Year |
Citation |
Score |
2023 |
Puneeth Kumar DR, Nalawade SA, Pahan S, Singh M, Senapati DK, Roy S, Dey S, Toraskar SU, Raghothama S, Gopi HN. Proteolytically Stable ααγ-Hybrid Peptides Inhibit the Aggregation and Cytotoxicity of Aβ. Acs Chemical Neuroscience. PMID 37656905 DOI: 10.1021/acschemneuro.3c00302 |
0.822 |
|
2022 |
Puneeth Kumar DR, Reja RM, Senapati DK, Singh M, Nalawade SA, George G, Kaul G, Akhir A, Chopra S, Raghothama S, Gopi HN. A cationic amphiphilic peptide chaperone rescues Aβ aggregation and cytotoxicity. Rsc Medicinal Chemistry. 14: 332-340. PMID 36846376 DOI: 10.1039/d2md00414c |
0.772 |
|
2021 |
Dolle A, Vijayasarathy M, Shekh S, Hunashal Y, Reddy KKA, Prakash S, Rana A, Biswal HS, Raghothama S, Gowd KH. The Redox-Active Conopeptide Derived from the Venom Duct Transcriptome of Assists in the Oxidative Folding of Conotoxin. Biochemistry. PMID 33829763 DOI: 10.1021/acs.biochem.1c00090 |
0.478 |
|
2020 |
Dolle A, Reddy KKA, Gunaga SS, Krishnamurthy K, Senapati DK, Rana A, Sindogi K, Biswal HS, Raghothama S, Gowd KH. Characterization of (Boc-Cys/Sec-NHMe) and (Boc-Cys/Sec-OMe) : Evidence of local conformational difference between disulfide and diselenide. Journal of Peptide Science : An Official Publication of the European Peptide Society. e3245. PMID 32103604 DOI: 10.1002/Psc.3245 |
0.787 |
|
2020 |
Misra R, George G, Reja RM, Dey S, Raghothama S, Gopi HN. Structural insight into hybrid peptide ε-helices. Chemical Communications (Cambridge, England). PMID 31970340 DOI: 10.1039/C9Cc07413A |
0.812 |
|
2020 |
Gopi H, Reja RM, Kumar V, George G, Patel R, Dr PK, Raghothama S. Structural Investigation of Hybrid Peptide Foldamers Composed of α-Dipeptide Equivalent β-Oxy-δ5-Amino Acids. Chemistry (Weinheim An Der Bergstrasse, Germany). PMID 31960517 DOI: 10.1002/Chem.201904780 |
0.83 |
|
2019 |
Yarava JR, Nishiyama Y, Raghothama S, Ramanathan KV. Conformational Investigation of Peptides Using Solid State NMR Spectroscopy - A Study of Polymorphism of β-turn Peptides Containing Diprolines. Chemical Biology & Drug Design. PMID 31755652 DOI: 10.1111/Cbdd.13649 |
0.577 |
|
2019 |
Misra R, George G, Saseendran A, Raghothama S, Gopi H. Ambidextrous α,γ-Hybrid Peptide Foldamers. Chemistry, An Asian Journal. PMID 31670907 DOI: 10.1002/Asia.201901411 |
0.816 |
|
2019 |
Dolle A, Nagati VB, Hunashal Y, Krishnamurthy K, Pasupulati AK, Raghothama S, Gowd KH. Disulfide engineering on temporin-SHf: Stabilizing the bioactive conformation of an ultra-short antimicrobial peptide. Chemical Biology & Drug Design. 94: 1634-1646. PMID 30924306 DOI: 10.1111/cbdd.13525 |
0.468 |
|
2019 |
Guterman T, Ing NL, Fleischer S, Rehak P, Basavalingappa V, Hunashal Y, Dongre R, Raghothama S, Král P, Dvir T, Hochbaum AI, Gazit E. Electrical Conductivity, Selective Adhesion, and Biocompatibility in Bacteria-Inspired Peptide-Metal Self-Supporting Nanocomposites. Advanced Materials (Deerfield Beach, Fla.). e1807285. PMID 30644148 DOI: 10.1002/Adma.201807285 |
0.39 |
|
2018 |
Krishnarjuna B, MacRaild CA, Sunanda P, Morales RAV, Peigneur S, Macrander J, Yu HH, Daly M, Raghothama S, Dhawan V, Chauhan S, Tytgat J, Pennington MW, Norton RS. Corrigendum to "Structure, folding and stability of a minimal homologue from Anemonia sulcata of the sea anemone potassium channel blocker ShK" [Peptides 99 (2018) 169-178]. Peptides. PMID 29361315 DOI: 10.1016/J.Peptides.2018.01.008 |
0.392 |
|
2017 |
Khare H, Dey D, Madhu C, Senapati D, Raghothama S, Govindaraju T, Ramakumar S. Conformational heterogeneity in tails of DNA-binding proteins is augmented by proline containing repeats. Molecular Biosystems. PMID 29104984 DOI: 10.1039/C7Mb00412E |
0.828 |
|
2017 |
Krishnarjuna B, MacRaild CA, Sunanda P, Morales RAV, Peigneur S, Macrander J, Yu HH, Daly M, Raghothama S, Dhawan V, Chauhan S, Tytgat J, Pennington MW, Norton RS. Structure, folding and stability of a minimal homologue from Anemonia sulcata of the sea anemone potassium channel blocker ShK. Peptides. PMID 28993277 DOI: 10.1016/J.Peptides.2017.10.001 |
0.342 |
|
2017 |
Wani NA, Raghothama S, Singh UP, Rai R. C₁₁/C₉ Helical Folding in αβ Hybrid Peptides Containing 1-Aminocyclohexane acetic acid (β³´³-Ac₆c). Chemistry (Weinheim An Der Bergstrasse, Germany). PMID 28440566 DOI: 10.1002/chem.201700265 |
0.51 |
|
2017 |
Misra R, Saseendran A, George G, Veeresh K, Raja KM, Raghothama S, Hofmann HJ, Gopi H. Structural Dimorphism of Achiral alpha,gamma-Hybrid Peptide Foldamers: Coexistence of 12- and 15/17-Helices. Chemistry (Weinheim An Der Bergstrasse, Germany). PMID 28052426 DOI: 10.1002/Chem.201605753 |
0.799 |
|
2017 |
Vasantha B, Yamanappa H, Raghothama S, Balaram P. Conformational properties and aggregation of homo-oligomeric β (R)-valine peptides in organic solvents. Biopolymers. 108. PMID 28026005 DOI: 10.1002/Bip.23011 |
0.751 |
|
2016 |
Vasantha B, George G, Raghothama S, Balaram P. Homooligomeric β(3) (R)-Valine Peptides: Transformation between C14 and C12 Helical Structures Induced by a Guest Aib Residue. Biopolymers. PMID 27539268 DOI: 10.1002/Bip.22935 |
0.83 |
|
2016 |
Misra R, Reja RM, Narendra LV, George G, Raghothama S, Gopi HN. Exploring structural features of folded peptide architectures in the construction of nanomaterials. Chemical Communications (Cambridge, England). PMID 27399170 DOI: 10.1039/C6Cc04502B |
0.786 |
|
2015 |
Duley A, Gowda V, Ganjiwale A, Raghothama S, Ramanathan G. Effect of methylene group insertions on the structural rigidity of Aib containing helices. Biopolymers. 104: 720-32. PMID 26152771 DOI: 10.1002/Bip.22691 |
0.815 |
|
2015 |
De Zoysa GH, Cameron AJ, Hegde VV, Raghothama S, Sarojini V. Antimicrobial peptides with potential for biofilm eradication: synthesis and structure activity relationship studies of battacin peptides. Journal of Medicinal Chemistry. 58: 625-39. PMID 25495219 DOI: 10.1021/jm501084q |
0.46 |
|
2015 |
Chandrappa S, Madhusudana Reddy MB, Sonti R, Basuroy K, Raghothama S, Balaram P. Directing peptide conformation with centrally positioned pre-organized dipeptide segments: studies of a 12-residue helix and β-hairpin. Amino Acids. 47: 291-301. PMID 25399053 DOI: 10.1007/S00726-014-1858-0 |
0.781 |
|
2014 |
Sonti R, Rao KN, Chidanand S, Gowd KH, Raghothama S, Balaram P. Conformational analysis of a 20-membered cyclic peptide disulfide from Conus virgo with a WPW segment: evidence for an aromatic-proline sandwich. Chemistry (Weinheim An Der Bergstrasse, Germany). 20: 5075-86. PMID 24644085 DOI: 10.1002/Chem.201303687 |
0.752 |
|
2014 |
Sonti R, Dinesh B, Basuroy K, Raghothama S, Shamala N, Balaram P. C12 helices in long hybrid (αγ)n peptides composed entirely of unconstrained residues with proteinogenic side chains. Organic Letters. 16: 1656-9. PMID 24588077 DOI: 10.1021/Ol500307P |
0.759 |
|
2013 |
Basuroy K, Dinesh B, Reddy MB, Chandrappa S, Raghothama S, Shamala N, Balaram P. Unconstrained homooligomeric γ-peptides show high propensity for C14 helix formation. Organic Letters. 15: 4866-9. PMID 24000950 DOI: 10.1021/Ol402248S |
0.692 |
|
2013 |
Makwana KM, Raghothama S, Mahalakshmi R. Stabilizing effect of electrostatic vs. aromatic interactions in diproline nucleated peptide β-hairpins Physical Chemistry Chemical Physics. 15: 15321-15324. PMID 23942893 DOI: 10.1039/C3Cp52770K |
0.7 |
|
2013 |
Narayan P, Krishnarjuna B, Vishwanathan V, Jagadeesh Kumar D, Babu S, Ramanathan KV, Easwaran KR, Nagendra HG, Raghothama S. Does aluminium bind to histidine? An NMR investigation of amyloid β12 and amyloid β16 fragments. Chemical Biology & Drug Design. 82: 48-59. PMID 23464626 DOI: 10.1111/Cbdd.12129 |
0.461 |
|
2012 |
Rajagopal A, Aravinda S, Raghothama S, Shamala N, Balaram P. Aromatic interactions in model peptide β-hairpins: ring current effects on proton chemical shifts. Biopolymers. 98: 185-94. PMID 22782561 DOI: 10.1002/Bip.22003 |
0.734 |
|
2012 |
Kaushik S, Krishnarjuna B, Raghothama S, Aggarwal S, Raghunathan V, Ganjiwale A. Theoretical and in vitro studies of a C-terminal peptide from PGKC of Leishmania mexicana mexicana. Molecular and Biochemical Parasitology. 185: 27-35. PMID 22710389 DOI: 10.1016/J.Molbiopara.2012.06.004 |
0.315 |
|
2012 |
Basuroy K, Rajagopal A, Raghothama S, Shamala N, Balaram P. β-Turn analogues in model αβ-hybrid peptides: structural characterization of peptides containing β(2,2)Ac6c and β(3,3)Ac6c residues. Chemistry, An Asian Journal. 7: 1671-8. PMID 22555984 DOI: 10.1002/Asia.201200052 |
0.756 |
|
2012 |
Chandrappa S, Aravinda S, Raghothama S, Sonti R, Rai R, Harini VV, Shamala N, Balaram P. Helix and hairpin nucleation in short peptides using centrally positioned conformationally constrained dipeptide segments. Organic & Biomolecular Chemistry. 10: 2815-23. PMID 22374581 DOI: 10.1039/C2Ob06817F |
0.753 |
|
2011 |
Rajagopal A, Aravinda S, Raghothama S, Shamala N, Balaram P. Chain length effects on helix-hairpin distribution in short peptides with Aib-DAla and Aib-Aib segments. Biopolymers. 96: 744-56. PMID 22252425 DOI: 10.1002/Bip.21613 |
0.752 |
|
2010 |
Raghothama S, Aravinda S, Shamala N, Balaram P. Helical conformations of hexapeptides containing N-terminus diproline segments. Biopolymers. 94: 360-70. PMID 20108314 DOI: 10.1002/Bip.21395 |
0.771 |
|
2009 |
Raghothama S, Raghavender US, Aravinda S, Shamala N, Balaram P. Conformations of heterochiral and homochiral proline-pseudoproline segments in peptides: context dependent cis-trans peptide bond isomerization. Biopolymers. 92: 405-16. PMID 19373926 DOI: 10.1002/Bip.21207 |
0.713 |
|
2009 |
Chatterjee S, Vasudev PG, Raghothama S, Ramakrishnan C, Shamala N, Balaram P. Expanding the peptide beta-turn in alphagamma hybrid sequences: 12 atom hydrogen bonded helical and hairpin turns. Journal of the American Chemical Society. 131: 5956-65. PMID 19341285 DOI: 10.1021/Ja900618H |
0.719 |
|
2008 |
Chatterjee S, Vasudev PG, Raghothama S, Shamala N, Balaram P. Solid state and solution conformations of a hybrid alphagammaalphaalphagammaalpha hexapeptide. Characterization of a backbone expanded analog of the alpha-polypeptide 3(10)-helix. Biopolymers. 90: 759-71. PMID 18767124 DOI: 10.1002/Bip.21076 |
0.7 |
|
2008 |
Chatterjee S, Vasudev PG, Ananda K, Raghothama S, Shamala N, Balaram P. Multiple conformational states in crystals and in solution in alphagamma hybrid peptides. Fragility of the C12 helix in short sequences. The Journal of Organic Chemistry. 73: 6595-606. PMID 18662036 DOI: 10.1021/Jo8009819 |
0.682 |
|
2008 |
Chatterjee B, Saha I, Raghothama S, Aravinda S, Rai R, Shamala N, Balaram P. Designed peptides with homochiral and heterochiral diproline templates as conformational constraints. Chemistry (Weinheim An Der Bergstrasse, Germany). 14: 6192-204. PMID 18491347 DOI: 10.1002/Chem.200702029 |
0.638 |
|
2007 |
Rai R, Vasudev PG, Ananda K, Raghothama S, Shamala N, Karle IL, Balaram P. Hybrid peptides: expanding the beta turn in peptide hairpins by the insertion of beta-, gamma-, and delta-residues. Chemistry (Weinheim An Der Bergstrasse, Germany). 13: 5917-26. PMID 17393543 DOI: 10.1002/Chem.200601562 |
0.675 |
|
2007 |
Rai R, Raghothama S, Sridharan R, Balaram P. Tuning the beta-turn segment in designed peptide beta-hairpins: construction of a stable type I' beta-turn nucleus and hairpin-helix transition promoting segments. Biopolymers. 88: 350-61. PMID 17154289 DOI: 10.1002/Bip.20649 |
0.636 |
|
2007 |
Mahalakshmi R, Sengupta A, Raghothama S, Shamala N, Balaram P. Tryptophan rich peptides: influence of indole rings on backbone conformation. Biopolymers. 88: 36-54. PMID 17091496 DOI: 10.1002/Bip.20625 |
0.834 |
|
2006 |
Rai R, Aravinda S, Kanagarajadurai K, Raghothama S, Shamala N, Balaram P. Diproline templates as folding nuclei in designed peptides. Conformational analysis of synthetic peptide helices containing amino terminal Pro-Pro segments Journal of the American Chemical Society. 128: 7916-7928. PMID 16771506 DOI: 10.1021/Ja060674V |
0.72 |
|
2006 |
Rai R, Raghothama S, Balaram P. Design of a peptide hairpin containing a central three-residue loop Journal of the American Chemical Society. 128: 2675-2681. PMID 16492054 DOI: 10.1021/Ja056861V |
0.79 |
|
2006 |
Roy RS, Gopi HN, Raghothama S, Karle IL, Balaram P. Hybrid peptide hairpins containing alpha- and omega-amino acids: conformational analysis of decapeptides with unsubstituted beta-, gamma-, and delta-residues at positions 3 and 8. Chemistry (Weinheim An Der Bergstrasse, Germany). 12: 3295-302. PMID 16453362 DOI: 10.1002/Chem.200500742 |
0.86 |
|
2006 |
Mahalakshmi R, Raghothama S, Balaram P. NMR analysis of aromatic interactions in designed peptide β-hairpins Journal of the American Chemical Society. 128: 1125-1138. PMID 16433528 DOI: 10.1021/Ja054040K |
0.803 |
|
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