsorbed significantly less (up to 90% less) fibrinogen, and that unfolding of adsorbed fibrinogen was more pronounced on the linear mPEG layers than on the PEG-like plasma polymer surfaces. Polymers 216-223 fibrinogen beta chain Homo sapiens 131-141 17291015-5 2007 Our study addressed the question regarding to which extent systematic variations in polymer structure can be used to optimize X-ray visibility and provide tunable degradation rates while generating protein-repellant surface properties that minimize fibrinogen adsorption. Polymers 84-91 fibrinogen beta chain Homo sapiens 249-259 17291015-8 2007 Within this subgroup of polymers, there was a strong correlation between decreasing air-water contact angles and decreasing fibrinogen adsorption (R2 = 0.95). Polymers 24-32 fibrinogen beta chain Homo sapiens 124-134 16881041-5 2006 Despite the difference in behavior between albumin (substantially non-adhesive) and fibrinogen (adhesive), the interactions of the polymers with proteins do not seem to be based on hydrophobic effects but on surface polar interactions. Polymers 131-139 fibrinogen beta chain Homo sapiens 84-94 16378437-0 2006 Colloid probe AFM investigation of interactions between fibrinogen and PEG-like plasma polymer surfaces. Polymers 87-94 fibrinogen beta chain Homo sapiens 56-66 16378437-6 2006 The plasma polymer coatings with the greatest protein-repelling properties were the most PEG-like in nature and showed the strongest repulsion in interaction force measurements with the fibrinogen-coated probe. Polymers 11-18 fibrinogen beta chain Homo sapiens 186-196 16378437-9 2006 This indicates that the structure of the fibrinogen molecules on the probe is changed from an extended conformation in buffer to a flat conformation in water, with the former state allowing for stronger interaction with the polymer chains on the surface. Polymers 224-231 fibrinogen beta chain Homo sapiens 41-51 16853860-1 2005 The adsorption behavior of fibrinogen to two biomedical polyurethanes and a perfluorinated polymer has been investigated. Polymers 91-98 fibrinogen beta chain Homo sapiens 27-37 16853860-4 2005 Amide I signals from SFG demonstrate that fibrinogen has post-adsorption conformational changes that are dependent upon the polymer surface properties. Polymers 124-131 fibrinogen beta chain Homo sapiens 42-52 16149026-6 2005 Proteins of the blood sample, especially fibrinogen, and thereafter also activated platelets, bind to the specific polymer surface. Polymers 115-122 fibrinogen beta chain Homo sapiens 41-51 15154777-21 2004 Thus, the Surrogate Model can be used to accurately and unambiguously identify polymers whose fibrinogen absorption is at the limits of the range (i.e., low or high) which is an essential requirement for assessing polymers for regenerative tissue applications. Polymers 79-87 fibrinogen beta chain Homo sapiens 94-104 14762929-0 2004 Small changes in the polymer structure influence the adsorption behavior of fibrinogen on polymer surfaces: validation of a new rapid screening technique. Polymers 21-28 fibrinogen beta chain Homo sapiens 76-86 14762929-8 2004 Thus, when the test polymers were grouped by backbone composition, increased hydrophobicity of the pendent chain was significantly correlated with reduced fibrinogen adsorption. Polymers 20-28 fibrinogen beta chain Homo sapiens 155-165 14762929-11 2004 Further, we demonstrate that small changes in chemical composition can significantly influence the adsorption of human fibrinogen on polymer surfaces. Polymers 133-140 fibrinogen beta chain Homo sapiens 119-129 14762929-12 2004 The lactide-based polymers were among those polymers exhibiting the highest tendency to adsorb fibrinogen. Polymers 18-26 fibrinogen beta chain Homo sapiens 95-105 11950049-6 2002 Precoating of the polymer surfaces with human serum albumin (HSA) or fibrinogen, markedly reduced neutrophil activation, whereas coating with human immunoglobulin G (IgG), a well-known opsonin, resulted in significantly higher levels of cell activation. Polymers 18-25 fibrinogen beta chain Homo sapiens 46-79 11205440-5 2001 Two proteins, namely bovine serum albumine (BSA) and fibrinogen, were physically entrapped in these hydrogels by mixing with the polymer solutions before gel formation. Polymers 129-136 fibrinogen beta chain Homo sapiens 28-63