Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Rahi M, Reja"'
Autor:
Alex J. Callahan, Satish Gandhesiri, Tara L. Travaline, Rahi M. Reja, Lia Lozano Salazar, Stephanie Hanna, Yen-Chun Lee, Kunhua Li, Olena S. Tokareva, Jean-Marie Swiecicki, Andrei Loas, Gregory L. Verdine, John H. McGee, Bradley L. Pentelute
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-13 (2024)
Abstract Widespread adoption of mirror-image biological systems presents difficulties in accessing the requisite D-protein substrates. In particular, mirror-image phage display has the potential for high-throughput generation of biologically stable m
Externí odkaz:
https://doaj.org/article/d0273f3cd1884e53b769531534d77eaf
Autor:
DRGKoppalu R. Puneeth Kumar, Rahi M. Reja, Dillip K. Senapati, Manjeet Singh, Sachin A. Nalawade, Gijo George, Grace Kaul, Abdul Akhir, Sidharth Chopra, Srinivasarao Raghothama, Hosahudya N. Gopi
Publikováno v:
RSC Medicinal Chemistry. 14:332-340
A cationic amphiphilic peptide effectively prevents the aggregation of soluble Aβ42 and also disintegrates matured fibrils into soluble precursors. In addition, the peptide also rescues cells from the toxicity of Aβ42.
Publikováno v:
Journal of the American Chemical Society. 144(34)
Binding via reversible covalent bond formation presents a novel and powerful mechanism to enhance the potency of synthetic inhibitors for therapeutically important proteins. Work on this front has yielded the anticancer drug bortezomib as well as the
Autor:
Vivek Kumar, Gijo George, DRGKoppalu R. Puneeth Kumar, Rahi M. Reja, Hosahudya N. Gopi, Rajat Patel, Srinivasarao Raghothama
Publikováno v:
Chemistry – A European Journal. 26:4304-4309
Due to their equivalent lengths, I´-amino acids can serve as surrogates of I±-dipeptides. However, I´-amino acids with proteinogenic side chains have not been well studied because of synthetic difficulties and because of their insolubility in orga
Publikováno v:
J Am Chem Soc
We report a new reversible lysine conjugation that features a novel diazaborine product and much slowed dissociation kinetics in comparison to the previously known iminoboronate chemistry. Incorporating the diazaborine-forming warhead RMR1 to a pepti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fc8ae71acb3011f2b287b94a3318d61a
https://europepmc.org/articles/PMC8928449/
https://europepmc.org/articles/PMC8928449/
Autor:
Rajkumar Misra, Hosahudya N. Gopi, Gijo George, Srinivasarao Raghothama, Sanjit Dey, Rahi M. Reja
Publikováno v:
Chemical Communications. 56:2171-2173
Unique ε-helical organizations (11-helices) from β,γ-hybrid peptides composed of chiral β3-amino acids along with achiral 3,3- or 4,4-dimethyl substituted γ-amino acids are disclosed.
Publikováno v:
ChemNanoMat. 5:51-54
Publikováno v:
Angewandte Chemie. 130:1069-1073
Double helices are not common in polypeptides and proteins except in the peptide antibiotic gramicidin A and analogous l,d-peptides. In contrast to natural polypeptides, remarkable β-double-helical structures from achiral γ-peptides built from α,
Publikováno v:
Organic Letters. 19:3572-3575
Synthesis and incorporation of a new amino acid with a nitroalkane side chain into peptides, in situ transformation of a nitroalkane side chain into nitrile oxide, and chemoselective 1,3-dipolar cycloaddition reactions between in situ generated nitri
Autor:
Rahi M, Reja, Vivek, Kumar, Gijo, George, Rajat, Patel, DRGKoppalu R, Puneeth Kumar, Srinivasarao, Raghothama, Hosahudya N, Gopi
Publikováno v:
Chemistry (Weinheim an der Bergstrasse, Germany). 26(19)
Due to their equivalent lengths, δ-amino acids can serve as surrogates of α-dipeptides. However, δ-amino acids with proteinogenic side chains have not been well studied because of synthetic difficulties and because of their insolubility in organic