B. Bhattacharyya

发表

Multiphasic denaturation of the λ repressor by urea and its implications for the repressor structure

Siddhartha Roy, S. Roy, U. Banik, 1992 .

Antimicrotubular drugs binding to vinca domain of tubulin

B. Bhattacharyya, Suvroma Gupta, 2003, Molecular and Cellular Biochemistry.

Excimer fluorescence of pyrene-maleimide-labeled tubulin.

B. Bhattacharyya, D. Panda, 1992, European journal of biochemistry.

Structure and activity of lysozyme on binding to ZnO nanoparticles.

P. Chakrabarti, Vinay Gupta, Tanaya Chatterjee, 2010, Langmuir : the ACS journal of surfaces and colloids.

Promotion of fluorescence upon binding of colchicine to tubulin.

B. Bhattacharyya, J. Wolff, 1974, Proceedings of the National Academy of Sciences of the United States of America.

Thermodynamics of Colchicinoid-Tubulin Interactions

Gopal Chakrabarti, B. Bhattacharyya, S. Sengupta, 1996, The Journal of Biological Chemistry.

Interaction of Prodan with tubulin. A fluorescence spectroscopic study.

B. Bhattacharyya, M. Mazumdar, P. Parrack, 1992, European journal of biochemistry.

Kinetic and thermodynamic analysis of taxol-induced polymerization of purified tubulin.

B. Bhattacharyya, G. G. Choudhury, B. Biswas, 1987, Biochemistry and cell biology = Biochimie et biologie cellulaire.

Anti‐mitotic activity of colchicine and the structural basis for its interaction with tubulin

B. Bhattacharyya, D. Panda, Suvroma Gupta, 2008, Medicinal research reviews.

Interaction of colchicine analogues with purified tubulin

B. Bhattacharyya, G. G. Choudhury, G. G. Choudhury, 1983, FEBS letters.

Anion-induced increases in the affinity of colcemid binding to tubulin.

B. Bhattacharyya, B. Biswas, K. Ray, 1984, European journal of biochemistry.

B ring regulation of colchicine binding kinetics and fluorescence.

A. Brossi, B. Bhattacharyya, J. Wolff, 1986, Proceedings of the National Academy of Sciences of the United States of America.

Tubulin aggregation and disaggregation: mediation by two distinct vinblastine-binding sites.

B. Bhattacharyya, J. Wolff, 1976, Proceedings of the National Academy of Sciences of the United States of America.

Bis-ANS as a specific inhibitor for microtubule-associated protein induced assembly of tubulin.

B. Bhattacharyya, M. Mazumdar, P. Parrack, 1992, Biochemistry.

Discrimination of ligands with different flexibilities resulting from the plasticity of the binding site in tubulin.

P. Chakrabarti, Devlina Chakravarty, B. Bhattacharyya, 2012, Biochemistry.

Fluorescence spectroscopic methods to analyze drug-tubulin interactions.

B. Bhattacharyya, D. Panda, S. Kapoor, 2010, Methods in cell biology.

Podophyllotoxin as a probe for the colchicine binding site of tubulin.

B. Bhattacharyya, J. Wolff, F. Cortese, 1977, The Journal of biological chemistry.

Immobilization-dependent fluorescence of colchicine.

B. Bhattacharyya, J. Wolff, 1984, The Journal of biological chemistry.

Role of B-ring of colchicine in its binding to tubulin.

B. Bhattacharyya, A. Banerjee, S. Maity, 1981, Indian journal of biochemistry & biophysics.

Molecular biology of tubulin: Its interaction with drugs and genomic organization

B. Bhattacharyya, G. G. Choudhury, G. Ghosh Choudhury, 1984, Journal of Biosciences.

The natural naphthoquinone plumbagin exhibits antiproliferative activity and disrupts the microtubule network through tubulin binding.

Bipul R. Acharya, Gopal Chakrabarti, B. Bhattacharyya, 2008, Biochemistry.

Local unfolding and the stepwise loss of the functional properties of tubulin.

D. Sackett, B. Bhattacharyya, J. Wolff, 1994, Biochemistry.

Genistein arrests cell cycle progression of A549 cells at the G(2)/M phase and depolymerizes interphase microtubules through binding to a unique site of tubulin.

Bipul R. Acharya, Gopal Chakrabarti, B. Bhattacharyya, 2010, Biochemistry.

Colcemid and colchicine binding to tubulin

B. Bhattacharyya, A. Banerjee, 1979, FEBS letters.

Deuterium oxide stabilizes conformation of tubulin:a biophysical and biochemical study.

Bipul R. Acharya, Gopal Chakrabarti, B. Bhattacharyya, 2008, BMB reports.

Interaction of a fluorescent analog of N-deacetyl-N-methyl-colchicine (colcemid) with liver alcohol dehydrogenase.

S. Roy, B. Bhattacharyya, S. Sengupta, 1995, European journal of biochemistry.

MICROTUBULES AND THYROID HORMONE MOBILIZATION

B. Bhattacharyya, J. Wolff, 1975, Annals of the New York Academy of Sciences.

Tubulin and the microtubule system in cellular growth and development.

A. Banerjee, B. Bhattacharyya, B. Biswas, 1981, Sub-cellular biochemistry.

anti-Mitotic Activity of Colchicine and the Structural Basis for Its Interaction with Tubulin

B. Bhattacharyya, D. Panda, Suvroma Gupta, 2008 .

Role of the C-terminal tail region in the self-assembly of lambda-repressor.

S. Roy, U. Banik, N. C. Mandal, 1995, Biochemistry.

The colchicine-binding and pyrene-excimer-formation activities of tubulin involve a common cysteine residue in the beta subunit.

B. Bhattacharyya, S. Chandra, P. Basusarkar, 1997, European journal of biochemistry.

Fluorescence energy transfer measurement of distances between ligand binding sites of tubulin and its implication for protein‐protein interaction

Siddhartha Roy, B. Bhattacharyya, A. Bhattacharya, 1996, Protein science : a publication of the Protein Society.

Antagonists of Hsp16.3, a Low-Molecular-Weight Mycobacterial Chaperone and Virulence Factor, Derived from Phage-Displayed Peptide Libraries

Siddhartha Roy, A. Saha, B. Bhattacharyya, 2005, Applied and Environmental Microbiology.

Maytansine binding to the vinblastine sites of tubulin

B. Bhattacharyya, J. Wolff, Vinblastine Maytansine, 1977, FEBS letters.

BisANS binding to tubulin: Isothermal titration calorimetry and the site‐specific proteolysis reveal the GTP‐induced structural stability of tubulin

B. Bhattacharyya, K. Das, Suvroma Gupta, 2002, Proteins.

Nucleotide-dependent bisANS binding to tubulin.

B. Bhattacharyya, S. Chakraborty, N. Sarkar, 1999, Biochimica et biophysica acta.

Chaperone-like activity of tubulin: Binding and reactivation of unfolded substrate enzymes

B. Bhattacharyya, K. Das, T. Manna, 2001 .

Role of the carboxy‐termini of tubulin on its chaperone‐like activity

Siddhartha Roy, S. Roy, B. Bhattacharyya, 2001, Proteins.

Zinc-induced self-assembly of goat brain tubulin: some novel aspects.

B. Bhattacharyya, A. Banerjee, S. Roychowdhury, 1982, Biochemical and biophysical research communications.

Charge effect on the colchicine binding-site of tubulin.

B. Bhattacharyya, A. Banerjee, S. Roychowdhuri, 1983, Biochemical and biophysical research communications.

Relative importance of inositol (1,4,5)trisphosphate and inositol (1,3,4,5)tetrakisphosphate in Entamoeba histolytica

B. Bhattacharyya, S. Raha, Banabihari Giri, 1996, FEBS letters.

Thyroid tubulin: purification and properties.

B. Bhattacharyya, J. Wolff, 1974, Biochemistry.

Membrane-bound tubulin in brain and thyroid tissue.

B. Bhattacharyya, J. Volff, 1975, The Journal of biological chemistry.

MAP2c prevents arachidonic acid-induced fibril formation of tau: Role of chaperone activity and phosphorylation.

Bhabatarak Bhattacharyya, Gopa Mitra, B. Bhattacharyya, 2015, Biophysical chemistry.

Interaction of mithramycin and chromomycin A3 with d(TAGCTAGCTA)2: Role of sugars in antibiotic-DNA recognition

B. Bhattacharyya, D. Dasgupta, S. Chakrabarti, 2002 .

Antimitotic sulfonamides inhibit microtubule assembly dynamics and cancer cell proliferation.

T. Owa, B. Bhattacharyya, D. Panda, 2006, Biochemistry.

Sulfonamide drugs binding to the colchicine site of tubulin: thermodynamic analysis of the drug-tubulin interactions by isothermal titration calorimetry.

T. Owa, A. Surolia, B. Bhattacharyya, 2005, Journal of medicinal chemistry.

Properties of B‐ring analogues of colchicine

B. Bhattacharyya, S. Maity, 1987, FEBS letters.

Oxalone and lactone moieties of podophyllotoxin exhibit properties of both the B and C rings of colchicine in its binding with tubulin.

B. Bhattacharyya, A. Datta, Suvroma Gupta, 2006, Biochemistry.

Inositol(1,3,4,5) tetrakisphosphate plays an important role in calcium mobilization from Entamoeba histolytica

B. Bhattacharyya, S. Raha, Banabihari Giri, 1995, FEBS letters.

Polymerisation of membrane tubulin

B. Bhattacharyya, J. Wolff, 1976, Nature.

The interaction of 1-anilino-8-naphthalene sulfonate with tubulin: a site independent of the colchicine-binding site.

B. Bhattacharyya, J. Wolff, 1975, Archives of biochemistry and biophysics.

Stable and potent analogues derived from the modification of the dicarbonyl moiety of curcumin.

P. Chakrabarti, A. Surolia, B. Bhattacharyya, 2013, Biochemistry.

Promotion of Tubulin Assembly by Carboxyterminal Charge Reduction

D. Sackett, B. Bhattacharyya, J. Wolff, 1986, Annals of the New York Academy of Sciences.

Chaperone-like Activity of Tubulin*

B Bhattacharyya, B. Bhattacharyya, K. Das, 1998, The Journal of Biological Chemistry.

Tubulin, hybrid dimers, and tubulin S. Stepwise charge reduction and polymerization.

D. Sackett, B. Bhattacharyya, J. Wolff, 1985, The Journal of biological chemistry.

Tubulin subunit carboxyl termini determine polymerization efficiency.

D. Sackett, B. Bhattacharyya, J. Wolff, 1985, The Journal of biological chemistry.

Lysozyme‐induced polymerization of tubulin

B. Bhattacharyya, A. Banerjee, A. Banerjee, 1981, FEBS letters.

-NH-dansyl isocolchicine exhibits a significantly improved tubulin-binding affinity and microtubule inhibition in comparison to isocolchicine by binding tubulin through its A and B rings.

B. Bhattacharyya, A. Datta, Suvroma Gupta, 2005, Biochemistry.

Colchicine binding activity of rat brain polysomes

B. Bhattacharyya, B. Biswas, K. Sen, 1983, Journal of Biosciences.

Stabilization of microtubules by lithium ion.

B. Bhattacharyya, J. Wolff, 1976, Biochemical and biophysical research communications.

Interaction of Ni2+ with the tubulin-microtubule system.

A. Banerjee, B. Bhattacharyya, S. Roychaudhury, 1982, Biochimica et biophysica acta.

Anion-induced increases in the rate of colchicine binding to tubulin.

B. Bhattacharyya, J. Wolff, 1976, Biochemistry.

Differential colchicine‐binding across eukaryotic families: The role of highly conserved Pro268β and Ala248β residues in animal tubulin

B. Bhattacharyya, D. Roy, G. Basu, 2007, FEBS letters.

MAP2 prevents protein aggregation and facilitates reactivation of unfolded enzymes.

B. Bhattacharyya, K. Das, D. Panda, 2004, European journal of biochemistry.

A study of energetics of cooperative interaction using a mutant λ-repressor

S. Roy, N. C. Mandal, B. Bhattacharyya, 2000 .

Chaperone-like Activity of Tubulin

B. Bhattacharyya, K. Das, T. Manna, 2001, The Journal of Biological Chemistry.

Sulfhydryls of tubulin

Sabita Roy, B. Bhattacharyya, S. Bhattacharyya, 2000 .

Sulfhydryls of tubulin. A probe to detect conformational changes of tubulin.

S. Roy, B. Bhattacharyya, S. Bhattacharyya, 2000, European journal of biochemistry.

Crocin, a carotenoid, suppresses spindle microtubule dynamics and activates the mitotic checkpoint by binding to tubulin

B. Bhattacharyya, D. Panda, S. Srivastava, 2019, Biochemical pharmacology.

Curcumin recognizes a unique binding site of tubulin.

P. Chakrabarti, A. Surolia, B. Bhattacharyya, 2011, Journal of medicinal chemistry.

Chaperone‐mediated inhibition of tubulin self‐assembly

A. Saha, B. Bhattacharyya, K. Das, 2007, Proteins.

Actin-curcumin interaction: insights into the mechanism of actin polymerization inhibition.

P. Chakrabarti, A. Surolia, Devlina Chakravarty, 2015, Biochemistry.

Colchicine binding to tubulin monomers: a mechanistic study.

B. Bhattacharyya, S. Banerjee, G. Chakrabarti, 1997, Biochemistry.

The B‐ring substituent at C‐7 of colchicine and the α‐C‐terminus of tubulin communicate through the “tail–body” interaction

B. Bhattacharyya, R. Solana, Suvroma Gupta, 2004, Proteins.

Refolding of urea-denatured tubulin: recovery of nativelike structure and colchicine binding activity from partly unfolded states.

B. Bhattacharyya, S. Guha, 1997, Biochemistry.

Tubulin conformation and dynamics: a red edge excitation shift study.

B. Bhattacharyya, A. Chattopadhyay, S. S. Rawat, 1996, Biochemistry.

Reversible dimer dissociation of tubulin S and tubulin detected by fluorescence anisotropy.

S. Roy, B. Bhattacharyya, D. Panda, 1992, Biochemistry.

Molecular dynamics simulation of colchicinoids.

C. Mukhopadhyay, B. Bhattacharyya, A. Bothra, 1998, Journal of biomolecular structure & dynamics.

N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)colcemid, a probe for different classes of colchicine-binding site on tubulin.

A. Surolia, Sabita Roy, S. Roy, 1993, European journal of biochemistry.

Biphasic kinetics of the colchicine-tubulin interaction: role of amino acids surrounding the A ring of bound colchicine molecule.

B. Bhattacharyya, D. Roy, Suvroma Gupta, 2005, Biochemistry.

Amino acid changes in the repressor of bacteriophage lambda due to temperature-sensitive mutations in its cI gene and the structure of a highly temperature-sensitive mutant repressor.

S. Roy, N. C. Mandal, B. Bhattacharyya, 1999, Protein engineering.

A partially folded intermediate during tubulin unfolding: its detection and spectroscopic characterization.

B. Bhattacharyya, S. Guha, 1995, Biochemistry.

Role of B-ring of colchicine in its binding to Zn(II)-induced tubulin-sheets

B. Bhattacharyya, A. Banerjee, S. Maity, 1987, Journal of Biosciences.

B‐ring of colchicine and its role in taxol‐induced tubulin polymerization

B. Bhattacharyya, S. Maity, B. B. Biswas, 1986, FEBS Letters.

A fluorescence anisotropy study of tetramer-dimer equilibrium of lambda repressor and its implication for function.

S. Roy, U. Banik, N. C. Mandal, 1993, The Journal of biological chemistry.

An operator-induced conformational change in the C-terminal domain of the lambda repressor.

S. Roy, U. Banik, R. Saha, 1992, The Journal of biological chemistry.

Fluorescence spectroscopic studies of proteins.

S. Roy, B. Bhattacharyya, 1995, Sub-cellular biochemistry.

Genistein arrests cell cycle progression of A549 cells at the G(2)/M phase and depolymerizes interphase microtubules through binding to a unique site of tubulin.

Bipul R. Acharya, Gopal Chakrabarti, B. Bhattacharyya, 2010, Biochemistry.

Stable and potent analogues derived from the modification of the dicarbonyl moiety of curcumin.

P. Chakrabarti, A. Surolia, B. Bhattacharyya, 2013, Biochemistry.

Structure and activity of lysozyme on binding to ZnO nanoparticles.

P. Chakrabarti, Vinay Gupta, Tanaya Chatterjee, 2010, Langmuir : the ACS journal of surfaces and colloids.

A study of colchicine tubulin complex by donor quenching of fluorescence energy transfer.

S. Roy, B. Bhattacharyya, A. Bhattacharyya, 1993, European journal of biochemistry.

Aging of tubulin monomers using 5,5'-bis(8-anilino-1-naphthalenesulfonate) as a probe.

B. Bhattacharyya, P. Parrack, K. Mukhopadhyay, 1995, Biochemistry.

Use of micelles in studying drug-binding sites: simulation of the tubulin-bound fluorescence of colchicine.

B. Bhattacharyya, D. Balasubramanian, J. Shobha, 1989, Journal of biochemical and biophysical methods.

Conformational properties of α-tubulin tail peptide: implications for tail-body interaction

D. Pal, P. Chakrabarti, A. Banerjee, 2001 .

Tubulin and its assembly promoting factor(s) during maturation of avian erythrocytes

B. Bhattacharyya, A. Banerjee, A. Banerjee, 1979, FEBS letters.