(Q51866230)

14 April 2018

title

Thermodynamics, conformation and active sites of the binding of Zn-Nd hetero-bimetallic Schiff base to bovine serum albumin. (English)

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14 April 2018

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Qi Xiao

1

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14 April 2018

Shan Huang

2

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14 April 2018

Yi Liu

3

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14 April 2018

Fang-fang Tian

4

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14 April 2018

Jun-cheng Zhu

5

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14 April 2018

publication date

21 October 2008

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14 April 2018

published in

Journal of Fluorescence

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14 April 2018

volume

19

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14 April 2018

issue

2

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14 April 2018

page(s)

317-326

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14 April 2018

https://scigraph.springernature.com/pub.10.1007/s10895-008-0418-y

exact match

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cites work

Investigation of Foscan interactions with plasma proteins.

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Thermodynamics of protein association reactions: forces contributing to stability

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Conformational transitions of the three recombinant domains of human serum albumin depending on pH

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Measuring the forces that control protein interactions

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Quenching of fluorescence by oxygen. Probe for structural fluctuations in macromolecules

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Interaction of Schiff base with bovine serum albumin: site-specific photocleavage

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Copper(II) Schiff base coordination compounds of dien with heterocyclic aldehydes and 2-amino-5-methyl-thiazole: synthesis, characterization, antiproliferative and antibacterial studies. Crystal structure of CudienOOCl2.

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Solute perturbation of protein fluorescence. Quenching of the tryptophyl fluorescence of model compounds and of lysozyme by iodide ion

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Fluorimetric analysis of the binding of warfarin to human serum albumin. Equilibrium and kinetic study

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Antibacterial Co(II), Cu(II), Ni(II) and Zn(II) complexes of thiadiazole derived furanyl, thiophenyl and pyrrolyl Schiff bases

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Conjugated polyene fatty acids as fluorescent probes: synthetic phospholipid membrane studies

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Biological activity of palladium(II) and platinum(II) complexes of the acetone Schiff bases of S-methyl- and S-benzyldithiocarbazate and the X-ray crystal structure of the [Pd(asme)2] (asme=anionic form of the acetone Schiff base of S-methyldithioca

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Location and characterization of the warfarin binding site of human serum albumin. A comparative study of two large fragments

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Interaction of wogonin with bovine serum albumin

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Spectroscopic characterization of arrestin interactions with competitive ligands: study of heparin and phytic acid binding

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Binding interaction of a biological photosensitizer with serum albumins: a biophysical study

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Interaction of copper(II) complex of compartmental Schiff base ligand N,N'-bis(3-hydroxysalicylidene)ethylenediamine with bovine serum albumin.

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Solvent perturbation of the fluorescence of fluorescein bound to specific antibody. Fluorescence quenching of the bound fluorophore by iodide

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Atomic structure and chemistry of human serum albumin

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Studies of the interaction between palmatine hydrochloride and human serum albumin by fluorescence quenching method

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Stereochemical aspects of benzodiazepine binding to human serum albumin. I. Enantioselective high performance liquid affinity chromatographic examination of chiral and achiral binding interactions between 1,4-benzodiazepines and human serum albumin

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Fluorescence study on the interaction of bovine serum albumin with p-aminoazobenzene

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Fluorescence Energy Transfer as a Spectroscopic Ruler

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A general, wide-rage spectrofluorometric method for measuring the site-specific affinities of drugs toward human serum albumin

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Species differences of serum albumins: I. Drug binding sites.

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Synthesis, characterization, cytotoxic activities, and DNA-binding properties of the La(III) complex with Naringenin Schiff-base

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Antibody responses to macrocycles in lymphoma

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Synthesis and crystal structure of some transition metal complexes with a novel bis-Schiff base ligand and their antitumor activities

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Derivatives of phosphate Schiff base transition metal complexes: synthesis, studies and biological activity

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12 December 2020

10.1007/S10895-008-0418-Y

Identifiers

DOI

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14 April 2018

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14 April 2018