about
ATP dependent rotational motion of group II chaperonin observed by X-ray single molecule trackingStructural dynamics of a single-chain Fv antibody against (4-hydroxy-3-nitrophenyl)acetyl.Real time ligand-induced motion mappings of AChBP and nAChR using X-ray single molecule trackingNano-mechanical methods in biochemistry using atomic force microscopy.Dynamics of a partially stretched protein molecule studied using an atomic force microscope.Molecular shape and binding force of Mycoplasma mobile's leg protein Gli349 revealed by an AFM study.Asymmetry in the function and dynamics of the cytosolic group II chaperonin CCT/TRiCDirect detection of cellular adaptation to local cyclic stretching at the single cell level by atomic force microscopy.Nonlinear displacement of ventral stress fibers under externally applied lateral force by an atomic force microscope.Forced extension of delipidated red blood cell cytoskeleton with little indication of spectrin unfolding.Interaction between pheromone and its receptor of the fission yeast Schizosaccharomyces pombe examined by a force spectroscopy study.Nanotechnology and protein mechanics.Cooling dynamics of self-assembled monolayer coating for integrated gold nanocrystals on a glass substrate.Characterization of group II chaperonins from an acidothermophilic archaeon Picrophilus torridus.A small-angle X-ray scattering study of alpha-synuclein from human red blood cellsPlatonic Micelles: Monodisperse Micelles with Discrete Aggregation Numbers Corresponding to Regular Polyhedra.Time-resolved X-ray Tracking of Expansion and Compression Dynamics in Supersaturating Ion-Networks.Single-molecule motions of MHC class II rely on bound peptides.Tracking 3D picometer-scale motions of single nanoparticles with high-energy electron probes.Nanoscale Dynamics of Protein Assembly Networks in Supersaturated Solutions.Diffracted X-ray tracking for monitoring intramolecular motion in individual protein molecules using broad band X-ray.Methods for reducing nonspecific interaction in antibody-antigen assay via atomic force microscopy.Unfolding study of native bacteriorhodopsin under acidic condition.First observation of metal ion-induced structural fluctuations of α-helical peptides by using diffracted X-ray tracking.High-sensitivity detection of proteins using gel electrophoresis and atomic force microscopy.Time-Resolved Measurement of the ATP-Dependent Motion of the Group II Chaperonin by Diffracted Electron Tracking.X-ray observations of single bio-supramolecular photochirogenesisDNA-binding induced conformational change of c-Myb R2R3 analyzed using diffracted X-ray trackingProgression of 3D Protein Structure and Dynamics MeasurementsInter-Ring Communication Is Dispensable in the Reaction Cycle of Group II ChaperoninsNanoscale Chemical Composition Analysis Using Peptides Targeting Inorganic MaterialsMolecular Dynamics Study of Forced Dissociation Process of Wheat Germ Agglutinin DimerSingle molecular dynamic interactions between glycophorin A and lectin as probed by atomic force microscopyDiffracted X-ray Blinking Tracks Single Protein MotionsOverview of "2SEA Frontiers of Synchrotron Radiation Biophysics" session of symposia in the 57th Annual Meeting of Biophysical Society of JapanMechanical Stabilization of Deoxyribonucleic Acid Solid Films Based on Hydrated Ionic Liquid
P50
Q27319527-B5B5AC06-333C-467F-B7AF-7FEEFBF2B6ACQ30388478-7E015EDD-6F6E-4BEA-BFB5-995B86151C60Q30587060-B4FF31E9-1825-4157-8CCC-BEEC434BB069Q30938658-46B88110-2D73-42EA-A1FC-8AAABC6E6375Q33197902-D8BEDCE0-7E80-45DB-A1F0-B67B47425BFCQ33518106-CA41F2DA-BF6A-4DB7-9DC3-F33EF5A32F27Q33626712-59D6AE0B-636B-4BA7-A6F6-DEE34A56FC30Q33808003-C164780A-988E-4EA7-96FE-D02A9F4B0CFFQ34041356-194D3DE1-7999-4BCB-AC36-ABE83CE7D5B3Q34116125-05772F8E-9307-42BC-9D74-E0F0341F8C55Q34231608-7BFC6C36-D6E0-4BA9-8B54-7440E78D3B1EQ34560576-F18E89DD-EDAD-478F-BBEB-F715AD24CF78Q35533490-F5C2E985-8655-4607-B8EA-CFC21B00E44FQ37063845-08D3F2F5-BCD9-41B1-979B-048834053E49Q37137415-4FC3BD36-56D9-4AD3-91AB-826EBAD63017Q37698731-9AD6757A-F2C4-4C2C-B929-E33245BC5EE5Q40220553-938E0300-87F3-4D3D-9E6B-AE4D3AD8143FQ41550764-15ADDE90-5059-4BDB-88F5-0B7AB8048277Q43085868-2D00106E-720A-4FC5-93C9-9A5B47E263A8Q45337719-D85A292D-9DF6-437F-97B8-16ABFD2CD82AQ45796847-9F4E54FA-C218-49D7-81ED-2708FEB67C2BQ47631303-78E84C58-022D-4276-96C7-7C55676F94B8Q47789650-906DBC0E-A556-4494-9848-00339FA22B98Q47891954-2DDE9DBB-AC50-4DDE-9868-6A7C866CF844Q51735583-6F837106-8F6D-4A3A-912F-A1404D264679Q52642765-C1970965-039D-4039-AE7D-26E70E5B70D3Q58824023-437A30C9-8F8E-4C53-8DF2-0A261220AE9CQ58824024-460A479E-59C7-4C0D-A806-DE713B1911C7Q58824026-C03884F7-2B03-4BE5-A2AC-A00B37371EF3Q58824032-0C7AF859-FF33-4D7A-B33F-030DF23AB098Q58824042-AAE69704-7682-407D-B193-E8E948C33AC3Q58824044-7C303AA7-5699-4EA9-BA8E-FB41B8664D9CQ58824045-E349D818-CAAA-4032-8FFB-132C287D7B61Q59799378-270B8D84-AC0F-47AD-B7E1-BF2FC5D21BE2Q90253545-F167D43E-CA59-44CA-9274-2F5FB4F9CAD8Q91683385-CA580C0E-4476-407C-ADA0-3A90CE4D380C
P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Hiroshi Sekiguchi
@ast
Hiroshi Sekiguchi
@en
Hiroshi Sekiguchi
@es
Hiroshi Sekiguchi
@nl
Hiroshi Sekiguchi
@sl
type
label
Hiroshi Sekiguchi
@ast
Hiroshi Sekiguchi
@en
Hiroshi Sekiguchi
@es
Hiroshi Sekiguchi
@nl
Hiroshi Sekiguchi
@sl
prefLabel
Hiroshi Sekiguchi
@ast
Hiroshi Sekiguchi
@en
Hiroshi Sekiguchi
@es
Hiroshi Sekiguchi
@nl
Hiroshi Sekiguchi
@sl
P1053
C-7365-2011
P106
P1153
7103358613
P31
P3829
P3835
hiroshi-sekiguchi3
P496
0000-0001-7590-3624