Myosin conformational states determined by single fluorophore polarization - Wikidata - wikimedia - TriplyDB

Myosin conformational states determined by single fluorophore polarization

Myosin conformational states determined by single fluorophore polarization

http://www.wikidata.org/entity/Q32057541

about

Coiled-coil unwinding at the smooth muscle myosin head-rod junction is required for optimal mechanical performance.Polarized fluorescence microscopy of individual and many kinesin motors bound to axonemal microtubules.Myosin V exhibits a high duty cycle and large unitary displacement Quantitative comparison of algorithms for tracking single fluorescent particles.Measurement of single macromolecule orientation by total internal reflection fluorescence polarization microscopy.Fluorescence polarization of green fluorescence protein.Kinetic differences at the single molecule level account for the functional diversity of rabbit cardiac myosin isoforms.The biochemical kinetics underlying actin movement generated by one and many skeletal muscle myosin molecules Spectral fluctuation of a single fluorophore conjugated to a protein molecule Imaging of the fluorescence spectrum of a single fluorescent molecule by prism-based spectroscopy.Regulatory and essential light chains of myosin rotate equally during contraction of skeletal muscle.Fluorescent tags of protein function in living cells.Structure and dynamics of the kinesin-microtubule interaction revealed by fluorescence polarization microscopy.Biomechanics, one molecule at a time.Light microscopy with doughnut modes: a concept to detect, characterize, and manipulate individual nanoobjects.Single molecule microscopy of biomembranes (review).Conformational change of the actomyosin complex drives the multiple stepping movement Comparative single-molecule and ensemble myosin enzymology: sulfoindocyanine ATP and ADP derivatives Thermodynamics and kinetics of a molecular motor ensemble Single-molecule dynamics of the calcium-dependent activation of plasma-membrane Ca2+-ATPase by calmodulin.Rotation of the lever arm of Myosin in contracting skeletal muscle fiber measured by two-photon anisotropy.Single-molecule fluorescence spectroscopy of enzyme conformational dynamics and cleavage mechanism.Stepping rotation of F1-ATPase visualized through angle-resolved single-fluorophore imaging.Mechanical coupling between myosin molecules causes differences between ensemble and single-molecule measurements.Dynamics and folding of single two-stranded coiled-coil peptides studied by fluorescent energy transfer confocal microscopy.Site-directed spectroscopic probes of actomyosin structural dynamics.Phosphorylation of myosin regulatory light chain has minimal effect on kinetics and distribution of orientations of cross bridges of rabbit skeletal muscle.Photophysical processes in single molecule organic fluorescent probes.Mesoscopic analysis of motion and conformation of cross-bridges.Kinetics of a single cross-bridge in familial hypertrophic cardiomyopathy heart muscle measured by reverse Kretschmann fluorescence.Single molecule kinetics in the familial hypertrophic cardiomyopathy D166V mutant mouse heart.Spectroscopy of single phycoerythrocyanin monomers: dark state identification and observation of energy transfer heterogeneities.Observing cycling of a few cross-bridges during isometric contraction of skeletal muscle Breaking the millisecond barrier: single molecule motors wobble to find their next binding sites.Three-dimensional structural dynamics of myosin V by single-molecule fluorescence polarization.Use of Single Molecule Fluorescence Polarization Microscopy to Study Protein Conformation and Dynamics of Kinesin-Microtubule Complexes.Single molecule detection approach to muscle study: kinetics of a single cross-bridge during contraction of muscle.DNA-Endonuclease Complex Dynamics by Simultaneous FRET and Fluorophore Intensity in Evanescent Field.

P2860

Q28360976-328A1A09-F35E-4FA2-A885-4B69F1D3F608 Q28362015-10357BBF-6545-4FE8-B700-7B1D990EAAE7 Q28512626-EA78D2D8-500A-413F-B3C3-DDE61BD8D388 Q30307940-71947401-0534-4BA8-BC2E-834935FE73FD Q30476746-34D0087D-8CAD-4CA5-9392-B29BDBBE9A47 Q30700877-B31F9E8C-0134-4D32-9901-2B98BF587173 Q30756973-3285F53E-620F-4265-A676-B8C8140018C7 Q30828410-B209E8C2-BE3A-4A20-A37A-EFC6821A4F6C Q30842216-79A06380-D8C3-4C9A-AA7A-F5FF7C98A5EE Q31039169-F4566729-2112-4E63-8A5B-F476E9DAA9C0 Q31060465-FDC0DD1C-6141-4830-A56C-1EA26E6FE401 Q33179627-7ABA3292-F761-48FC-8299-5D2747B38FBD Q33577618-DF9A9991-82D5-4422-95DA-BF1DB8577E07 Q33636092-C4A8CB98-49C2-414A-8DE2-460C204057C3 Q33904364-DA5D9C6D-779D-433B-BCAA-0A0BA124764C Q33926068-A88CBCB6-F86B-4FBE-9CDD-089E0F050DFF Q34034412-319D68B5-F3F4-4047-B022-8A4409B316B3 Q34173268-8F22F7B6-A7EF-4C85-AF85-54C88BE01B39 Q34173985-B4649D70-0D6D-41B2-B5A3-4FAECFEC61F5 Q34187118-483FE04B-36D1-43C4-AF7F-36DE6180D40A Q34188096-7D255CD4-4956-4668-A4BF-4004BC82A77A Q34931551-0E1D88E5-A5E3-4DAF-8DC2-48A095B107F3 Q35155735-D6455CC7-7646-4945-85AE-9D5871511194 Q36150807-2E8F92FD-94C0-4A23-AD10-DF21FFB81D71 Q37278854-B11C6E99-F21A-40E0-8F63-B56C58E5A71F Q37470689-BCF3646D-B838-44B1-A555-DFC2F8AEA421 Q37578155-653F45E0-B62D-4E3D-BCCF-2E6655B82473 Q38154104-B9084202-6234-45FE-8B96-63C82406D6B9 Q39310881-CB2F382F-F083-4F8B-B950-8A9AFDF48AED Q39859287-F63D0E8F-068F-4F6B-A6C7-D9F1E8183C8F Q40011699-118830D2-3528-4ACB-9268-FAC25982DBE3 Q40210365-00FBF16B-4B34-4919-99E3-153FF20E6209 Q41809936-F6FB8031-CD26-4675-B6CD-C35DE550612E Q43224270-516CBA96-AC35-4688-8BF0-516E6A98851A Q44379280-1D704112-7AF6-487F-836B-C590D3244684 Q47757660-86CBECB4-FA1A-4F96-BE8C-3082704AE32A Q47785204-C3071851-7E02-4F14-B366-48EB44DDA038 Q50798010-B403F7DD-635F-4F9D-B72C-5D9D414BBF8A

P2860

Myosin conformational states determined by single fluorophore polarization

http://www.wikidata.org/entity/Q32057541

description

1998 nî lūn-bûn

@nan

1998 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

1998 թվականի հուլիսին հրատարակված գիտական հոդված

@hy

1998年の論文

@ja

1998年論文

@yue

1998年論文

@zh-hant

1998年論文

@zh-hk

1998年論文

@zh-mo

1998年論文

@zh-tw

1998年论文

@wuu

name

Myosin conformational states determined by single fluorophore polarization

@ast

Myosin conformational states determined by single fluorophore polarization

@en

type

label

Myosin conformational states determined by single fluorophore polarization

@ast

Myosin conformational states determined by single fluorophore polarization

@en

prefLabel

Myosin conformational states determined by single fluorophore polarization

@ast

Myosin conformational states determined by single fluorophore polarization

@en

P1433

Q32057541-2CC3A614-CDDA-4D4D-BBB8-517D39839182

P1476

Q32057541-12438F3F-BC9F-460C-A01A-DD234E73B6CC

P2093

Q32057541-188B7BC9-EFA8-4107-A146-A7E4D7D81D2D

Q32057541-6DCF5116-1CDC-4824-B4DD-71FD9C1BE930

Q32057541-93C067FB-D0D0-4AC8-B13F-048E181E6A0F

Q32057541-9B374BA8-B6AD-47AB-92DF-1600AB06FADE

Q32057541-A1FEE7D5-8EF5-435A-A59F-8E0E9843299E

Q32057541-CE85F715-88E7-447C-9DA9-333D1BBE4427

Q32057541-E5406FA5-3F9D-46B5-9AD8-737B7931824E

Q32057541-F5E0A639-5B8F-417A-B99F-52812F130570

Q32057541-FE3971EA-99A8-4350-A055-3980E01D82E0

P2860

Q32057541-04BF5D20-285E-4EEA-97AE-13094419989D

Q32057541-084CB980-B356-4484-B24A-15C46611A293

Q32057541-129A4BC5-E99C-45C3-B2EE-C2724C674DFC

Q32057541-12D2E993-22F0-419A-8EDE-1BE25E06F1C2

Q32057541-20F44860-34F9-4F72-8102-DA2D4E4D1917

Q32057541-26AE1251-BCC7-4E73-A247-4A8BDACD2533

Q32057541-278EA800-EE2E-4FAC-8FE9-1740D3D19BB6

Q32057541-2ADAF010-842D-4310-AE8D-C40FB8F6761D

Q32057541-432B21B2-7801-416B-BC9A-E0CC52E61373

Q32057541-55F4D0EC-9E9A-4F0A-BD72-F13032CC7C8A

P304

Q32057541-AF12E9C2-4EEB-4233-B242-FEDAD3129CE7

P31

Q32057541-B2093CE1-1327-423A-B1CC-7AA5F620C5A0

P356

Q32057541-5A440F69-7476-4B2E-B3AD-AAB58C49EAFD

P407

Q32057541-FF76FD15-0605-4CA3-A9AF-D481EB74C9CE

P433

Q32057541-76034511-EBCD-4D81-9DAE-5A5EB3CA331D

P478

Q32057541-F49C86F7-C4FF-4D43-8A60-AE0E8C68C91E

P577

Q32057541-112B42A2-B278-42E7-862E-A279B0E26C20

P5875

Q32057541-195CB13F-1D24-4F8D-9290-152C1B51DB4F

P698

Q32057541-03134108-020D-48C9-BCEE-3155D5E4E8B9

P932

Q32057541-6DC6213C-DCAA-4DA2-A60F-C19B48900894

P356

PNAS.95.14.8034

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Myosin conformational states determined by single fluorophore polarization

@en

P2093

A M Lauzon

http://www.w3.org/2001/XMLSchema#string

C Berger

http://www.w3.org/2001/XMLSchema#string

D Gaffney

http://www.w3.org/2001/XMLSchema#string

D M Warshaw

http://www.w3.org/2001/XMLSchema#string

E Hayes

http://www.w3.org/2001/XMLSchema#string

G Kennedy

http://www.w3.org/2001/XMLSchema#string

J Wu

http://www.w3.org/2001/XMLSchema#string

K Trybus

http://www.w3.org/2001/XMLSchema#string

S Lowey

http://www.w3.org/2001/XMLSchema#string

P2860

Three-dimensional structure of myosin subfragment-1: a molecular motor

The mechanism of muscular contraction

Structure of the actin-myosin complex and its implications for muscle contraction

Mechanism of adenosine triphosphate hydrolysis by actomyosin

Smooth muscle and skeletal muscle myosins produce similar unitary forces and displacements in the laser trap

Rotational dynamics of actin-bound intermediates of the myosin adenosine triphosphatase cycle in myofibrils.

Fluorescence polarization of skeletal muscle fibers labeled with rhodamine isomers on the myosin heavy chain.

Cross-bridge model of muscle contraction. Quantitative analysis.

Probing individual molecules with confocal fluorescence microscopy.

A large and distinct rotation of the myosin light chain domain occurs upon muscle contraction.

P304

8034-8039

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1073/PNAS.95.14.8034

http://www.w3.org/2001/XMLSchema#string

P407

P433

14

http://www.w3.org/2001/XMLSchema#string

P478

95

http://www.w3.org/2001/XMLSchema#string

P577

1998-07-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

13631920

http://www.w3.org/2001/XMLSchema#string

P698

9653135

http://www.w3.org/2001/XMLSchema#string

P932

20924

http://www.w3.org/2001/XMLSchema#string