Year |
Citation |
Score |
2023 |
Li NZ, Yu CH, Wu JY, Huang SJ, Huang SL, Cheng RP. Diagonal Interactions between Glutamate and Arginine Analogs with Varying Side-Chain Lengths in a β-Hairpin. Molecules (Basel, Switzerland). 28. PMID 37049652 DOI: 10.3390/molecules28072888 |
0.51 |
|
2022 |
Chang JY, Pan YJ, Huang PY, Sun YT, Yu CH, Ning ZJ, Huang SL, Huang SJ, Cheng RP. The Effects of Charged Amino Acid Side-Chain Length on Diagonal Cross-Strand Interactions between Carboxylate- and Ammonium-Containing Residues in a β-Hairpin. Molecules (Basel, Switzerland). 27. PMID 35807421 DOI: 10.3390/molecules27134172 |
0.472 |
|
2021 |
Chang JY, Li NZ, Wang WM, Liu CT, Yu CH, Chen YC, Lu D, Lin PH, Huang CH, Kono O, Yang TY, Sun YT, Huang PY, Pan YJ, Chen TH, ... ... Cheng RP, et al. Longer charged amino acids favor β-strand formation in hairpin peptides. Journal of Peptide Science : An Official Publication of the European Peptide Society. e3333. PMID 34114290 DOI: 10.1002/psc.3333 |
0.561 |
|
2021 |
Huang CH, Wong TW, Yu CH, Chang JY, Huang SJ, Huang SL, Cheng RP. Swapping the Positions in a Cross-Strand Lateral Ion-Pairing Interaction between Ammonium- and Carboxylate-Containing Residues in a β-Hairpin. Molecules (Basel, Switzerland). 26. PMID 33802596 DOI: 10.3390/molecules26051346 |
0.461 |
|
2021 |
Wang WM, Yu CH, Chang JY, Chen TH, Chen YC, Sun YT, Wang SH, Jao SC, Cheng RP. Insertion of Pro-Hyp-Gly provides 2 kcal mol stability but attenuates the specific assembly of ABC heterotrimeric collagen triple helices. Organic & Biomolecular Chemistry. PMID 33565556 DOI: 10.1039/d0ob02190c |
0.351 |
|
2019 |
Wu PY, Chen CY, Li JH, Lin JK, Chen TH, Huang SL, Huang SJ, Cheng RP. Effect of arginine deimination and citrulline side chain length on secondary structure formation. Chembiochem : a European Journal of Chemical Biology. PMID 31071235 DOI: 10.1002/Cbic.201900231 |
0.634 |
|
2016 |
Chen YT, Chao WC, Kuo HT, Shen JY, Chen IH, Yang HC, Wang JS, Lu JF, Cheng RP, Chou PT. Probing the polarity and water environment at the protein-peptide binding interface using tryptophan analogues. Biochemistry and Biophysics Reports. 7: 113-118. PMID 28955897 DOI: 10.1016/J.Bbrep.2016.05.022 |
0.513 |
|
2016 |
Liu MC, Chen CY, Chiang CH, Wang WM, Cheng RP. Effect of lysine methylation and acetylation on the RNA recognition and cellular uptake of Tat-derived peptides. Bioorganic & Medicinal Chemistry. PMID 27670097 DOI: 10.1016/J.Bmc.2016.08.015 |
0.488 |
|
2015 |
Wu CH, Chen YP, Liu SL, Chien FC, Mou CY, Cheng RP. Attenuating HIV Tat/TAR-mediated protein expression by exploring the side chain length of positively charged residues. Organic & Biomolecular Chemistry. PMID 26399751 DOI: 10.1039/C5Ob01729G |
0.501 |
|
2015 |
Koubek J, Chen YR, Cheng RP, Huang JJ. Nonorthogonal tRNA(cys)(Amber) for protein and nascent chain labeling. Rna (New York, N.Y.). 21: 1672-82. PMID 26194135 DOI: 10.1261/Rna.051805.115 |
0.356 |
|
2015 |
Li JH, Chiu WC, Yao YC, Cheng RP. Effect of arginine methylation on the RNA recognition and cellular uptake of Tat-derived peptides. Bioorganic & Medicinal Chemistry. 23: 2281-6. PMID 25800434 DOI: 10.1016/J.Bmc.2015.01.051 |
0.489 |
|
2015 |
Kuo HT, Liu SL, Chiu WC, Fang CJ, Chang HC, Wang WR, Yang PA, Li JH, Huang SJ, Huang SL, Cheng RP. Effect of charged amino acid side chain length on lateral cross-strand interactions between carboxylate- and guanidinium-containing residues in a β-hairpin. Amino Acids. 47: 885-98. PMID 25646959 DOI: 10.1007/S00726-015-1916-2 |
0.61 |
|
2014 |
Wu CH, Weng MH, Chang HC, Li JH, Cheng RP. Effect of each guanidinium group on the RNA recognition and cellular uptake of Tat-derived peptides. Bioorganic & Medicinal Chemistry. 22: 3016-20. PMID 24767816 DOI: 10.1016/J.Bmc.2014.03.037 |
0.503 |
|
2014 |
Kuo HT, Yang PA, Wang WR, Hsu HC, Wu CH, Ting YT, Weng MH, Kuo LH, Cheng RP. Effect of side chain length on intrahelical interactions between carboxylate- and guanidinium-containing amino acids. Amino Acids. 46: 1867-83. PMID 24744084 DOI: 10.1007/S00726-014-1737-8 |
0.688 |
|
2013 |
Kuo HT, Fang CJ, Tsai HY, Yang MF, Chang HC, Liu SL, Kuo LH, Wang WR, Yang PA, Huang SJ, Huang SL, Cheng RP. Effect of charged amino acid side chain length on lateral cross-strand interactions between carboxylate-containing residues and lysine analogues in a β-hairpin. Biochemistry. 52: 9212-22. PMID 24328126 DOI: 10.1021/Bi400974X |
0.569 |
|
2013 |
Wu CH, Chen YP, Wu SH, Hung Y, Mou CY, Cheng RP. Enhanced non-endocytotic uptake of mesoporous silica nanoparticles by shortening the peptide transporter arginine side chain. Acs Applied Materials & Interfaces. 5: 12244-8. PMID 24261815 DOI: 10.1021/Am4039882 |
0.401 |
|
2013 |
Kuo LH, Li JH, Kuo HT, Hung CY, Tsai HY, Chiu WC, Wu CH, Wang WR, Yang PA, Yao YC, Wong TW, Huang SJ, Huang SL, Cheng RP. Effect of charged amino acid side chain length at non-hydrogen bonded strand positions on β-hairpin stability. Biochemistry. 52: 7785-97. PMID 24156236 DOI: 10.1021/Bi400911P |
0.607 |
|
2013 |
Wu CH, Chen YP, Mou CY, Cheng RP. Altering the Tat-derived peptide bioactivity landscape by changing the arginine side chain length. Amino Acids. 44: 473-80. PMID 22821217 DOI: 10.1007/S00726-012-1357-0 |
0.542 |
|
2012 |
Cheng RP, Wang WR, Girinath P, Yang PA, Ahmad R, Li JH, Hart P, Kokona B, Fairman R, Kilpatrick C, Argiros A. Effect of glutamate side chain length on intrahelical glutamate-lysine ion pairing interactions. Biochemistry. 51: 7157-72. PMID 22931137 DOI: 10.1021/Bi300655Z |
0.774 |
|
2012 |
Cheng RP, Weng YJ, Wang WR, Koyack MJ, Suzuki Y, Wu CH, Yang PA, Hsu HC, Kuo HT, Girinath P, Fang CJ. Helix formation and capping energetics of arginine analogs with varying side chain length. Amino Acids. 43: 195-206. PMID 21922267 DOI: 10.1007/S00726-011-1064-2 |
0.742 |
|
2010 |
Cheng RP, Girinath P, Suzuki Y, Kuo HT, Hsu HC, Wang WR, Yang PA, Gullickson D, Wu CH, Koyack MJ, Chiu HP, Weng YJ, Hart P, Kokona B, Fairman R, et al. Positional effects on helical Ala-based peptides Biochemistry. 49: 9372-9384. PMID 20925317 DOI: 10.1021/Bi101156J |
0.714 |
|
2010 |
Cheng RP, Gellman SH, DeGrado WF. ChemInform Abstract: β-Peptides: From Structure to Function Cheminform. 32: no-no. DOI: 10.1002/chin.200152275 |
0.504 |
|
2009 |
Chiu HP, Kokona B, Fairman R, Cheng RP. Effect of highly fluorinated amino acids on protein stability at a solvent-exposed position on an internal strand of protein G B1 domain. Journal of the American Chemical Society. 131: 13192-3. PMID 19711980 DOI: 10.1021/Ja903631H |
0.764 |
|
2009 |
Heimburg-Molinaro J, Almogren A, Morey S, Glinskii OV, Roy R, Wilding GE, Cheng RP, Glinsky VV, Rittenhouse-Olson K. Development, characterization, and immunotherapeutic use of peptide mimics of the Thomsen-Friedenreich carbohydrate antigen. Neoplasia (New York, N.Y.). 11: 780-92. PMID 19649208 DOI: 10.1593/Neo.09504 |
0.315 |
|
2007 |
Chiu HP, Cheng RP. Chemoenzymatic synthesis of (S)-hexafluoroleucine and (S)-tetrafluoroleucine. Organic Letters. 9: 5517-20. PMID 18044910 DOI: 10.1021/Ol702470J |
0.668 |
|
2007 |
Cheng RP, Girinath P, Ahmad R. Effect of lysine side chain length on intra-helical glutamate--lysine ion pairing interactions. Biochemistry. 46: 10528-37. PMID 17718542 DOI: 10.1021/bi700701z |
0.788 |
|
2006 |
Chiu HP, Suzuki Y, Gullickson D, Ahmad R, Kokona B, Fairman R, Cheng RP. Helix propensity of highly fluorinated amino acids. Journal of the American Chemical Society. 128: 15556-7. PMID 17147342 DOI: 10.1021/Ja0640445 |
0.785 |
|
2006 |
Koyack MJ, Cheng RP. Design and synthesis of beta-peptides with biological activity. Methods in Molecular Biology (Clifton, N.J.). 340: 95-109. PMID 16957334 DOI: 10.1385/1-59745-116-9:95 |
0.797 |
|
2004 |
Cheng RP. Beyond de novo protein design--de novo design of non-natural folded oligomers. Current Opinion in Structural Biology. 14: 512-20. PMID 15313247 DOI: 10.1016/J.Sbi.2004.07.001 |
0.358 |
|
2003 |
Walsh ST, Cheng RP, Wright WW, Alonso DO, Daggett V, Vanderkooi JM, DeGrado WF. The hydration of amides in helices; a comprehensive picture from molecular dynamics, IR, and NMR. Protein Science : a Publication of the Protein Society. 12: 520-31. PMID 12592022 DOI: 10.1110/Ps.0223003 |
0.689 |
|
2002 |
Cheng RP, DeGrado WF. Long-range interactions stabilize the fold of a non-natural oligomer. Journal of the American Chemical Society. 124: 11564-5. PMID 12296699 DOI: 10.1021/Ja020728A |
0.614 |
|
2001 |
Cheng RP, Suich DJ, Cheng H, Roder H, DeGrado WF. Template-constrained somatostatin analogues: a biphenyl linker induces a type-V' turn. Journal of the American Chemical Society. 123: 12710-1. PMID 11741449 DOI: 10.1021/Ja0116932 |
0.416 |
|
2001 |
Cheng RP, Gellman SH, DeGrado WF. beta-Peptides: from structure to function. Chemical Reviews. 101: 3219-32. PMID 11710070 DOI: 10.1021/Cr000045I |
0.585 |
|
2001 |
Cheng RP, DeGrado WF. De novo design of a monomeric helical beta-peptide stabilized by electrostatic interactions. Journal of the American Chemical Society. 123: 5162-3. PMID 11457373 DOI: 10.1021/Ja010438E |
0.638 |
|
2001 |
Mezo AR, Cheng RP, Imperiali B. Oligomerization of uniquely folded mini-protein motifs: development of a homotrimeric betabetaalpha peptide. Journal of the American Chemical Society. 123: 3885-91. PMID 11457138 DOI: 10.1021/Ja004292F |
0.707 |
|
2001 |
Cheng RP, Gellman SH, DeGrado WF. β-peptides: From structure to function Chemical Reviews. 101: 3219-3232. DOI: 10.1021/cr000045i |
0.534 |
|
1996 |
Struthers MD, Cheng RP, Imperiali B. Design of a monomeric 23-residue polypeptide with defined tertiary structure. Science (New York, N.Y.). 271: 342-5. PMID 8553067 DOI: 10.1126/Science.271.5247.342 |
0.585 |
|
1996 |
Cheng RP, Fisher SL, Imperiali B. Metallopeptide design: Tuning the metal cation affinities with unnatural amino acids and peptide secondary structure Journal of the American Chemical Society. 118: 11349-11356. DOI: 10.1021/Ja9619723 |
0.692 |
|
1996 |
Struthers MD, Cheng RP, Imperiali B. Economy in protein design: Evolution of a metal-independent ββα motif based on the zinc finger domains Journal of the American Chemical Society. 118: 3073-3081. DOI: 10.1021/Ja954014U |
0.638 |
|
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