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Статті в журналах з теми "Interactions protéine – protéine (IPP)":
Sperandio, Olivier, Bruno O. Villoutreix, Xavier Morelli, and Philippe Roche. "Les chimiothèques ciblant les interactions protéine-protéine." médecine/sciences 31, no. 3 (March 2015): 312–19. http://dx.doi.org/10.1051/medsci/20153103017.
Béganton, Benoît, Etienne Coyaud, Alain Mangé, and Jérôme Solassol. "Approches nouvelles pour l’étude des interactions protéine-protéine." médecine/sciences 35, no. 3 (March 2019): 223–31. http://dx.doi.org/10.1051/medsci/2019035.
Laudet, Béatrice, Renaud Prudent, Odile Filhol, and Claude Cochet. "Des agents thérapeutiques ciblant des interactions protéine-protéine." médecine/sciences 23, no. 3 (March 2007): 273–78. http://dx.doi.org/10.1051/medsci/2007233273.
Maire, Marc le. "Les interactions protéine-protéine dans les membranes: quelques concepts et l'exemple de l'ATPase calcique du reticulum sarcoplasmique." Biochimie 68, no. 3 (March 1986): 395–400. http://dx.doi.org/10.1016/s0300-9084(86)80006-2.
Demouveaux, Bastien, Valérie Gouyer, Mylène Magnien, Ségolène Plet, Frédéric Gottrand, Tetsuharu Narita, and Jean-Luc Desseyn. "La structure des mucines conditionne les propriétés viscoélastiques des gels de mucus." médecine/sciences 34, no. 10 (October 2018): 806–12. http://dx.doi.org/10.1051/medsci/2018206.
Taillandier, Daniel. "Contrôle des voies métaboliques par les enzymes E3 ligases : une opportunité de ciblage thérapeutique." Biologie Aujourd’hui 215, no. 1-2 (2021): 45–57. http://dx.doi.org/10.1051/jbio/2021006.
Maïa, N., and L. Cardin. "Accumulation de la protéine soluble (PR 1a) dans les interactions Nicotiana tabacuml Phytophthora ssp." Agronomie 13, no. 6 (1993): 527–36. http://dx.doi.org/10.1051/agro:19930610.
Bertoldo, M. J., E. Guibert, P. Tartarin, F. Guillou, M. Foretz, B. Viollet, and P. Froment. "L’AMPK, une protéine impliquée dans les interactions entre les cellules nourricières et les cellules germinales." Annales d'Endocrinologie 74, no. 4 (September 2013): 266. http://dx.doi.org/10.1016/j.ando.2013.07.097.
Perron, H. "La voie des rétrovirus humain endogènes, un espoir thérapeutique dans la schizophrénie." European Psychiatry 30, S2 (November 2015): S25. http://dx.doi.org/10.1016/j.eurpsy.2015.09.077.
Binart, Nadine. "Interactions du récepteur de la progestérone de l'oviducte de poulet avec la protéine de choc thermique hsp90." Biochimie 68, no. 1 (January 1986): 223–27. http://dx.doi.org/10.1016/s0300-9084(86)81087-2.
Дисертації з теми "Interactions protéine – protéine (IPP)":
Alleman, Cécile. "Accès synthétique au châssis [5-8-5] de la fusicoccine-A pour la synthèse d’analogues simplifiés en vue d'étudier les interactions protéine-protéine." Electronic Thesis or Diss., Université de Rennes (2023-....), 2023. http://www.theses.fr/2023URENS090.
In biological media, protein-protein interactions (PPI) are of huge importance, as they allow the regulation of many cellular events. PPI classically involve two partners: an adapter protein and its effector protein(s) regulated either in a positive or a negative manner. Inhibition of PPI has thus been considered as a solid therapeutic approach. On the other hand, stabilization of PPI remains scarcely investigated, but may lead to new promising approaches. This project focuses on the 14-3-3 family adapter protein which interacts with more than 200 protein partners. Among them, p53 protein is subjected to a lot of studies as this tumor suppressor protein regulates multiple biological processes (DNA repair, apoptosis). However, those major functions appear to be silenced in most cancer cases, thus allowing tumor cells proliferation. Some studies have shown that stabilization of the 14-3-3/p53 pair with the help of a molecular glue permitted to restore tumor suppressor activity of p53. Among the examined molecular glues, the fusicoccin-A (FC-A) natural product is shown to lodge in the valley formed by 14-3-3 and increases stabilization of the 14-3-3/p53 interaction. In this context, to enlarge the p53/14-3-3 molecular glue library, this project focuses on the access to simplified FC-A analogs through the synthesis of tricyclic scaffold. [6-8-5] analogs from an aromatic substrate are envisaged, as well as [5-8-5] analogs from a cyclopentane derivative, closer to the target structure. Various strategies have been explored in order to access these analogs
Kuenemann, Mélaine. "Etude de l'espace chimique des modulateurs d'interactions protéine-protéine et leurs applications en chimie biologie." Sorbonne Paris Cité, 2015. http://www.theses.fr/2015USPCC215.
Protein-protein interactions (PPI) represent a wealth of potential therapeutic targets. However targeting them with synthetic compounds represent a major challenge. The aim of this thesis was to find a way to overcome these challenges by studying the physicochemical profile of PPI inhibitors (aka chemical space). We firstly manually collected structures, pharmacological and physicochemical profiles of inhibitors of PPI (iPPI) in a database named iPPI-DB. Then, we identified new iPPI properties to favour and that did not preclude further drug development. Indeed, 4 descriptors were found specific to iPPI and that do not rely on the hydrophobicity and on the size. They represent either the 3D shape of the compounds or the distribution of their hydrophobic/hydrophilic interacting regions. This opens new ways to design and select iPPI. In a second analysis, we further validated these properties on larger datasets and address the disparity between PPI families. We could demonstrate that comparable classes of PPI targets can identified using separately their target- or their ligand-space. This analysis may help to prioritize the desired physicochemical properties of iPPI using class-specific profiles. Finally, using a combination virtual screening and cell viability assay, we were able to identify 6 compounds that inhibit the interaction between TRAIL and DR5 implied in HIV (human immunodeficiency virus)
Chamoun, Jean. "Contribution du couplage CE-ICP/MS dans l'étude des interactions métals-protéine non-covalentes." Université Louis Pasteur (Strasbourg) (1971-2008), 2005. http://www.theses.fr/2005STR13090.
The screening of metal/protein interactions using CE coupled to ICP/MS was investigated. The development of this new analytical tool requires, besides the hyphenation of the two techniques, both an efficient separation of the proteins and a sensitive detection of metals. The optimization of the electrophoretic separation of a protein-test mixture led to the use of a borate buffer, pH 9. 2, which both minimizes adsorption and allows the separation of all proteins’ mixture with a good migration times reproducibility. The hyphenation between capillary electrophoresis and ICP/MS was performed using a sheath flow interface. The optimization of parameters, such as coolant, auxiliary and nebulizer gases, composition and flowrate of the sheath flow solution and position of the capillary in the nebulizer was carried out in order to obtain the best detection sensitivity and separation efficiency. However, this type of interface involves important samples dilutions, which led us to develop an on-line preconcentration technique in order to improve the detection limits. The detection limits calculated for the copper and zinc contained in the carbonic anhydrase, the less efficiently concentrated protein, showed an improvement of the detection limits in CE-ICP/MS of 6 times for copper and 5 times for zinc. CE-ICP/MS was then used in the study of the interactions of three transition metals (Cd, Co and Ni) with a mixture of proteins made of metalloproteins and major blood serum proteins. These studies revealed a similar behavior of cobalt and nickel, completely different from that of cadmium. In the case of the metalloproteins, hyphenated CE-ICP/MS allowed to identify the probable nature of the interaction sites. Moreover, this method allowed studies on the relative affinity of various metals with a mixture of proteins. The dissociative aspect of the separation was also exploited in order to obtain kinetic data which allowed the access to the dissociation constants of the complexes and in certain cases, highlighted the presence of multiple interaction sites. Finally, the technique was applied to so-called “hard cations”: lanthanides and uranyl ion (UO22+). The first results showed a massive adsorption of these cations on the capillaries surface. Nevertheless, the studies, carried out on a mixture of six proteins, previously identified as uranium-targets, showed that four of them interact with the uranium, among which albumin and transferrin
Becker, Emmanuelle. "Prédictions bioinformatiques des propriétés des domaines de reconnaissance peptidique." Phd thesis, Université Pierre et Marie Curie - Paris VI, 2007. http://tel.archives-ouvertes.fr/tel-00553471.
Pinet, Louise. "Structural and functional investigation of the C-terminal intrinsically disordered fragment of ErbB2." Thesis, Université Paris-Saclay (ComUE), 2019. http://www.theses.fr/2019SACLS375/document.
ErbB2/HER2 is a receptor tyrosine kinase of the EGFR (ErbB1) family overexpressed in 20% of breast cancers and associated to a particularly aggressive form of the disease. ErbB receptors are only active upon dimerization that enables phosphorylation of their C-terminal tail by their tyrosine kinase domain. Phosphorylation then triggers interaction with adaptor proteins and activation of signaling pathways, mainly Ras/MAPK and Akt/PI3K. Those pathways control cell proliferation, motility and resistance to apoptosis. Contrary to ErbB1/3/4, ErbB2 can dimerize without any ligand. Understanding other mechanisms of regulation of its tyrosine phosphorylation and of its interactions is thus particularly interesting.ErbB2 structure and function have been extensively studied. This has led to the development of several FDA-approved targeted drugs, that are effective but to which resistance occurs, amongst which the Trastuzumab antibody that targets ErbB2 extracellular domain. The C-terminal tail of ErbB2 (CtErbB2) has been widely ignored in these studies. Since it is intrinsically disordered, the concepts and tools to study it have only emerged in the last few years.In the present work, I have performed the structural and dynamic study of CtErbB2. I showed that despite its lack of any stable structure, this proline-rich region exhibits several transient secondary structures and a long-range contact that might participate in the regulation of its intra- and inter-molecular interactions. Then, I characterized the adaptor protein Grb2, which is a partner of ErbB2 that is essential for the activation of the MAPK pathway. The solution organization of the domains of this modular protein in its apo-form was unknown so far. I also studied the interaction between Grb2 and CtErbB2, showing that in addition to the known SH2-phosphotyrosine interaction, a polyproline motif of CtErbB2 binds to the N-terminal SH3 domain of Grb2. Finally, I implemented several strategies to phosphorylate CtErbB2 tyrosines, to study more extensively the effect of phosphorylation on the whole tail
Boudoukha, Selim. "Étude de la régulation post-transcriptionnelle de l’expression des gènes par la protéine de liaison à l’ARN IMP-2 au cours de la myogenèse." Thesis, Paris 11, 2011. http://www.theses.fr/2011PA11T095/document.
The RNA-binding proteins IMPs (IGF-II mRNA binding protein) first discovered in rhabdomyosarcoma cells (RMS) are expressed during embryonic development but their expression is decreased in adult tissues.We showed that IMPs and particularly IMP-2 are strongly expressed in mouse myoblatsts, during early regeneration of skeletal muscle in vivo and in and RMS. IMP-2 loss of function experiments using siRNA have shown that IMP-2 is necessary for microtubules stability(MTs), cell motility and invasion of myoblasts and RMS.Expression of IMP-2 specifically increases MTs stability by an enrichment of detyrosinated tubulin Glu-tubulin. Detyrosination is indispensable for myogenic differentiation and plays substantial role in tumor growth. Additionaly, MTs stabilization play an important role in focal adhesion remodeling, in cytoskeleton integrity, cell adhesion and cell motility.To get new insight into molecular mechanism underlying the function of IMP-2 in MTs stability and cell motility, full ranscriptome analysis was performed between IMP-2 knockdown (KD) myoblasts and control myoblatsts. We have further shown that IMP-2 controls the mRNA levels of many important mediators of cell adhesion such as PINCH-2, as well as multiple cytoskeleton remodeling, such as MuRF-3.We have identified a number of functionally relevant protein partners of IMP-2.Moreover subsequent RNAi screens have revealed the importance of IMP-2 regulated transcripts involved in cell motility and cell adhesion In conclusion, we show that IMP-2 dependent regulation of mRNA such as MuRF3 and PINCH2 largely contributes to the motility –deficient in IMP-2 KD cells. Moreover these results indicate clearly, that further analysis of IMP2 protein partners and RNA targets regulated by IMP-2 will help to characterized the function of IMP-2 and to propose a model of IMP-2 transcriptional regulation of gene expression in myoblasts and RMS cells
Milhas, Sabine. "Développement d'outils pour l'étude des interactions protéine-protéine." Thesis, Aix-Marseille, 2016. http://www.theses.fr/2016AIXM4020.
In my thesis I became interested in protein-protein interactions (PPI's). PPI's play a major role in a variety of cellular processes and are now considered a major target in order to develop new drugs. However, targeting such interactions requires the development of dedicated libraries, to accelerate the discovery of “hits”molecules .To overcome this issue, a focused chemical library PPI (2P2I3D) was designed in the laboratory.At first, I evaluated this chemical library on different complexes with diverse interfaces. The results showed higher hit rate to those obtained with non-oriented libraries, from 0.2 to 1.6% against 0.01 to 0.1%, respectively. This study has established a proof of concept of the feasibility of creating a focused chemical library PPI, thus accelerating the discovery of biologically active compounds.Secondly, I am interested in the interaction between two major proteins of dengue virus: the NS3 and NS5 proteins. I initially identified and characterized a novel interaction site, which allowed me to demonstrate that this interaction had the effect of increasing the enzymatic activity of the helicase domain. I searched and identified small molecules able to inhibit this interaction. The different characterizations helped to highlight an antiviral effect. These inhibitors are an excellent starting point to further explore the biological role of this complex
Herrada, Isaline. "Etude des interactions protéine-protéine à l'enveloppe nucléaire." Thesis, Université Paris-Saclay (ComUE), 2015. http://www.theses.fr/2015SACLS278/document.
During my PhD, several papers revealed that the inner nuclear membrane (INM) proteins, andespecially emerin, lamin A, SUN1, actin and BAF, played an essential role in the mechanicalproperties of the nucleus and the cell. The nuclear envelope assembly and the interactions betweenthese proteins are regulated by phosphorylation and oligomerization events. My aim was to describemolecular events essential for inner nuclear envelope assembly as a first step to understand how thenuclear envelope responds to a mechanical stress.I first characterized the oligomerization and phosphorylation states of the protein emerin. I showedthat this protein is capable of forming, in vitro and in cells, large oligomers essential to its interactionwith lamin A. I also observed that several emerin mutations leading to Emery-Dreifuss musculardystrophy impaired the self-association properties of this protein.In parallel, I studied the interactions between emerin, lamin, SUN1, actin and BAF in vitro. I was ableto demonstrate direct interactions between the C-terminal domain of lamin A and the proteins emerin,actin and SUN1. These three proteins bind lamin A on different surfaces suggesting the existence ofcomplexes of 3 or 4 proteins in the cell. Analysis of the mechanisms regulating interactions betweenthese proteins should be pursued in order to understand what are the molecular events responsible forthe maintenance of nuclear integrity and the transmission of a mechanical signal between thecytoskeleton and the nucleoskeleton
Lugari, Adrien. "Spécificité et inhibition des interactions protéine-protéine : Exemples d'approches." Thesis, Aix-Marseille 1, 2011. http://www.theses.fr/2011AIX10210.
Protein-protein interactions (PPIs) participate in and regulate almost all essential cellular functions. As a consequence, they are frequently involved in various pathologies (going from cancer development to viral replication and host cell infection) but their study remains a challenge.Thus understanding those interactions as well as finding small drug candidates able to modulate them, a field of research not currently fully developed, appear as the future of the healthcare industry.In this context, I chose to learn different techniques to study PPIs that are usually employed in academic (IMR laboratory, CNRS, France) or corporate environments (Genentech, USA). Moreover, I also worked on the development of small organic inhibitors of PPIs coupling in silico methodologies (chemo-informatics, Drug Design) to biological and structural validations.During my PhD, I could manage and work on different projects involving the study of PPIs involved in cancer signaling pathways as well as the development of potent antiviral drugs targeting the HIV and SARS viruses.My organizational, personal and scientific skills as well as the practical experience I developed on various techniques (from cell biology to biophysics, structural biochemistry and Drug Design), make me feel confident on the management of PPIs drug discovery projects.I am thus able to efficiently work on, and manage, the study of protein-protein interactions in various pathologies as well as the development of potent PPIs inhibitors, that will be a major breakthrough for Biotech/Pharma companies in the coming years
Costenaro, Lionel. "Interactions faibles protéine – protéine en solution : La malate déshydrogénase halophile." Phd thesis, Université Joseph Fourier (Grenoble), 2001. http://tel.archives-ouvertes.fr/tel-00007698.
Dans quelle mesure les interactions protéine – solvant influencent-elles les interactions protéine – protéine ? Nous avons mis en relation ces deux types d'interactions pour la malate déshydrogénase (Hm MalDH) de Haloarcula marismortui, protéine halophile très acide qui a des solvatations variées et très riches en eau et en sel.
Nous avons développé une nouvelle méthode de détermination du second coefficient du viriel A2 par la modélisation des profils de vitesse de sédimentation en ultracentrifugation analytique, qui permet l'étude de solvants complexes.
Les interactions protéine – protéine de la Hm MalDH en divers sels ont été caractérisées par diffusion de neutrons ou de rayons X aux petits angles. Les A2 et les facteurs de structure en solution ont été modélisés par des potentiels d'interaction de type DLVO. Les interactions répulsives sont principalement dues au terme de volume exclu et dans une moindre mesure au terme électrostatique. Les interactions attractives sont qualitativement corrélées à des valeurs positives ou négatives des paramètres d'interaction préférentielle avec le sel. Ces résultats permettent d'expliquer l'adaptation moléculaire des protéines halophiles qui doivent ainsi avoir une solvatation riche en sel pour rester soluble à haut sel.
La cristallisation par dilution de la Hm MalDH dans des mélanges sel – MPD (méthyl-2-pentanediol-2,4) résulte d'une lente évolution des interactions protéine – protéine, de répulsives à modérément attractives. Le MPD modifie les interactions protéine – protéine en divers sels en ajoutant une attraction qui est liée à la répulsion du MPD par les charges de la protéine.
Книги з теми "Interactions protéine – protéine (IPP)":
Symposium on Dynamic Interactions of Myelin Proteins (1989 Chicago, Ill.). Dynamic interactions of myelin proteins: Proceedings of a Symposium on Dynamic Interactions of Myelin Proteins, held in Chicago, Illinois, April 5-10, 1989. Edited by Hashim George A and Moscarello Mario. New York: Wiley-Liss, 1990.
Saluz, H. P. A laboratory guide for in vivo studies of DNA methylation and protein/DNA interactions. Basel: Birkhäuser Verlag, 1990.
Nussinov, Ruth, and Gideon Schreiber. Computational Protein-Protein Interactions. Taylor & Francis Group, 2017.
Nussinov, Ruth, and Gideon Schreiber. Computational Protein-Protein Interactions. Taylor & Francis Group, 2009.
Nussinov, Ruth, and Gideon Schreiber. Computational Protein-Protein Interactions. Taylor & Francis Group, 2009.
Hirata, Fumio. Exploring Life Phenomena with Statistical Mechanics of Molecular Liquids. Taylor & Francis Group, 2020.