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Chittaranjan Das - Publications

Affiliations: 
Chemistry Purdue University, West Lafayette, IN, United States 
Area:
Biochemistry
Website:
https://www.chem.purdue.edu/das/people.php
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52 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2021 Iyer S, Das C. The unity of opposites: Strategic interplay between bacterial effectors to regulate cellular homeostasis. The Journal of Biological Chemistry. 101340. PMID 34695417 DOI: 10.1016/j.jbc.2021.101340  0.734
2021 Shrestha R, Das C. Crystal structure of the Thr316Ala mutant of a yeast JAMM deubiquitinase: implication of active-site loop dynamics in catalysis. Acta Crystallographica. Section F, Structural Biology Communications. 77: 163-170. PMID 34100774 DOI: 10.1107/S2053230X21005124  0.83
2021 Puvar K, Das C. Acquisition of a Mysterious New Domain Modulates the Function of a Bacterial Effector. Biochemistry. PMID 33620203 DOI: 10.1021/acs.biochem.1c00069  0.775
2021 Sheedlo MJ, Kenny S, Podkorytov IS, Brown K, Ma J, Iyer S, Hewitt CS, Arbough T, Mikhailovskii O, Flaherty DP, Wilson MA, Skrynnikov NR, Das C. Insights into Ubiquitin Product Release in Hydrolysis Catalyzed by the Bacterial Deubiquitinase SdeA. Biochemistry. PMID 33583181 DOI: 10.1021/acs.biochem.0c00760  0.823
2020 Hewitt CS, Krabill AD, Das C, Flaherty DP. Development of Ubiquitin Variants with Selectivity for Ubiquitin C-Terminal Hydrolase Deubiquitinases. Biochemistry. PMID 32865982 DOI: 10.1021/Acs.Biochem.9B01076  0.463
2020 Puvar K, Iyer S, Fu J, Kenny S, Negrón Terón KI, Luo ZQ, Brzovic PS, Klevit RE, Das C. Legionella effector MavC targets the Ube2N~Ub conjugate for noncanonical ubiquitination. Nature Communications. 11: 2365. PMID 32398758 DOI: 10.1038/S41467-020-16211-X  0.826
2020 Hausman JM, Kenny S, Iyer S, Babar A, Qiu J, Fu J, Luo ZQ, Das C. The Two Deubiquitinating Enzymes from Have Distinct Ubiquitin Recognition Properties. Biochemistry. PMID 32275137 DOI: 10.1021/Acs.Biochem.9B01107  0.815
2020 Puvar K, Saleh AM, Curtis R, Zhou Y, Nyalapatla PR, Fu J, Rovira AR, Tor Y, Luo ZQ, Ghosh AK, Wirth MJ, Chmielewski J, Kinzer-Ursem TL, Das C. Fluorescent Probes for Monitoring Serine Ubiquitination. Biochemistry. PMID 32207972 DOI: 10.1021/Acs.Biochem.0C00067  0.821
2019 Gan N, Guan H, Huang Y, Yu T, Fu J, Nakayasu ES, Puvar K, Das C, Wang D, Ouyang S, Luo ZQ. Legionella pneumophila regulates the activity of UBE2N by deamidase-mediated deubiquitination. The Embo Journal. e102806. PMID 31825121 DOI: 10.15252/Embj.2019102806  0.826
2019 Krabill AD, Chen H, Hussain S, Feng C, Abdullah A, Das C, Aryal UK, Post CB, Wendt MK, Galardy PJ, Flaherty DP. Biochemical and cellular characterization of a cyanopyrrolidine covalent Ubiquitin C-terminal hydrolase L1 inhibitor. Chembiochem : a European Journal of Chemical Biology. PMID 31449350 DOI: 10.1002/Cbic.201900434  0.328
2019 Gan N, Zhen X, Liu Y, Xu X, He C, Qiu J, Liu Y, Fujimoto GM, Nakayasu ES, Zhou B, Zhao L, Puvar K, Das C, Ouyang S, Luo ZQ. Regulation of phosphoribosyl ubiquitination by a calmodulin-dependent glutamylase. Nature. PMID 31330531 DOI: 10.2210/Pdb6K4L/Pdb  0.813
2019 Puvar K, Iyer S, Sheedlo MJ, Das C. Purification and functional characterization of the DUB domain of SdeA. Methods in Enzymology. 618: 343-355. PMID 30850059 DOI: 10.1016/Bs.Mie.2018.12.024  0.8
2018 Puvar K, Luo ZQ, Das C. Uncovering the Structural Basis of a New Twist in Protein Ubiquitination. Trends in Biochemical Sciences. PMID 30583962 DOI: 10.1016/J.Tibs.2018.11.006  0.827
2018 Ha L, Colquhoun J, Noinaj N, Das C, Dunman PM, Flaherty DP. Crystal structure of the ribonuclease-P-protein subunit from Staphylococcus aureus. Acta Crystallographica. Section F, Structural Biology Communications. 74: 632-637. PMID 30279314 DOI: 10.1107/S2053230X18011512  0.403
2017 Scarborough NM, Godaliyadda GMDP, Ye DH, Kissick DJ, Zhang S, Newman JA, Sheedlo MJ, Chowdhury A, Fischetti RF, Das C, Buzzard GT, Bouman CA, Simpson GJ. Synchrotron X-Ray Diffraction Dynamic Sampling for Protein Crystal Centering. Is&T International Symposium On Electronic Imaging. 2017: 6-9. PMID 29527589 DOI: 10.2352/Issn.2470-1173.2017.17.Coimg-415  0.745
2017 Puvar K, Zhou Y, Qiu J, Luo ZQ, Wirth MJ, Das C. Ubiquitin chains modified by the bacterial ligase SdeA are protected from DUB hydrolysis. Biochemistry. PMID 28809541 DOI: 10.1021/Acs.Biochem.7B00664  0.816
2017 Qiu J, Yu K, Fei X, Liu Y, Nakayasu ES, Piehowski PD, Shaw JB, Puvar K, Das C, Liu X, Luo ZQ. A unique deubiquitinase that deconjugates phosphoribosyl-linked protein ubiquitination. Cell Research. PMID 28497808 DOI: 10.1038/Cr.2017.66  0.834
2017 Scarborough NM, Godaliyadda GM, Ye DH, Kissick DJ, Zhang S, Newman JA, Sheedlo MJ, Chowdhury AU, Fischetti RF, Das C, Buzzard GT, Bouman CA, Simpson GJ. Dynamic X-ray diffraction sampling for protein crystal positioning. Journal of Synchrotron Radiation. 24: 188-195. PMID 28009558 DOI: 10.1107/S160057751601612X  0.741
2016 Nepal M, Sheedlo MJ, Das C, Chmielewski J. Accessing Three-Dimensional Crystals with Incorporated Guests through Metal-Directed Coiled-Coil Peptide Assembly. Journal of the American Chemical Society. PMID 27500907 DOI: 10.1021/Jacs.6B06708  0.733
2016 Newman JA, Zhang S, Sullivan SZ, Dow XY, Becker M, Sheedlo MJ, Stepanov S, Carlsen MS, Everly RM, Das C, Fischetti RF, Simpson GJ. Guiding synchrotron X-ray diffraction by multimodal video-rate protein crystal imaging. Journal of Synchrotron Radiation. 23: 959-965. PMID 27359145 DOI: 10.1107/S1600577516005919  0.732
2016 Qiu J, Sheedlo MJ, Yu K, Tan Y, Nakayasu ES, Das C, Liu X, Luo ZQ. Ubiquitination independent of E1 and E2 enzymes by bacterial effectors. Nature. PMID 27049943 DOI: 10.1038/Nature17657  0.809
2015 Sheedlo MJ, Qiu J, Tan Y, Paul LN, Luo ZQ, Das C. Structural basis of substrate recognition by a bacterial deubiquitinase important for dynamics of phagosome ubiquitination. Proceedings of the National Academy of Sciences of the United States of America. PMID 26598703 DOI: 10.1073/Pnas.1514568112  0.811
2015 Bueno AN, Shrestha RK, Ronau JA, Babar A, Sheedlo MJ, Fuchs JE, Paul LN, Das C. Dynamics of an Active-Site Flap Contributes to Catalysis in a JAMM Family Metallo Deubiquitinase. Biochemistry. 54: 6038-51. PMID 26368668 DOI: 10.1021/Acs.Biochem.5B00631  0.796
2015 Newman JA, Scarborough NM, Pogranichniy NR, Shrestha RK, Closser RG, Das C, Simpson GJ. Intercalating dyes for enhanced contrast in second-harmonic generation imaging of protein crystals. Acta Crystallographica. Section D, Biological Crystallography. 71: 1471-7. PMID 26143918 DOI: 10.1107/S1399004715008287  0.779
2014 Ronau JA, Paul LN, Fuchs JE, Liedl KR, Abu-Omar MM, Das C. A conserved acidic residue in phenylalanine hydroxylase contributes to cofactor affinity and catalysis. Biochemistry. 53: 6834-48. PMID 25295853 DOI: 10.1021/Bi500734H  0.801
2014 Shrestha RK, Ronau JA, Davies CW, Guenette RG, Strieter ER, Paul LN, Das C. Insights into the mechanism of deubiquitination by JAMM deubiquitinases from cocrystal structures of the enzyme with the substrate and product. Biochemistry. 53: 3199-217. PMID 24787148 DOI: 10.1021/Bi5003162  0.815
2013 Davies CW, Paul LN, Das C. Mechanism of recruitment and activation of the endosome-associated deubiquitinase AMSH. Biochemistry. 52: 7818-29. PMID 24151880 DOI: 10.1021/Bi401106B  0.71
2013 Ronau JA, Paul LN, Fuchs JE, Corn IR, Wagner KT, Liedl KR, Abu-Omar MM, Das C. An additional substrate binding site in a bacterial phenylalanine hydroxylase. European Biophysics Journal : Ebj. 42: 691-708. PMID 23860686 DOI: 10.1007/S00249-013-0919-8  0.81
2013 Madden JT, Toth SJ, Dettmar CM, Newman JA, Oglesbee RA, Hedderich HG, Everly RM, Becker M, Ronau JA, Buchanan SK, Cherezov V, Morrow ME, Xu S, Ferguson D, Makarov O, ... Das C, et al. Integrated nonlinear optical imaging microscope for on-axis crystal detection and centering at a synchrotron beamline. Journal of Synchrotron Radiation. 20: 531-40. PMID 23765294 DOI: 10.1107/S0909049513007942  0.771
2013 Arnst JL, Davies CW, Raja SM, Das C, Natarajan A. High-throughput compatible fluorescence resonance energy transfer-based assay to identify small molecule inhibitors of AMSH deubiquitinase activity. Analytical Biochemistry. 440: 71-7. PMID 23747283 DOI: 10.1016/J.Ab.2013.05.017  0.612
2013 Davies CW, Das C. HHARI is one HECT of a RING. Structure (London, England : 1993). 21: 872-4. PMID 23747110 DOI: 10.1016/J.Str.2013.05.003  0.694
2013 Morrow ME, Kim MI, Ronau JA, Sheedlo MJ, White RR, Chaney J, Paul LN, Lill MA, Artavanis-Tsakonas K, Das C. Stabilization of an unusual salt bridge in ubiquitin by the extra C-terminal domain of the proteasome-associated deubiquitinase UCH37 as a mechanism of its exo specificity. Biochemistry. 52: 3564-78. PMID 23617878 DOI: 10.1021/Bi4003106  0.817
2013 Hussain S, Feldman AL, Das C, Ziesmer SC, Ansell SM, Galardy PJ. Ubiquitin hydrolase UCH-L1 destabilizes mTOR complex 1 by antagonizing DDB1-CUL4-mediated ubiquitination of raptor. Molecular and Cellular Biology. 33: 1188-97. PMID 23297343 DOI: 10.1128/Mcb.01389-12  0.332
2013 DeWalt EL, Begue VJ, Ronau JA, Sullivan SZ, Das C, Simpson GJ. Polarization-resolved second-harmonic generation microscopy as a method to visualize protein-crystal domains. Acta Crystallographica. Section D, Biological Crystallography. 69: 74-81. PMID 23275165 DOI: 10.1107/S0907444912042503  0.792
2012 Tsou WL, Sheedlo MJ, Morrow ME, Blount JR, McGregor KM, Das C, Todi SV. Systematic analysis of the physiological importance of deubiquitinating enzymes. Plos One. 7: e43112. PMID 22937016 DOI: 10.1371/Journal.Pone.0043112  0.81
2012 Davies CW, Chaney J, Korbel G, Ringe D, Petsko GA, Ploegh H, Das C. The co-crystal structure of ubiquitin carboxy-terminal hydrolase L1 (UCHL1) with a tripeptide fluoromethyl ketone (Z-VAE(OMe)-FMK). Bioorganic & Medicinal Chemistry Letters. 22: 3900-4. PMID 22617491 DOI: 10.1016/J.Bmcl.2012.04.124  0.806
2012 Boudreaux DA, Chaney J, Maiti TK, Das C. Contribution of active site glutamine to rate enhancement in ubiquitin C-terminal hydrolases. The Febs Journal. 279: 1106-18. PMID 22284438 DOI: 10.1111/J.1742-4658.2012.08507.X  0.661
2011 Maiti TK, Permaul M, Boudreaux DA, Mahanic C, Mauney S, Das C. Crystal structure of the catalytic domain of UCHL5, a proteasome-associated human deubiquitinating enzyme, reveals an unproductive form of the enzyme. The Febs Journal. 278: 4917-26. PMID 21995438 DOI: 10.1111/J.1742-4658.2011.08393.X  0.553
2011 Davies CW, Paul LN, Kim MI, Das C. Structural and thermodynamic comparison of the catalytic domain of AMSH and AMSH-LP: nearly identical fold but different stability. Journal of Molecular Biology. 413: 416-29. PMID 21888914 DOI: 10.1016/J.Jmb.2011.08.029  0.692
2010 Boudreaux DA, Maiti TK, Davies CW, Das C. Ubiquitin vinyl methyl ester binding orients the misaligned active site of the ubiquitin hydrolase UCHL1 into productive conformation. Proceedings of the National Academy of Sciences of the United States of America. 107: 9117-22. PMID 20439756 DOI: 10.1073/Pnas.0910870107  0.704
2006 Das C, Hoang QQ, Kreinbring CA, Luchansky SJ, Meray RK, Ray SS, Lansbury PT, Ringe D, Petsko GA. Structural basis for conformational plasticity of the Parkinson's disease-associated ubiquitin hydrolase UCH-L1. Proceedings of the National Academy of Sciences of the United States of America. 103: 4675-80. PMID 16537382 DOI: 10.1073/Pnas.0510403103  0.705
2005 Kornilova AY, Bihel F, Das C, Wolfe MS. The initial substrate-binding site of gamma-secretase is located on presenilin near the active site. Proceedings of the National Academy of Sciences of the United States of America. 102: 3230-5. PMID 15722417 DOI: 10.1073/Pnas.0407640102  0.39
2004 Bihel F, Das C, Bowman MJ, Wolfe MS. Discovery of a Subnanomolar helical D-tridecapeptide inhibitor of gamma-secretase. Journal of Medicinal Chemistry. 47: 3931-3. PMID 15267231 DOI: 10.1021/Jm049788C  0.327
2003 Das C, Berezovska O, Diehl TS, Genet C, Buldyrev I, Tsai JY, Hyman BT, Wolfe MS. Designed helical peptides inhibit an intramembrane protease. Journal of the American Chemical Society. 125: 11794-5. PMID 14505382 DOI: 10.1021/Ja037131V  0.433
2003 Aravinda S, Shamala N, Das C, Sriranjini A, Karle IL, Balaram P. Aromatic-aromatic interactions in crystal structures of helical peptide scaffolds containing projecting phenylalanine residues. Journal of the American Chemical Society. 125: 5308-15. PMID 12720442 DOI: 10.1021/Ja0341283  0.348
2003 Kornilova AY, Das C, Wolfe MS. Differential effects of inhibitors on the gamma-secretase complex. Mechanistic implications. The Journal of Biological Chemistry. 278: 16470-3. PMID 12644463 DOI: 10.1074/jbc.C300019200  0.303
2002 Aravinda S, Shamala N, Das C, Balaram P. Structural analysis of peptide helices containing centrally positioned lactic acid residues. Biopolymers. 64: 255-67. PMID 12115133 DOI: 10.1002/Bip.10192  0.31
2001 Karle IL, Das C, Balaram P. Effects of hydrogen-bond deletion on peptide helices: structural characterization of depsipeptides containing lactic acid. Biopolymers. 59: 276-89. PMID 11473352 DOI: 10.1002/1097-0282(20011005)59:4<276::Aid-Bip1024>3.0.Co;2-X  0.323
2001 Das C, Shankaramma SC, Balaram P. Molecular Carpentry: Piecing Together Helices and Hairpins in Designed Peptides Chemistry: a European Journal. 7: 840-847. PMID 11288876 DOI: 10.1002/1521-3765(20010216)7:4<840::Aid-Chem840>3.0.Co;2-M  0.327
2000 Aravinda S, Shamala N, Pramanik A, Das C, Balaram P. An unusual C-H...O hydrogen bond mediated reversal of polypeptide chain direction in a synthetic peptide helix. Biochemical and Biophysical Research Communications. 273: 933-936. PMID 10891350 DOI: 10.1006/Bbrc.2000.3026  0.307
2000 Karle IL, Das C, Balaram P. De novo protein design: crystallographic characterization of a synthetic peptide containing independent helical and hairpin domains. Proceedings of the National Academy of Sciences of the United States of America. 97: 3034-3037. DOI: 10.1073/Pnas.97.7.3034  0.345
1998 Das C, Raghothama S, Balaram P. A designed three stranded β-sheet peptide as a multiple β-hairpin model [4] Journal of the American Chemical Society. 120: 5812-5813. DOI: 10.1021/Ja973739Q  0.318
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