Výsledky vyhledávání - "Julian Nomme"

Akademický článek

Biosynthesis of a clickable pyoverdine via in vivo enzyme engineering of an adenylation domain

Autor: Hélène Puja, Laurent Bianchetti, Johan Revol-Tissot, Nicolas Simon, Anastasiia Shatalova, Julian Nommé, Sarah Fritsch, Roland H. Stote, Gaëtan L. A. Mislin, Noëlle Potier, Annick Dejaegere, Coraline Rigouin

Publikováno v: Microbial Cell Factories, Vol 23, Iss 1, Pp 1-16 (2024)

Abstract The engineering of non ribosomal peptide synthetases (NRPS) for new substrate specificity is a potent strategy to incorporate non-canonical amino acids into peptide sequences, thereby creating peptide diversity and broadening applications. T

Externí odkaz: https://doaj.org/article/22b918acf0c04a738ddc527f2d7544cd

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NMR secondary structure and interactions of recombinant human MOZART1 protein, a component of the gamma-tubulin complex

Autor: Alain Milon, Audrey Tourdes, Cyprian D. Cukier, Virginie Gervais, Andreas Merdes, Valérie Guillet, Dounia El-Mazouni, Lionel Mourey, Julian Nomme

Publikováno v: Protein Science. 26:2240-2248

MOZART1 (Mitotic-spindle organizing protein associated with a ring of γ-tubulin 1) is an 8.5 kDa protein linked to regulation of γ-tubulin ring complexes (γTuRCs), which are involved in nucleation of microtubules. Despite its small size, MOZART1 r

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::30c67987ef24b972e4f2a84402a183c2
https://doi.org/10.1002/pro.3282

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Structural Basis of a Key Factor Regulating the Affinity between the Zonula Occludens First PDZ Domain and Claudins

Autor: Aleksandar Antanasijevic, Michael Caffrey, Arnon Lavie, Christina M. Van Itallie, James M. Anderson, Alan S. Fanning, Julian Nomme

Publikováno v: Journal of Biological Chemistry. 290:16595-16606

The molecular seal between epithelial cells, called the tight junction (TJ), is built by several membrane proteins, with claudins playing the most prominent role. The scaffold proteins of the zonula occludens family are required for the correct local

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ad93bd7664194623e58192bfea53730e
https://doi.org/10.1074/jbc.m115.646695

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Elucidation of the Specific Function of the Conserved Threonine Triad Responsible for Human l-Asparaginase Autocleavage and Substrate Hydrolysis

Autor: Arnon Lavie, Ying Su, Julian Nomme

Publikováno v: Journal of Molecular Biology. 426:2471-2485

Our long-term goal is the design of a human l-asparaginase (hASNase3) variant, suitable for use in cancer therapy without the immunogenicity problems associated with the currently used bacterial enzymes. Asparaginases catalyze the hydrolysis of the a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ad5f804619187c220e627c541f2f03d7
https://doi.org/10.1016/j.jmb.2014.04.016

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Structural characterization of new deoxycytidine kinase inhibitors rationalizes the affinity-determining moieties of the molecules

Autor: Arnon Lavie, Julian Nomme, Caius G. Radu, Steven T. Olson, Amanda L. Armijo, Jennifer M. Murphy, Natasha D. Sansone, Ying Su

Publikováno v: Acta crystallographica. Section D, Biological crystallography, vol 70, iss Pt 1

Deoxycytidine kinase (dCK) is a key enzyme in the nucleoside salvage pathway that is also required for the activation of several anticancer and antiviral nucleoside analog prodrugs. Additionally, dCK has been implicated in immune disorders and has be

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0962ad62940b638fb15cfea454a62888
https://doi.org/10.1107/s1399004713025030

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Free Glycine Accelerates the Autoproteolytic Activation of Human Asparaginase

Autor: Julian Nomme, Theresa McSorley, Ying Su, Christos S. Karamitros, Arnon Lavie, Manfred Konrad

Publikováno v: Chemistry and Biology

Summary Human asparaginase 3 (hASNase3), which belongs to the N-terminal nucleophile hydrolase superfamily, is synthesized as a single polypeptide that is devoid of asparaginase activity. Intramolecular autoproteolytic processing releases the amino g

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3ecd3d23855a9ddc6674d60558b266c2

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Targeting human Rad51 by specific DNA aptamers induces inhibition of homologous recombination

Autor: Pierre Weigel, Masayuki Takahashi, Susan F. Martinez, Fabrice Fleury, Axelle Renodon-Cornière, Damien Eveillard, Julian Nomme

Publikováno v: Biochimie. 92:1832-1838

Human Rad51 (HsRad51), a key element of the homologous recombination repair pathway, is related to the resistance of cancer cells to chemo- and radio-therapies. This protein is thus a good target for the development of anti-cancer treatments. We have

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3fa4c31829cba93f3399e36c3965edf4
https://doi.org/10.1016/j.biochi.2010.08.006

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Design of Potent Inhibitors of Human RAD51 Recombinase Based on BRC Motifs of BRCA2 Protein: Modeling and Experimental Validation of a Chimera Peptide

Autor: Masayuki Takahashi, Bengt Nordén, Axelle Renodon-Cornière, Kazuyasu Sakaguchi, Julian Nomme, V.H. Tran, Yuya Asanomi, Andrzej Stasiak, Alicja Z. Stasiak

Publikováno v: Journal of Medicinal Chemistry, vol. 53, no. 15, pp. 5782-5791
Journal of Medicinal Chemistry

We have previously shown that a 28-amino acid peptide derived from the BRC4 motif of BRCA2 tumor suppressor inhibits selectively human RAD51 recombinase (HsRad51). With the aim of designing better inhibitors for cancer treatment, we combined an in si

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fe7904583315ec8beb502f5d13d30b99
https://doi.org/10.1021/jm1002974

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Inhibition of filament formation of human Rad51 protein by a small peptide derived from the BRC-motif of the BRCA2 protein

Autor: Susan F. Martinez, Ken Ichi Yamamoto, Fabrice Fleury, Yoshimasa Takizawa, Julian Nomme, Axelle Renodon-Cornière, Pierre Weigel, Masayuki Takahashi, Hitoshi Kurumizaka

Publikováno v: Genes to Cells. 13:471-481

Human Rad51 is a key element of recombinational DNA repair and is related to the resistance of cancer cells to chemo- and radiotherapies. The protein is thus a potential target of anti-cancer treatment. The crystallographic analysis shows that the BR

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ddc3d5f86bd1e46dc6c26ac5102c858e
https://doi.org/10.1111/j.1365-2443.2008.01180.x

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Structure-guided development of deoxycytidine kinase inhibitors with nanomolar affinity and improved metabolic stability

Autor: Tony Smith, Bernard D. Santarsiero, Arnon Lavie, Amanda L. Armijo, Johannes Czernin, Jue Wang, Michael E. Jung, Hien Anh Nguyen, Caius G. Radu, Thuc Le, Raymond M. Gipson, Julian Nomme, Zheng Li, Anastassia N. Alexandrova, Soumya Poddar

Publikováno v: Journal of medicinal chemistry, vol 57, iss 22
Journal of Medicinal Chemistry
Nomme, J; Li, Z; Gipson, RM; Wang, J; Armijo, AL; Le, T; et al.(2014). Structure-guided development of deoxycytidine kinase inhibitors with nanomolar affinity and improved metabolic stability. Journal of Medicinal Chemistry, 57(22), 9480-9494. doi: 10.1021/jm501124j. UCLA: Retrieved from: http://www.escholarship.org/uc/item/9fv4j1bs

© 2014 American Chemical Society. Recently, we have shown that small molecule dCK inhibitors in combination with pharmacological perturbations of de novo dNTP biosynthetic pathways could eliminate acute lymphoblastic leukemia cells in animal models.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5ed3f11060d74e247782e3622cb5968a
https://escholarship.org/uc/item/9fv4j1bs

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