Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Gérald, Lelais"'
Autor:
Laura J, Kingsley, Xiaohui, He, Matthew, McNeill, John, Nelson, Victor, Nikulin, Zhiwei, Ma, Wenshuo, Lu, Vicki W, Zhou, Mari, Manuia, Andreas, Kreusch, Mu-Yun, Gao, Darbi, Witmer, Mei-Ting, Vaillancourt, Min, Lu, Sarah, Greenblatt, Christian, Lee, Ajay, Vashisht, Steven, Bender, Glen, Spraggon, Pierre-Yves, Michellys, Yong, Jia, Jacob R, Haling, Gérald, Lelais
Publikováno v:
Journal of medicinal chemistry. 64(8)
LONP1 is an AAA+ protease that maintains mitochondrial homeostasis by removing damaged or misfolded proteins. Elevated activity and expression of LONP1 promotes cancer cell proliferation and resistance to apoptosis-inducing reagents. Despite the impo
Autor:
Gérald, Lelais, Robert, Epple, Thomas H, Marsilje, Yun O, Long, Matthew, McNeill, Bei, Chen, Wenshuo, Lu, Jaganmohan, Anumolu, Sangamesh, Badiger, Badry, Bursulaya, Michael, DiDonato, Rina, Fong, Jose, Juarez, Jie, Li, Mari, Manuia, Daniel E, Mason, Perry, Gordon, Todd, Groessl, Kevin, Johnson, Yong, Jia, Shailaja, Kasibhatla, Chun, Li, John, Isbell, Glen, Spraggon, Steven, Bender, Pierre-Yves, Michellys
Publikováno v:
Journal of medicinal chemistry. 59(14)
Over the past decade, first and second generation EGFR inhibitors have significantly improved outcomes for lung cancer patients with activating mutations in EGFR. However, both resistance through a secondary T790M mutation at the gatekeeper residue a
Publikováno v:
Helvetica Chimica Acta. 91:2035-2056
The new electrophilic trifluoromethylating 1-(trifluoromethyl)-benziodoxole reagents A and B (Scheme 1) have been used to selectively attach CF3 groups to the S-atom of cysteine side chains of α- and β-peptides (up to 13-residues-long; products 7
Publikováno v:
Helvetica Chimica Acta. 87:1545-1560
(S)-β2-Homoamino acids with the side chains of Asp, Glu, Asn, and Gln have been prepared and suitably protected (N-Fmoc, CO2tBu, CONHTrt) for solid-phase peptide syntheses. The key steps of the syntheses are: N-acylation of 5,5-diphenyl-4-isopropyl-
Autor:
Dieter Seebach, Gérald Lelais
Publikováno v:
Biopolymers. 76:206-243
Although they are less abundant than their alpha-analogues, beta-amino acids occur in nature both in free form and bound to peptides. Oligomers composed exclusively of beta-amino acids (so-called beta-peptides) might be the most thoroughly investigat
Autor:
Radovan Šebesta, Bernd Schweizer, Gérald Lelais, Laurent Schaeffer, Peter Micuch, Sascha Kopp, Yogesh R. Mahajan, Dieter Seebach, Delphine Josien, François Gessier, Pascal Bindschädler, Corinna Jäger
Publikováno v:
Helvetica Chimica Acta. 86:1852-1861
Multigram amounts of suitably protected β2-amino acids with 17 of the 20 proteinogenic side chains are prepared by diastereoselective reactions of Li, B, or Ti enolates of the corresponding 3-acyl-4-isopropyl-5,5-diphenyloxazolidin-2-ones (acyl-DIOZ
Autor:
Gérald Lelais, David W. C. MacMillan
Publikováno v:
New Frontiers in Asymmetric Catalysis
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9c4f1d490a704ee268f8d9d4508f3551
https://doi.org/10.1002/9780470098004.ch11
https://doi.org/10.1002/9780470098004.ch11
Autor:
Gérald, Lelais, Dieter, Seebach
Publikováno v:
Biopolymers. 76(3)
Although they are less abundant than their alpha-analogues, beta-amino acids occur in nature both in free form and bound to peptides. Oligomers composed exclusively of beta-amino acids (so-called beta-peptides) might be the most thoroughly investigat
Autor:
Dieter Seebach, Gérald Lelais
Publikováno v:
Peptides: The Wave of the Future ISBN: 9789401039055
It has been demonstrated that short oligomers derived from β-amino acids (β-peptides) can fold into well-ordered secondary structures like helices, turns and sheets [1]. Furthermore, they show an outstanding stability against a large range of prote
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3334bb777ac2292161683aa7faae3729
https://doi.org/10.1007/978-94-010-0464-0_269
https://doi.org/10.1007/978-94-010-0464-0_269