| Year |
Citation |
Score |
| 2023 |
Dixit A, Chakraborty A, Nath JR, Chowdhury PK, Kundu B. Ocular protein optineurin shows reversibility from unfolded states and exhibits chaperone-like activity. Rsc Advances. 13: 6827-6837. PMID 36865578 DOI: 10.1039/d2ra07931c |
0.373 |
|
| 2022 |
Admane N, Srivastava A, Jamal S, Sharma R, Kundu B, Grover A. Molecular insights into the critical role of gallate moiety of green tea catechins in modulating prion fibrillation, cellular internalization, and neuronal toxicity. International Journal of Biological Macromolecules. PMID 36368361 DOI: 10.1016/j.ijbiomac.2022.11.049 |
0.339 |
|
| 2022 |
Sharma R, Kumari A, Kundu B, Grover A. Amyloid fibrillation of the glaucoma associated myocilin protein is inhibited by epicatechin gallate (ECG). Rsc Advances. 12: 29469-29481. PMID 36320765 DOI: 10.1039/d2ra05061g |
0.331 |
|
| 2020 |
Sharma P, Tomar R, Yadav SS, Badmalia MD, Nath SK, Ashish, Kundu B. Heat induces end to end repetitive association in P. furiosus L-asparaginase which enables its thermophilic property. Scientific Reports. 10: 21702. PMID 33303914 DOI: 10.1038/s41598-020-78877-z |
0.333 |
|
| 2020 |
Jena R, Garg DK, Achary MMV, Singh J, Tomar R, Choudhury L, Bansal R, Kundu B. Application of a protein domain as chaperone for enhancing biological activity and stability of other proteins. Journal of Biotechnology. PMID 32014561 DOI: 10.1016/J.Jbiotec.2020.01.017 |
0.752 |
|
| 2020 |
Pradhan P, Srivastava A, Singh J, Biswas B, Saini A, Siddique I, Kumari P, Khan MA, Mishra A, Yadav PK, Kumar S, Bhavesh NS, Venkatraman P, Vivekanandan P, Kundu B. Prion protein transcription is auto-regulated through dynamic interactions with G-quadruplex motifs in its own promoter. Biochimica Et Biophysica Acta. Gene Regulatory Mechanisms. 194479. PMID 31931179 DOI: 10.1016/J.Bbagrm.2019.194479 |
0.388 |
|
| 2019 |
Admane N, Srivastava A, Jamal S, Kundu B, Grover A. Protective effects of a neurohypophyseal hormone analogue on prion aggregation, cellular internalization and toxicity. Acs Chemical Neuroscience. PMID 31407881 DOI: 10.1021/Acschemneuro.9B00299 |
0.448 |
|
| 2019 |
Rajput R, G L B, Srivastava A, Wahi D, Shrivastava N, Kundu B, Grover A. Specific Keratinase Derived Designer Peptides Potently Inhibit A Aggregation Resulting in Reduced Neuronal Toxicity and Apoptosis. The Biochemical Journal. PMID 31138770 DOI: 10.1042/Bcj20190183 |
0.426 |
|
| 2019 |
Kant K, Tomar AK, Sharma P, Kundu B, Singh S, Yadav S. Human epididymis protein 4 quantification and interaction network analysis in seminal plasma. Protein and Peptide Letters. PMID 30919767 DOI: 10.2174/0929866526666190327124919 |
0.39 |
|
| 2018 |
Kumar V, Wahiduzzaman, Prakash A, Tomar AK, Srivastava A, Kundu B, Lynn AM, Imtaiyaz Hassan M. Exploring the Aggregation-prone regions from structural domains of. Human TDP-43. Biochimica Et Biophysica Acta. Proteins and Proteomics. PMID 30315897 DOI: 10.1016/J.Bbapap.2018.10.008 |
0.483 |
|
| 2018 |
Kataria A, Singh J, Kundu B. Identification and validation of l-asparaginase as a potential metabolic target against Mycobacterium tuberculosis. Journal of Cellular Biochemistry. PMID 30230585 DOI: 10.1002/Jcb.27169 |
0.329 |
|
| 2018 |
Srivastava A, Singh J, Singh Yadav SP, Arya P, Kalim F, Rose P, Ashish, Kundu B. The Gelsolin Pathogenic D187N Mutant Exhibits Altered Conformational Stability and Forms Amyloidogenic Oligomers. Biochemistry. PMID 29637772 DOI: 10.1021/Acs.Biochem.8B00039 |
0.469 |
|
| 2018 |
Sachdev R, Kappes-Horn K, Paulsen L, Duernberger Y, Pleschka C, Denner P, Kundu B, Reimann J, Vorberg I. Endoplasmic Reticulum Stress Induces Myostatin High Molecular Weight Aggregates and Impairs Mature Myostatin Secretion. Molecular Neurobiology. PMID 29546591 DOI: 10.1007/S12035-018-0997-9 |
0.308 |
|
| 2017 |
Jena R, Garg DK, Choudhury L, Saini A, Kundu B. Heterologous expression of an engineered protein domain acts as chaperone and enhances thermotolerance of Escherichia coli. International Journal of Biological Macromolecules. PMID 29042276 DOI: 10.1016/J.Ijbiomac.2017.10.081 |
0.721 |
|
| 2017 |
Sharma P, Tomar AK, Kundu B. Interplay between CedA, rpoB and double stranded DNA: A step towards understanding CedA mediated cell division in E. coli. International Journal of Biological Macromolecules. PMID 29037875 DOI: 10.1016/J.Ijbiomac.2017.10.075 |
0.302 |
|
| 2017 |
Singh J, Khan MI, Singh Yadav SP, Srivastava A, Sinha KK, Ashish, Das P, Kundu B. L-Asparaginase of Leishmania donovani: Metabolic target and its role in Amphotericin B resistance. International Journal For Parasitology. Drugs and Drug Resistance. 7: 337-349. PMID 28988014 DOI: 10.1016/J.Ijpddr.2017.09.003 |
0.333 |
|
| 2017 |
Tiwari N, Srivastava A, Kundu B, Munde M. Biophysical insight into the heparin-peptide interaction and its modulation by a small molecule. Journal of Molecular Recognition : Jmr. PMID 28961341 DOI: 10.1002/Jmr.2674 |
0.336 |
|
| 2017 |
Sharma P, Tomar AK, Kundu B. Identification of functional interactome of a key cell division regulatory protein CedA of E.coli. International Journal of Biological Macromolecules. PMID 28818726 DOI: 10.1016/J.Ijbiomac.2017.08.073 |
0.375 |
|
| 2017 |
Garg DK, Kundu B. Hyperthermophilic L-asparaginase bypasses monomeric intermediates during folding to retain cooperativity and avoid amyloid assembly. Archives of Biochemistry and Biophysics. PMID 28461187 DOI: 10.1016/J.Abb.2017.04.010 |
0.756 |
|
| 2017 |
Gautam S, Karmakar S, Batra R, Sharma P, Pradhan P, Singh J, Kundu B, Chowdhury PK. Polyphenols in combination with β-cyclodextrin can inhibit and disaggregate α-synuclein amyloids under cell mimicking conditions: A promising therapeutic alternative. Biochimica Et Biophysica Acta. PMID 28238838 DOI: 10.1016/J.Bbapap.2017.02.014 |
0.38 |
|
| 2017 |
Singh J, Srivastava A, Sharma P, Pradhan P, Kundu B. DNA intercalators as amyloid assembly modulators: mechanistic insights Rsc Advances. 7: 493-506. DOI: 10.1039/C6Ra26313E |
0.419 |
|
| 2016 |
Srivastava A, Sharma S, Sadanandan S, Gupta S, Singh J, Gupta S, Haridas V, Kundu B. Modulation of prion polymerization and toxicity by rationally designed peptidomimetics. The Biochemical Journal. PMID 27803245 DOI: 10.1042/Bcj20160737 |
0.493 |
|
| 2016 |
Garg DK, Kundu B. Clues for divergent, polymorphic amyloidogenesis through dissection of amyloid forming steps of bovine carbonic anhydrase and its critical amyloid forming stretch. Biochimica Et Biophysica Acta. 1864: 794-804. PMID 27045222 DOI: 10.1016/J.Bbapap.2016.03.019 |
0.737 |
|
| 2016 |
Tomar R, Sharma P, Srivastava A, Bansal S, Kundu B. Structural and functional insights into an archaeal L-asparaginase obtained through the linker-less assembly of constituent domains. Corrigendum. Acta Crystallographica. Section D, Structural Biology. 72: 180. PMID 26901530 DOI: 10.1107/S205979831502361X |
0.321 |
|
| 2015 |
Srivastava A, Arya P, Goel S, Kundu B, Mishra P, Fnu A. Gelsolin Amyloidogenesis Is Effectively Modulated by Curcumin and Emetine Conjugated PLGA Nanoparticles. Plos One. 10: e0127011. PMID 25996685 DOI: 10.1371/Journal.Pone.0127011 |
0.369 |
|
| 2015 |
Mahanta S, Paul S, Srivastava A, Pastor A, Kundu B, Chaudhuri TK. Stable self-assembled nanostructured hen egg white lysozyme exhibits strong anti-proliferative activity against breast cancer cells. Colloids and Surfaces. B, Biointerfaces. 130: 237-45. PMID 25935265 DOI: 10.1016/J.Colsurfb.2015.04.017 |
0.322 |
|
| 2015 |
Singh J, Srivastava A, Jha P, Sinha KK, Kundu B. l-Asparaginase as a new molecular target against leishmaniasis: insights into the mechanism of action and structure-based inhibitor design. Molecular Biosystems. 11: 1887-96. PMID 25893895 DOI: 10.1039/C5Mb00251F |
0.355 |
|
| 2015 |
Garg DK, Tomar R, Dhoke RR, Srivastava A, Kundu B. Domains of Pyrococcus furiosus L-asparaginase fold sequentially and assemble through strong intersubunit associative forces. Extremophiles : Life Under Extreme Conditions. 19: 681-91. PMID 25862541 DOI: 10.1007/S00792-015-0748-Z |
0.741 |
|
| 2015 |
Bhatia NK, Srivastava A, Katyal N, Jain N, Khan MA, Kundu B, Deep S. Curcumin binds to the pre-fibrillar aggregates of Cu/Zn superoxide dismutase (SOD1) and alters its amyloidogenic pathway resulting in reduced cytotoxicity. Biochimica Et Biophysica Acta. 1854: 426-36. PMID 25666897 DOI: 10.1016/J.Bbapap.2015.01.014 |
0.401 |
|
| 2014 |
Tomar R, Sharma P, Srivastava A, Bansal S, Kundu B. Structural and functional insights into an archaeal L-asparaginase obtained through the linker-less assembly of constituent domains. Acta Crystallographica. Section D, Biological Crystallography. 70: 3187-97. PMID 25478837 DOI: 10.1107/S1399004714023414 |
0.342 |
|
| 2014 |
Arya P, Srivastava A, Vasaikar SV, Mukherjee G, Mishra P, Kundu B. Selective interception of gelsolin amyloidogenic stretch results in conformationally distinct aggregates with reduced toxicity. Acs Chemical Neuroscience. 5: 982-92. PMID 25118567 DOI: 10.1021/Cn500002V |
0.497 |
|
| 2013 |
Kong Q, Mills JL, Kundu B, Li X, Qing L, Surewicz K, Cali I, Huang S, Zheng M, Swietnicki W, Sönnichsen FD, Gambetti P, Surewicz WK. Thermodynamic stabilization of the folded domain of prion protein inhibits prion infection in vivo. Cell Reports. 4: 248-54. PMID 23871665 DOI: 10.1016/J.Celrep.2013.06.030 |
0.453 |
|
| 2013 |
Tomar R, Garg DK, Mishra R, Thakur AK, Kundu B. N-terminal domain of Pyrococcus furiosus l-asparaginase functions as a non-specific, stable, molecular chaperone. The Febs Journal. 280: 2688-99. PMID 23551356 DOI: 10.1111/Febs.12271 |
0.766 |
|
| 2012 |
Bansal S, Srivastava A, Mukherjee G, Pandey R, Verma AK, Mishra P, Kundu B. Hyperthermophilic asparaginase mutants with enhanced substrate affinity and antineoplastic activity: structural insights on their mechanism of action. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 26: 1161-71. PMID 22166247 DOI: 10.1096/Fj.11-191254 |
0.371 |
|
| 2010 |
Bansal S, Gnaneswari D, Mishra P, Kundu B. Structural stability and functional analysis of L-asparaginase from Pyrococcus furiosus. Biochemistry. Biokhimiií¡A. 75: 375-81. PMID 20370616 DOI: 10.1134/S0006297910030144 |
0.405 |
|
| 2008 |
Rana A, Gupta TP, Bansal S, Kundu B. Formation of amyloid fibrils by bovine carbonic anhydrase. Biochimica Et Biophysica Acta. 1784: 930-5. PMID 18395531 DOI: 10.1016/J.Bbapap.2008.02.020 |
0.507 |
|
| 2007 |
Basu S, Mohan ML, Luo X, Kundu B, Kong Q, Singh N. Modulation of proteinase K-resistant prion protein in cells and infectious brain homogenate by redox iron: implications for prion replication and disease pathogenesis. Molecular Biology of the Cell. 18: 3302-12. PMID 17567949 DOI: 10.1091/Mbc.E07-04-0317 |
0.304 |
|
| 2005 |
Grover A, Dugar D, Kundu B. Predicting alternate structure attainment and amyloidogenesis: a nonlinear signal analysis approach. Biochemical and Biophysical Research Communications. 338: 1410-6. PMID 16263079 DOI: 10.1016/J.Bbrc.2005.10.104 |
0.367 |
|
| 2004 |
Kundu B, Shukla A, Chaba R, Guptasarma P. The excised heat-shock domain of alphaB crystallin is a folded, proteolytically susceptible trimer with significant surface hydrophobicity and a tendency to self-aggregate upon heating. Protein Expression and Purification. 36: 263-71. PMID 15249049 DOI: 10.1016/J.Pep.2004.04.001 |
0.488 |
|
| 2003 |
Kundu B, Maiti NR, Jones EM, Surewicz KA, Vanik DL, Surewicz WK. Nucleation-dependent conformational conversion of the Y145Stop variant of human prion protein: structural clues for prion propagation. Proceedings of the National Academy of Sciences of the United States of America. 100: 12069-74. PMID 14519851 DOI: 10.1073/Pnas.2033281100 |
0.47 |
|
| 2003 |
Kundu B, Shukla A, Guptasarma P. Peptide scanning-based identification of regions of gamma-II crystallin involved in thermal aggregation: evidence of the involvement of structurally analogous, helix-containing loops from the two double Greek key domains of the molecule. Archives of Biochemistry and Biophysics. 410: 69-75. PMID 12559977 DOI: 10.1016/S0003-9861(02)00676-8 |
0.496 |
|
| 2002 |
Kundu B, Guptasarma P. Use of a hydrophobic dye to indirectly probe the structural organization and conformational plasticity of molecules in amorphous aggregates of carbonic anhydrase. Biochemical and Biophysical Research Communications. 293: 572-7. PMID 12054640 DOI: 10.1016/S0006-291X(02)00257-7 |
0.513 |
|
| 2002 |
Kundu B, Shukla A, Guptasarma P. Manipulation of unfolding-induced protein aggregation by peptides selected for aggregate-binding ability through phage display library screening. Biochemical and Biophysical Research Communications. 291: 903-7. PMID 11866450 DOI: 10.1006/Bbrc.2002.6549 |
0.444 |
|
| 1999 |
Kundu B, Guptasarma P. Hydrophobic dye inhibits aggregation of molten carbonic anhydrase during thermal unfolding and refolding. Proteins. 37: 321-4. PMID 10591093 DOI: 10.1002/(Sici)1097-0134(19991115)37:3<321::Aid-Prot1>3.0.Co;2-L |
0.461 |
|
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