Clinical candidates modulating protein-protein interactions

Publikováno v: European Journal of Medicinal Chemistry. 167:76-95

Protein-protein interactions (PPIs) cover a very wide range of biological functions and consequently have become one of the favourite targets for new therapeutic strategies. PPIs are strongly characterised by an intricate and dynamic network of surfa

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dris___01180::56a9cdba7475dd5776c6709f9c5fab9e
https://research.tue.nl/en/publications/3fa6d7ab-a7a7-4e98-92ce-374e7f310397

Adaptive landscape flattening in amino acid sequence space for the computational design of protein:peptide binding

Autor: Thomas Simonson, Francesco Villa, Nicolas Panel, Xingyu Chen

Publikováno v: Journal of Chemical Physics
Journal of Chemical Physics, American Institute of Physics, 2018, 149 (7), pp.072302. ⟨10.1063/1.5022249⟩

International audience; For the high throughput design of protein:peptide binding, one must explore a vast space of amino acid sequences in search of low binding free energies. This complex problem is usually addressed with either simple heuristic sc

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9bacfcd013a2ab009841d86812aef832
https://pubmed.ncbi.nlm.nih.gov/30134674

Peptide- and Amine-Modified Glucan Particles for the Delivery of Therapeutic siRNA

Autor: Jessica Cohen, Pranitha Vangala, Joseph C. Yawe, Michael P. Czech, Shinya U. Amano, Yuefei Shen, Sarah M. Nicoloro, Myriam Aouadi, Michaela Tencerova

Publikováno v: Cohen, J L, Shen, Y, Aouadi, M, Vangala, P, Tencerova, M, Amano, S U, Nicoloro, S M, Yawe, J C & Czech, M P 2016, ' Peptide-and Amine-Modified Glucan Particles for the Delivery of Therapeutic siRNA ', Molecular Pharmaceutics, vol. 13, no. 3, pp. 964-978 . https://doi.org/10.1021/acs.molpharmaceut.5b00831

Translation of siRNA technology into the clinic is limited by the need for improved delivery systems that target specific cell types. Macrophages are particularly attractive targets for RNAi therapy because they promote pathogenic inflammatory respon

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9caf88296b889e21e513790651dfbabf
https://europepmc.org/articles/PMC5153885/

Alanine Scanning Mutagenesis of the Second Extracellular Loop of Type 1 Corticotropin-Releasing Factor Receptor Revealed Residues Critical for Peptide Binding

Autor: T. Tselios, Iakovos Lazaridis, Achille Gravanis, Olga Rassouli, George Deraos, Kostas Gkountelias, Maria Venihaki, George Liapakis

Publikováno v: Molecular Pharmacology. 75:793-800

Upon binding of the corticotropin-releasing factor (CRF) analog sauvagine to the type 1 CRF receptor (CRF(1)), the amino-terminal portion of the peptide has been shown to lie near Lys257 in the receptor's second extracellular loop (EL2). To test the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7fbb5d54e38766f401c49617f1cd939b
https://doi.org/10.1124/mol.108.052423

Fragment N2, a caspase-3-generated RasGAP fragment, inhibits breast cancer metastatic progression

Autor: Christian Widmann, David Viertl, Benoit Lhermitte, David Barras, Girieca Lorusso, Curzio Rüegg

Publikováno v: International Journal of Cancer. Journal International Du Cancer, vol. 135, no. 1, pp. 242-247

The p120 RasGAP protein negatively regulates Ras via its GAP domain. RasGAP carries several other domains that modulate several signaling molecules such as Rho. RasGAP is also a caspase-3 substrate. One of the caspase-3-generated RasGAP fragments, co

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f18959e564ce0b3a472771f3bb8f5d86
https://serval.unil.ch/resource/serval:BIB_1FACF08B8A65.P001/REF.pdf