Dissecting streptavidin-biotin interaction with a laminar flow chamber.
about
Peptide tag forming a rapid covalent bond to a protein, through engineering a bacterial adhesinA streptavidin variant with slower biotin dissociation and increased mechanostabilityMagnetic fingerprints of rolling cells for quantitative flow cytometry in whole bloodHow the biotin–streptavidin interaction was made even stronger: investigation via crystallography and a chimaeric tetramerDynamics of receptor-mediated nanoparticle internalization into endothelial cellsBead mediated separation of microparticles in droplets.Dual Recognition Element Lateral Flow Assay Toward Multiplex Strain Specific Influenza Virus Detection.A Rough Energy Landscape to Describe Surface-Linked Antibody and Antigen Bond Formation.Reconsideration of dynamic force spectroscopy analysis of streptavidin-biotin interactions.Effects of intermediate bound states in dynamic force spectroscopy.Specific recognition of macroscopic objects by the cell surface: evidence for a receptor density threshold revealed by micrometric particle binding characteristicsBeta-1 integrin-mediated adhesion may be initiated by multiple incomplete bonds, thus accounting for the functional importance of receptor clustering.Quantitative modeling assesses the contribution of bond strengthening, rebinding and force sharing to the avidity of biomolecule interactions.Shear stress increases the residence time of adhesion of Pseudomonas aeruginosa.Unraveling the role of surface mucus-binding protein and pili in muco-adhesion of Lactococcus lactisEngineering Streptavidin and a Streptavidin-Binding Peptide with Infinite Binding Affinity and Reversible Binding Capability: Purification of a Tagged Recombinant Protein to High Purity via Affinity-Driven Thiol CouplingIn vivo PEG modification of vascular surfaces for targeted deliveryExtending Bell's model: how force transducer stiffness alters measured unbinding forces and kinetics of molecular complexes.Tuning the formation and rupture of single ligand-receptor bonds by hyaluronan-induced repulsion.Biomolecule association rates do not provide a complete description of bond formation.How Cells feel their environment: a focus on early dynamic events.Studying Molecular Interactions at the Single Bond Level with a Laminar Flow Chamber.Determination of single cell surface protein expression using a tagless microfluidic method.Cell membrane alignment along adhesive surfaces: contribution of active and passive cell processes.Kinetics and mechanics of two-dimensional interactions between T cell receptors and different activating ligandsThe cellular environment regulates in situ kinetics of T-cell receptor interaction with peptide major histocompatibility complex.Dissecting subsecond cadherin bound states reveals an efficient way for cells to achieve ultrafast probing of their environment.Electrical detection of fast reaction kinetics in nanochannels with an induced flow.Quantum dot targeting with lipoic acid ligase and HaloTag for single-molecule imaging on living cells.The solution to the streptavidin-biotin paradox: the influence of history on the strength of single molecular bonds.Friction force microscopy as an alternative method to probe molecular interactions.Analyzing single-bond experiments: influence of the shape of the energy landscape and universal law between the width, depth, and force spectrum of the bond.Stochastic dynamics of adhesion clusters under shared constant force and with rebinding.Dynamics of detachment of Escherichia coli from plasma-mediated coatings under shear flow.
P2860
Q24610696-EFB42842-BF6D-4881-B97C-D58C0D674775Q24630310-6EF23D12-6F01-480D-ADE3-D89952760D1DQ27312347-526919CF-CD90-4DE5-A6E1-18022A303DFEQ27666604-E688EA47-9B2E-4502-8AAD-C66D51C598F7Q28546649-625E1DF9-7E14-4C57-B87B-79E2A68D240BQ30360146-BEAB22E2-EC96-456C-B6AB-0F681DE2A33FQ30402541-96798FB1-9A5F-4F16-8B06-5396EA0EE646Q30820933-93809434-E803-421A-ACA9-7CF2F17517CAQ33608708-7B92A993-B934-483E-A991-65E8FE4FAE06Q34184910-69160469-769E-4D58-8105-B366D9EC61F5Q34185774-667C49EC-F354-4226-B5A4-C60391E86CC4Q34186139-204E6A10-540B-4DAE-85BC-996997D0FAD2Q34424986-6A6AD1B1-7D74-4D7B-8A61-D62BE2D40BD9Q34494515-8B202B22-A407-40E4-93EB-F6F9CEEB7A70Q35048740-D9AA19D5-6049-48F6-99E3-DDCC536546CDQ35787955-3619F94C-B37C-458B-8BA7-2AF98AC8EA1CQ35869834-44FD5118-1DE3-47F0-BF8A-615ACD05CE82Q36494889-78AA615B-CCEB-4F7B-8E49-EB44514F2075Q36908316-48071B89-45A7-4E7E-8D61-73E67F7E3757Q37263754-FAA8078C-137A-4FAF-AB14-F6D19FCBECB4Q37820172-E7DCFEB0-AF72-437F-A1E8-338DD909148FQ37820173-62F6F78B-508C-47BF-9414-4EA35F704E71Q39380153-410A250D-6AA4-459C-BDE8-57B9995A6140Q40232501-AF70461C-C1EC-4596-901C-76255FF58253Q40487156-F296A13C-3766-4106-8631-D5DB71AC08B7Q40972761-4D7B474E-E0D5-4058-B1D7-C9328E7EB8B2Q41353371-E8DBAE7F-8EC4-44F4-A6C5-BE2D98FE9FB2Q41987827-CBFB2D8B-774C-464B-9988-D9A0A81105EEQ42127438-BC5A1F65-DC0D-4564-B098-049956657667Q42183779-A9100BEE-5EF1-4168-AF7F-04705C4AA0DCQ46612110-9E1B67A9-0447-4362-9EA3-77129A07A83EQ51622285-3F87A80F-6D9B-4C89-B6C2-F857BA9E3B4FQ51984848-67E1B011-893E-4A54-9B57-E29E0811AB4CQ54328378-C2B7AB09-EEEC-456C-A404-B23130707776
P2860
Dissecting streptavidin-biotin interaction with a laminar flow chamber.
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
2002年论文
@zh
2002年论文
@zh-cn
name
Dissecting streptavidin-biotin interaction with a laminar flow chamber.
@en
type
label
Dissecting streptavidin-biotin interaction with a laminar flow chamber.
@en
prefLabel
Dissecting streptavidin-biotin interaction with a laminar flow chamber.
@en
P2093
P2860
P1433
P1476
Dissecting streptavidin-biotin interaction with a laminar flow chamber.
@en
P2093
Anne Pierres
Anne-Marie Benoliel
Dominique Touchard
Pierre Bongrand
P2860
P304
P356
10.1016/S0006-3495(02)75664-6
P407
P577
2002-06-01T00:00:00Z