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In vitro effect of cryptophycin 52 on microtubule assembly and tubulin: molecular modeling of the mechanism of action of a new antimitotic drug.
TLDR
This report details the mechanism by which C52 substoichiometrically inhibits tubulin self-assembly into microtubules and shows that C52 induces tubulin to form ring-shaped oligomers (single rings) and inhibits the formation of double rings from either GTP- or GDP-tubulin. Expand
Tubulin binding of two 1-deaza-7,8-dihydropteridines with different biological properties: enantiomers NSC 613862 (S)-(-) and NSC 613863 (R)-(+).
TLDR
It is hypothesized that the R-isomer is positioned differently in its binding locus as compared with the S-isomers, which would explain the differences in fluorescence behavior after binding to tubulin. Expand
Study of the interaction between human serum albumin and some cephalosporins.
Dialysis and microcalorimetric methods were used to calculate the binding parameters of some cephalosporins to human serum albumin (HSA) and to study the nature of the interactions involved in theExpand
Differentiation of human colon cancer cells changes the expression of β-tubulin isotypes and MAPs
TLDR
The results indicate that the composition of microtubules should be considered as one of the criteria involved in the response of tumour cells to chemotherapy with anti-microtubule agents. Expand
Interaction of tubulin and cellular microtubules with the new antitumor drug MDL 27048. A powerful and reversible microtubule inhibitor.
TLDR
This anti-tumor drug constitutes a new and potent microtubule inhibitor, characterized by its specificity and reversibility. Expand
Mechanism of binding of the new antimitotic drug MDL 27048 to the colchicine site of tubulin: equilibrium studies.
TLDR
In contrast with close analogues of colchicine, MDL 27048 and podophyllotoxin neither affected the far-ultraviolet circular dichroism spectrum of tubulin, within experimental error, nor induced tubulin GTPase activity. Expand
Influence of time and chloride ions on the interaction of cisplatin with human albumin in‐vitro
TLDR
The interaction of cis‐dichlorodiammineplatinum (II) (cisplatin) with human serum albumin (HSA), dissolved in phosphate buffer with or without sodium chloride has been examined and it was shown that the lone SH‐group of the HSA macromolecule is involved in cisplatin binding. Expand
Microcalorimetric studies on the binding of some benzodiazepine derivatives to human serum albumin.
TLDR
A microcalorimetric method is employed to study the nature of the interactions between several benzodiazepin molecules and human serum albumin, demonstrating both electrostatic and hydrophobic interactions which vary according to the drug's molecular structure. Expand
Comparison of an iterative microcalorimetric method and dialysis equilibrium for calculating thermodynamic parameters of a binding protein which presents a weak affinity for its substrate.
TLDR
This iterative microcalorimetric method can be applied to all techniques involving the measurement of a phenomenon which is proportional to the concentration of the complex, and the partially competitive binding of dipotassium chlorazepate and 5-fluorouracil is shown. Expand
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