Fitting two- and three-site binding models to isothermal titration calorimetric data.
about
Disrupting the allosteric interaction between the Plasmodium falciparum cAMP-dependent kinase and its regulatory subunitDocking and molecular dynamics simulations of the Fyn-SH3 domain with free and phospholipid bilayer-associated 18.5-kDa myelin basic protein (MBP)-Insights into a noncanonical and fuzzy interaction.On the acquisition and analysis of microscale thermophoresis data.Integration and global analysis of isothermal titration calorimetry data for studying macromolecular interactions.SEDPHAT--a platform for global ITC analysis and global multi-method analysis of molecular interactions.Nuclear Magnetic Resonance Structural Mapping Reveals Promiscuous Interactions between Clathrin-Box Motif Sequences and the N-Terminal Domain of the Clathrin Heavy Chain.Use of fluorescence-detected sedimentation velocity to study high-affinity protein interactions.Applications of isothermal titration calorimetry - the research and technical developments from 2011 to 2015.High-precision, automated integration of multiple isothermal titration calorimetric thermograms: new features of NITPICNa/K-ATPase as a target for anticancer metal based drugs: insights into molecular interactions with selected gold(iii) complexes.Crystal structure of the spliceosomal DEAH-box ATPase Prp2.Thermal Activity in Affinity Separation Techniques Such as Liquid-Liquid Extraction Analyzed by Isothermal Titration Calorimetry and Accuracy Analysis of the Technique in the Molar Concentration DomainG-Quadruplex-Forming DNA Aptamers Inhibit the DNA-Binding Function of HupB and Mycobacteriumtuberculosis Entry into Host Cells
P2860
Q27728470-66D7085C-E380-4981-BAB1-803542DCBC26Q30008752-BE439E26-F326-41F0-BE9E-38383726BC09Q31035661-18866672-7CB6-4684-94E2-9479B6DAD379Q31071302-B7BD03B8-E87C-445F-8DD5-9313679942CFQ35236150-6B8770DE-A9C0-47DB-BC57-989FD8892C17Q35600686-1825DD42-9237-4D6E-95B1-26C8271DE724Q38644638-CC8B989A-A2CB-4FEC-8271-C716082D88C7Q38843472-E7251B76-565D-4801-BA57-4DB50E8C6978Q41669619-6F90B14C-4089-4884-A24C-3EAA90E46FADQ48258073-023F4501-C864-44A4-BC02-52DFCC2E8261Q55546975-2D3AAD74-4978-442B-8F01-90D037617075Q57073268-66F13FEC-05B2-4781-BEBD-627461ED6061Q58717959-E7F8367F-1262-4A6F-BCFB-868210137824
P2860
Fitting two- and three-site binding models to isothermal titration calorimetric data.
description
2014 nî lūn-bûn
@nan
2014 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
name
Fitting two- and three-site binding models to isothermal titration calorimetric data.
@ast
Fitting two- and three-site binding models to isothermal titration calorimetric data.
@en
type
label
Fitting two- and three-site binding models to isothermal titration calorimetric data.
@ast
Fitting two- and three-site binding models to isothermal titration calorimetric data.
@en
prefLabel
Fitting two- and three-site binding models to isothermal titration calorimetric data.
@ast
Fitting two- and three-site binding models to isothermal titration calorimetric data.
@en
P2860
P1433
P1476
Fitting two- and three-site binding models to isothermal titration calorimetric data.
@en
P2860
P304
P356
10.1016/J.YMETH.2014.11.018
P577
2014-12-05T00:00:00Z