Relevant bibliographies by topics / Domaine SH2

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Academic literature on the topic 'Domaine SH2'

Author: Grafiati
Published: 4 June 2021
Last updated: 16 February 2022

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Journal articles on the topic "Domaine SH2"

1

Panchamoorthy, G., T. Fukazawa, L. Stolz, G. Payne, K. Reedquist, S. Shoelson, Z. Songyang, L. Cantley, C. Walsh, and H. Band. "Physical and functional interactions between SH2 and SH3 domains of the Src family protein tyrosine kinase p59fyn." Molecular and Cellular Biology 14, no. 9 (September 1994): 6372–85. http://dx.doi.org/10.1128/mcb.14.9.6372.

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The Src family protein tyrosine kinases participate in signalling through cell surface receptors that lack intrinsic tyrosine kinase domains. All nine members of this family possess adjacent Src homology (SH2 and SH3) domains, both of which are essential for repression of the enzymatic activity. The repression is mediated by binding between the SH2 domain and a C-terminal phosphotyrosine, and the SH3 domain is required for this interaction. However, the biochemical basis of functional SH2-SH3 interaction is unclear. Here, we demonstrate that when the SH2 and SH3 domains of p59fyn (Fyn) were present as adjacent domains in a single protein, binding of phosphotyrosyl peptides and proteins to the SH2 domain was enhanced, whereas binding of a subset of cellular polypeptide ligands to the SH3 domain was decreased. An interdomain communication was further revealed by occupancy with domain-specific peptide ligands: occupancy of the SH3 domain with a proline-rich peptide enhanced phosphotyrosine binding to the linked SH2 domain, and occupancy of the SH2 domain with phosphotyrosyl peptides enhanced binding of certain SH3-specific cellular polypeptides. Second, we demonstrate a direct binding between purified SH2 and SH3 domains of Fyn and Lck Src family kinases. Heterologous binding between SH2 and SH3 domains of closely related members of the Src family, namely, Fyn, Lck, and Src, was also observed. In contrast, Grb2, Crk, Abl, p85 phosphatidylinositol 3-kinase, and GTPase-activating protein SH2 domains showed lower or no binding to Fyn or Lck SH3 domains. SH2-SH3 binding did not require an intact phosphotyrosine binding pocket on the SH2 domain; however, perturbations of the SH2 domain induced by specific high-affinity phosphotyrosyl peptide binding abrogated binding of the SH3 domain. SH3-SH2 binding was observed in the presence of proline-rich peptides or when a point mutation (W119K) was introduced in the putative ligand-binding pouch of the Fyn SH3 domain, although these treatments completely abolished the binding to p85 phosphatidylinositol 3-kinase and other SH3-specific polypeptides. These biochemical SH2-SH3 interactions suggest novel mechanisms of regulating the enzymatic activity of Src kinases and their interactions with other proteins.
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2

Panchamoorthy, G., T. Fukazawa, L. Stolz, G. Payne, K. Reedquist, S. Shoelson, Z. Songyang, L. Cantley, C. Walsh, and H. Band. "Physical and functional interactions between SH2 and SH3 domains of the Src family protein tyrosine kinase p59fyn." Molecular and Cellular Biology 14, no. 9 (September 1994): 6372–85. http://dx.doi.org/10.1128/mcb.14.9.6372-6385.1994.

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The Src family protein tyrosine kinases participate in signalling through cell surface receptors that lack intrinsic tyrosine kinase domains. All nine members of this family possess adjacent Src homology (SH2 and SH3) domains, both of which are essential for repression of the enzymatic activity. The repression is mediated by binding between the SH2 domain and a C-terminal phosphotyrosine, and the SH3 domain is required for this interaction. However, the biochemical basis of functional SH2-SH3 interaction is unclear. Here, we demonstrate that when the SH2 and SH3 domains of p59fyn (Fyn) were present as adjacent domains in a single protein, binding of phosphotyrosyl peptides and proteins to the SH2 domain was enhanced, whereas binding of a subset of cellular polypeptide ligands to the SH3 domain was decreased. An interdomain communication was further revealed by occupancy with domain-specific peptide ligands: occupancy of the SH3 domain with a proline-rich peptide enhanced phosphotyrosine binding to the linked SH2 domain, and occupancy of the SH2 domain with phosphotyrosyl peptides enhanced binding of certain SH3-specific cellular polypeptides. Second, we demonstrate a direct binding between purified SH2 and SH3 domains of Fyn and Lck Src family kinases. Heterologous binding between SH2 and SH3 domains of closely related members of the Src family, namely, Fyn, Lck, and Src, was also observed. In contrast, Grb2, Crk, Abl, p85 phosphatidylinositol 3-kinase, and GTPase-activating protein SH2 domains showed lower or no binding to Fyn or Lck SH3 domains. SH2-SH3 binding did not require an intact phosphotyrosine binding pocket on the SH2 domain; however, perturbations of the SH2 domain induced by specific high-affinity phosphotyrosyl peptide binding abrogated binding of the SH3 domain. SH3-SH2 binding was observed in the presence of proline-rich peptides or when a point mutation (W119K) was introduced in the putative ligand-binding pouch of the Fyn SH3 domain, although these treatments completely abolished the binding to p85 phosphatidylinositol 3-kinase and other SH3-specific polypeptides. These biochemical SH2-SH3 interactions suggest novel mechanisms of regulating the enzymatic activity of Src kinases and their interactions with other proteins.
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3

Richard, S., D. Yu, K. J. Blumer, D. Hausladen, M. W. Olszowy, P. A. Connelly, and A. S. Shaw. "Association of p62, a multifunctional SH2- and SH3-domain-binding protein, with src family tyrosine kinases, Grb2, and phospholipase C gamma-1." Molecular and Cellular Biology 15, no. 1 (January 1995): 186–97. http://dx.doi.org/10.1128/mcb.15.1.186.

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src family tyrosine kinases contain two noncatalytic domains termed src homology 3 (SH3) and SH2 domains. Although several other signal transduction molecules also contain tandemly occurring SH3 and SH2 domains, the function of these closely spaced domains is not well understood. To identify the role of the SH3 domains of src family tyrosine kinases, we sought to identify proteins that interacted with this domain. By using the yeast two-hybrid system, we identified p62, a tyrosine-phosphorylated protein that associates with p21ras GTPase-activating protein, as a src family kinase SH3-domain-binding protein. Reconstitution of complexes containing p62 and the src family kinase p59fyn in HeLa cells demonstrated that complex formation resulted in tyrosine phosphorylation of p62 and was mediated by both the SH3 and SH2 domains of p59fyn. The phosphorylation of p62 by p59fyn required an intact SH3 domain, demonstrating that one function of the src family kinase SH3 domains is to bind and present certain substrates to the kinase. As p62 contains at least five SH3-domain-binding motifs and multiple tyrosine phosphorylation sites, p62 may interact with other signalling molecules via SH3 and SH2 domain interactions. Here we show that the SH3 and/or SH2 domains of the signalling proteins Grb2 and phospholipase C gamma-1 can interact with p62 both in vitro and in vivo. Thus, we propose that one function of the tandemly occurring SH3 and SH2 domains of src family kinases is to bind p62, a multifunctional SH3 and SH2 domain adapter protein, linking src family kinases to downstream effector and regulatory molecules.
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Mayer, B. J., and D. Baltimore. "Mutagenic analysis of the roles of SH2 and SH3 domains in regulation of the Abl tyrosine kinase." Molecular and Cellular Biology 14, no. 5 (May 1994): 2883–94. http://dx.doi.org/10.1128/mcb.14.5.2883.

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We have used in vitro mutagenesis to examine in detail the roles of two modular protein domains, SH2 and SH3, in the regulation of the Abl tyrosine kinase. As previously shown, the SH3 domain suppresses an intrinsic transforming activity of the normally nontransforming c-Abl product in vivo. We show here that this inhibitory activity is extremely position sensitive, because mutants in which the position of the SH3 domain within the protein is subtly altered are fully transforming. In contrast to the case in vivo, the SH3 domain has no effect on the in vitro kinase activity of the purified protein. These results are consistent with a model in which the SH3 domain binds a cellular inhibitory factor, which in turn must physically interact with other parts of the kinase. Unlike the SH3 domain, the SH2 domain is required for transforming activity of activated Abl alleles. We demonstrate that SH2 domains from other proteins (Ras-GTPase-activating protein, Src, p85 phosphatidylinositol 3-kinase subunit, and Crk) can complement the absence of the Abl SH2 domain and that mutants with heterologous SH2 domains induce altered patterns of tyrosine-phosphorylated proteins in vivo. The positive function of the SH2 domain is relatively position independent, and the effect of multiple SH2 domains appears to be additive. These results suggest a novel mechanism for regulation of tyrosine kinases in which the SH2 domain binds to, and thereby enhances the phosphorylation of, a subset of proteins phosphorylated by the catalytic domain. Our data also suggest that the roles of the SH2 and SH3 domains in the regulation of Abl are different in several respects from the roles proposed for these domains in the closely related Src family of tyrosine kinases.
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Mayer, B. J., and D. Baltimore. "Mutagenic analysis of the roles of SH2 and SH3 domains in regulation of the Abl tyrosine kinase." Molecular and Cellular Biology 14, no. 5 (May 1994): 2883–94. http://dx.doi.org/10.1128/mcb.14.5.2883-2894.1994.

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We have used in vitro mutagenesis to examine in detail the roles of two modular protein domains, SH2 and SH3, in the regulation of the Abl tyrosine kinase. As previously shown, the SH3 domain suppresses an intrinsic transforming activity of the normally nontransforming c-Abl product in vivo. We show here that this inhibitory activity is extremely position sensitive, because mutants in which the position of the SH3 domain within the protein is subtly altered are fully transforming. In contrast to the case in vivo, the SH3 domain has no effect on the in vitro kinase activity of the purified protein. These results are consistent with a model in which the SH3 domain binds a cellular inhibitory factor, which in turn must physically interact with other parts of the kinase. Unlike the SH3 domain, the SH2 domain is required for transforming activity of activated Abl alleles. We demonstrate that SH2 domains from other proteins (Ras-GTPase-activating protein, Src, p85 phosphatidylinositol 3-kinase subunit, and Crk) can complement the absence of the Abl SH2 domain and that mutants with heterologous SH2 domains induce altered patterns of tyrosine-phosphorylated proteins in vivo. The positive function of the SH2 domain is relatively position independent, and the effect of multiple SH2 domains appears to be additive. These results suggest a novel mechanism for regulation of tyrosine kinases in which the SH2 domain binds to, and thereby enhances the phosphorylation of, a subset of proteins phosphorylated by the catalytic domain. Our data also suggest that the roles of the SH2 and SH3 domains in the regulation of Abl are different in several respects from the roles proposed for these domains in the closely related Src family of tyrosine kinases.
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Tian, M., and G. S. Martin. "The role of the Src homology domains in morphological transformation by v-src." Molecular Biology of the Cell 8, no. 7 (July 1997): 1183–93. http://dx.doi.org/10.1091/mbc.8.7.1183.

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The Src homology (SH2 and SH3) domains of v-Src are required for transformation of Rat-2 cells and for wild-type (morphr) transformation of chicken embryo fibroblasts (CEFs). We report herein that the N-terminal domains of v-Src, when expressed in trans, cannot complement the transformation defect of a deletion mutant lacking the "unique," SH3, and SH2 regions. However, the same regions of Src can promote transformation when translocated to the C terminus of v-Src, although the transformation of CEFs is somewhat slower. We conclude that the SH3 and SH2 domains must be present in cis to the catalytic domain to promote transformation but that transformation is not dependent on the precise intramolecular location of these domains. In CEFSs and in Rat-2 cells, the expression of wild-type v-Src results in tyrosine phosphorylation of proteins that bind to the v-Src SH3 and SH2 domains in vitro; mutations in the SH2 or SH3 and SH2 domains prevent the phosphorylation of these proteins. These findings are most consistent with models in which the SH3 and SH2 domains of v-Src directly or indirectly target the catalytic domain to substrates involved in transformation. However, the N-terminal domains of v-Src can promote tyrosine phosphorylation of certain proteins, in particular p130Cas, even when expressed in the absence of the catalytic domain, indicating that the N-terminal domains of v-Src have effects that are independent of the catalytic domain.
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DeBell, Karen E., Bogdan A. Stoica, Maria-Concetta Verí, Angela Di Baldassarre, Sebastiano Miscia, Laurie J. Graham, Barbara L. Rellahan, Masamichi Ishiai, Tomohiro Kurosaki, and Ezio Bonvini. "Functional Independence and Interdependence of the Src Homology Domains of Phospholipase C-γ1 in B-Cell Receptor Signal Transduction." Molecular and Cellular Biology 19, no. 11 (November 1, 1999): 7388–98. http://dx.doi.org/10.1128/mcb.19.11.7388.

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ABSTRACT B-cell receptor (BCR)-induced activation of phospholipase C-γ1 (PLCγ1) and PLCγ2 is crucial for B-cell function. While several signaling molecules have been implicated in PLCγ activation, the mechanism coupling PLCγ to the BCR remains undefined. The role of PLCγ1 SH2 and SH3 domains at different steps of BCR-induced PLCγ1 activation was examined by reconstitution in a PLCγ-negative B-cell line. PLCγ1 membrane translocation required a functional SH2 N-terminal [SH2(N)] domain, was decreased by mutation of the SH3 domain, but was unaffected by mutation of the SH2(C) domain. Tyrosine phosphorylation did not require the SH2(C) or SH3 domains but depended exclusively on a functional SH2(N) domain, which mediated the association of PLCγ1 with the adapter protein, BLNK. Forcing PLCγ1 to the membrane via a myristoylation signal did not bypass the SH2(N) domain requirement for phosphorylation, indicating that the phosphorylation mediated by this domain is not due to membrane anchoring alone. Mutation of the SH2(N) or the SH2(C) domain abrogated BCR-stimulated phosphoinositide hydrolysis and signaling events, while mutation of the SH3 domain partially decreased signaling. PLCγ1 SH domains, therefore, have interrelated but distinct roles in BCR-induced PLCγ1 activation.
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Sipeki, Szabolcs, Kitti Koprivanacz, Tamás Takács, Anita Kurilla, Loretta László, Virag Vas, and László Buday. "Novel Roles of SH2 and SH3 Domains in Lipid Binding." Cells 10, no. 5 (May 13, 2021): 1191. http://dx.doi.org/10.3390/cells10051191.

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Signal transduction, the ability of cells to perceive information from the surroundings and alter behavior in response, is an essential property of life. Studies on tyrosine kinase action fundamentally changed our concept of cellular regulation. The induced assembly of subcellular hubs via the recognition of local protein or lipid modifications by modular protein interactions is now a central paradigm in signaling. Such molecular interactions are mediated by specific protein interaction domains. The first such domain identified was the SH2 domain, which was postulated to be a reader capable of finding and binding protein partners displaying phosphorylated tyrosine side chains. The SH3 domain was found to be involved in the formation of stable protein sub-complexes by constitutively attaching to proline-rich surfaces on its binding partners. The SH2 and SH3 domains have thus served as the prototypes for a diverse collection of interaction domains that recognize not only proteins but also lipids, nucleic acids, and small molecules. It has also been found that particular SH2 and SH3 domains themselves might also bind to and rely on lipids to modulate complex assembly. Some lipid-binding properties of SH2 and SH3 domains are reviewed here.
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Tu, Yizeng, Fugang Li, and Chuanyue Wu. "Nck-2, a Novel Src Homology2/3-containing Adaptor Protein That Interacts with the LIM-only Protein PINCH and Components of Growth Factor Receptor Kinase-signaling Pathways." Molecular Biology of the Cell 9, no. 12 (December 1998): 3367–82. http://dx.doi.org/10.1091/mbc.9.12.3367.

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Many of the protein–protein interactions that are essential for eukaryotic intracellular signal transduction are mediated by protein binding modules including SH2, SH3, and LIM domains. Nck is a SH3- and SH2-containing adaptor protein implicated in coordinating various signaling pathways, including those of growth factor receptors and cell adhesion receptors. We report here the identification, cloning, and characterization of a widely expressed, Nck-related adaptor protein termed Nck-2. Nck-2 comprises primarily three N-terminal SH3 domains and one C-terminal SH2 domain. We show that Nck-2 interacts with PINCH, a LIM-only protein implicated in integrin-linked kinase signaling. The PINCH-Nck-2 interaction is mediated by the fourth LIM domain of PINCH and the third SH3 domain of Nck-2. Furthermore, we show that Nck-2 is capable of recognizing several key components of growth factor receptor kinase-signaling pathways including EGF receptors, PDGF receptor-β, and IRS-1. The association of Nck-2 with EGF receptors was regulated by EGF stimulation and involved largely the SH2 domain of Nck-2, although the SH3 domains of Nck-2 also contributed to the complex formation. The association of Nck-2 with PDGF receptor-β was dependent on PDGF activation and was mediated solely by the SH2 domain of Nck-2. Additionally, we have detected a stable association between Nck-2 and IRS-1 that was mediated primarily via the second and third SH3 domain of Nck-2. Thus, Nck-2 associates with PINCH and components of different growth factor receptor-signaling pathways via distinct mechanisms. Finally, we provide evidence indicating that a fraction of the Nck-2 and/or Nck-1 proteins are associated with the cytoskeleton. These results identify a novel Nck-related SH2- and SH3-domain–containing protein and suggest that it may function as an adaptor protein connecting the growth factor receptor-signaling pathways with the integrin-signaling pathways.
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Kazemein Jasemi, Neda S., Christian Herrmann, Eva Magdalena Estirado, Lothar Gremer, Dieter Willbold, Luc Brunsveld, Radovan Dvorsky, and Mohammad R. Ahmadian. "The intramolecular allostery of GRB2 governing its interaction with SOS1 is modulated by phosphotyrosine ligands." Biochemical Journal 478, no. 14 (July 23, 2021): 2793–809. http://dx.doi.org/10.1042/bcj20210105.

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Growth factor receptor-bound protein 2 (GRB2) is a trivalent adaptor protein and a key element in signal transduction. It interacts via its flanking nSH3 and cSH3 domains with the proline-rich domain (PRD) of the RAS activator SOS1 and via its central SH2 domain with phosphorylated tyrosine residues of receptor tyrosine kinases (RTKs; e.g. HER2). The elucidation of structural organization and mechanistic insights into GRB2 interactions, however, remain challenging due to their inherent flexibility. This study represents an important advance in our mechanistic understanding of how GRB2 links RTKs to SOS1. Accordingly, it can be proposed that (1) HER2 pYP-bound SH2 potentiates GRB2 SH3 domain interactions with SOS1 (an allosteric mechanism); (2) the SH2 domain blocks cSH3, enabling nSH3 to bind SOS1 first before cSH3 follows (an avidity-based mechanism); and (3) the allosteric behavior of cSH3 to other domains appears to be unidirectional, although there is an allosteric effect between the SH2 and SH3 domains.
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Dissertations / Theses on the topic "Domaine SH2"

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Hardré-Liénard, Hélène. "Régulation de l'activation cellulaire par les phosphatases à domaine SH2." Paris, Muséum national d'histoire naturelle, 2001. http://www.theses.fr/2001MNHN0004.

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Dorey, Karel. "Mecanismes moleculaires de la regulation de c-abl, une tyrosine kinase a domaine sh2 et sh3." Paris 6, 2001. http://www.theses.fr/2001PA066078.

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La tyrosine kinase de type non-recepteur c-abl est exprimee ubiquitairement chez tous les metazoaires. En plus de son domaine catalytique, c-abl possede des domaines d'interaction proteine-proteine qui sont essentiels pour sa fonction. Si la fonction precise de c-abl est inconnue, elle est impliquee dans une grande variete de processus. L'inactivation du gene a un phenotype pleiotropique conduisant a une mort embryonnaire precoce. L'activation constitutive de c-abl la transforme en un oncogene puissant implique dans des leucemies humaines. Il est donc vital pour la cellule de reguler de maniere extremement precise son activite catalytique. Au cours de ce travail de these, nous avons etudie les mecanismes moleculaires regulant c-abl. La tyr 412 est situee dans la boucle d'activation du domaine catalytique de c-abl. Ce residu est au cur du mecanisme de regulation de l'activite catalytique de c-abl. Son positionnement a l'interieur du domaine catalytique est essentiel au maintien de la forme inactive de c-abl. La phosphorylation de la tyr 412 est requise pour activer l'enzyme. La tyr 412 est un site de trans-autophosphorylation qui permet une boucle d'amplification du signal. Une particularite de la regulation de c-abl est le role d'un domaine de 80 acides amines situe en n-terminal de la molecule et contenant le site de myristoylation. Il interagit de maniere intramoleculaire avec le reste de la molecule. Cette interaction est necessaire pour la regulation de c-abl. Le point commun des formes oncogeniques de c-abl est l'absence de ce domaine. La deletion de ce domaine suffit a rendre c-abl oncogenique. C'est peut-etre la que reside la difference fondamentale entre la forme sauvage et les formes oncogeniques d'abl. L'activite catalytique de c-abl est donc sous le controle d'une combinaison de facteurs -interactions intramoleculaires, interactions proteine-proteine, evenement de phosphorylation- qui permettent d'assurer une reponse appropriee a un stimulus donne.
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Courme, Caroline. "Conception de novo et synthèse de ligands non peptidiques potentiels du domaine SH2 de Grb2." Paris 5, 2008. http://www.theses.fr/2008PA05P605.

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Grb2 est une protéine adaptatrice qui intervient dans plusieurs voies de signalisation mitogéniques. Elle est constituée de deux domaines SH3 et d’un domaine SH2, ce dernier reconnaissant les phosphotyrosines situées dans la partie intracellulaire des récepteurs à tyrosine kinase activés. Ces voies contrôlent divers processus comme la prolifération et la survie cellulaire et sont impliquées dans les cancers du sein (Ras/MAPK) et du rein (HGF/cMet). Depuis plus d’une décennie, plusieurs groupes de recherche se sont intéressés à l’inhibition de Grb2, qui ouvrirait de nouvelles perspectives en oncologie. La co-cristallisation de Grb2 avec un de ses ligands endogènes, Bcr-Abl, a permis de définir les pharmacophores essentiels à la reconnaissance par la protéine. De nombreux inhibiteurs peptidiques ou peptidomimétiques ont été développés mais très peu d’inhibiteurs non-peptidiques ont été décrits jusqu’à présent. C’est dans ce contexte que s’est inséré notre programme de recherche, en partant des structures de deux ligands de référence : un peptide développé par l’équipe de C. Garbay et un thiazole non-peptidique développé par Novartis, à trois et deux pharmacophores, respectivement. Nous décrivons dans cette thèse la conception de novo et la synthèse multi-étapes de ligands non﷓peptidiques potentiels de Grb2-SH2. Des composés originaux basés sur les sous-structures dites privilégiées 2-anilinopyrimidine et triazine ont été conçus à partir de la structure cristallographique de Grb2-SH2 avec le peptide de Garbay et coll. De plus, une stratégie de synthèse d’analogues du ligand de Novartis a été développée en exploitant la structure triazine via la chimie ‘click’
Grb2 is an adaptor protein involved in several mitogenic signaling pathways. It consists of two SH3 domains and one SH2 domain, the latter recognizing phosphotyrosines located in the intracellular part of activated tyrosine kinase receptors. These pathways control various processes such as cell proliferation and survival and are involved in the development of breast cancer (Ras/MAPK) and kidney cancer (HGF/cMet). For over a decade, several research groups have been interested in Grb2 inhibition, which could open new perspectives in oncology. The co-crystallization of Grb2 with one of its endogenous ligands, Bcr-Abl, permitted the identification of key pharmacophores for protein recognition. Many peptidic or peptidomimetic inhibitors have been developed but very few non-peptidic inhibitors have been described until today. In this context, we have based our research program on the structure of two reference ligands: a peptide developed by the team of C. Garbay and a non-peptidic thiazole developed by Novartis, with three and two pharmacophores, respectively. We have described in this PhD the de novo design and multi-step synthesis of potential Grb2-SH2 non-peptidic inhibitors. Novel compounds based on 2-anilinopyrimidine and triazine ‘privileged’ scaffolds have been designed using the X-ray structure of Grb2-SH2 co-crystallized with the peptide developed by the team of Garbay. Furthermore, a synthesis strategy has been developed to prepare analogs of Novartis’ ligand, using the triazine scaffold via ‘click’ chemistry
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Leroux, Vincent Maigret Bernard. "Modélisation d'inhibiteurs du domaine SH2 de la protéine Grb2 par dynamique moléculaire, docking et criblage virtuel." [S.l.] : [s.n.], 2006. http://www.scd.uhp-nancy.fr/docnum/SCD_T_2006_0220_LEROUX.pdf.

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Leroux, Vincent. "Modélisation d’inhibiteurs du domaine SH2 de la protéine Grb2 par dynamique moléculaire, docking et criblage virtuel." Nancy 1, 2006. http://docnum.univ-lorraine.fr/public/SCD_T_2006_0220_LEROUX.pdf.

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Ce manuscrit constitue une étude théorique de l’inhibition de l’activité du domaine SH2 de la protéine Grb2 par la liaison de ligands. La première partie décrit le contexte de ce travail, qui se situe plus généralement à travers le ciblage de Grb2 SH2 parmi les multiples approches de lutte contre le cancer, de l’étude du vivant à l’échelle moléculaire (domaine interdisciplinaire par excellence), et, plus précisément, de la recherche pharmaceutique. La seconde partie s’emploiera à détailler les connaissances disponibles sur la cible au moment de débuter ce travail, en incluant les avancées qui sont apparues en parallèle à ce travail. On trouvera dans la troisième partie un résumé des principaux résultats obtenus au cours de cette thèse. Ceux-ci se classent selon trois approches méthodologiques distinctes : celle de la dynamique moléculaire, du docking et enfin du screening virtuel. On pourra constater que de nouvelles connaissances sur la nature physico-chimique de la liaison de certains ligands sur Grb2 SH2 sont mises en évidence dans le premier cas, tandis que les deux autres approches ont surtout donné naissance à des avancées méthodologiques.
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THOME, MARGOT. "Le role du domaine sh2 de la tyrosine kinase p561ck dans la transduction du signal via le recepteur de l'antigene des lymphocytes t." Paris 6, 1995. http://www.theses.fr/1995PA066739.

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Nous avons choisi une approche biochimique pour etudier le mecanisme par lequel la tyrosine kinase p56#l#c#k, et plus specifiquement son domaine sh2, contribue a la transduction du signal via le recepteur t (tcr) et les co-recepteurs cd4 ou cd8, au cours de l'activation des lymphocytes t. Lors de la reconnaissance de l'antigene par les cellules t, le tcr et la molecule cd4 (respectivement cd8) semblent interagir avec la meme molecule du cmh de classe ii (respectivement de classe i) pour former un complexe ternaire stable. La partie cytoplasmique de cd4 ou de cd8 est associee, de facon non covalente, avec la tyrosine kinase p56#l#c#k. En plus d'un domaine kinase, la p56#l#c#k comporte un domaine sh2 qui pourrait etre implique dans des interactions proteine-proteine via un residu tyrosine phosphoryle. Nous avons pu montrer que la p56#l#c#k se lie directement par son domaine sh2 a zap-70 et syk, deux tyrosine kinases homologues associees avec cd3/zeta, apres stimulation des cellules jurkat via le complexe tcr/cd3. De plus, un peptide phosphoryle sur une tyrosine, de sequence a priori optimale pour la liaison au domaine sh2 des tyrosine kinases de la famille src, entre en competition avec zap-70 ou syk pour leur liaison a la p56#l#c#k. Les interactions analogues, via sh2, entre zap-70 ou syk et cd3/zeta, ne sont pas affectees par ce peptide. Le meme peptide est capable d'inhiber l'association du tcr avec cd4 ou cd8 induite par l'activation des cellules jurkat. Par ailleurs, la co-localisation de zap-70 et de cd4 est observee dans des lymphoblastes t humains apres stimulation via cd3. Ces resultats suggerent que l'interaction du domaine sh2 de la p56#l#c#k avec zap-70 ou syk, kinases phosphorylees liees a cd3/zeta, permet l'association de cd4 ou cd8 avec le complexe tcr/cd3/zeta au cours de la stimulation antigenique. Ainsi, ces co-recepteurs seraient recrutes activement par les quelques recepteurs t engages avec les races complexes mhc/ag specifiques, a la surface de la cellule presentatrice ; les processus de reconnaissance et de transduction du signal s'en trouveraient plus efficaces
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Lesourne, Renaud. "Bases moléculaires et cellulaires du recrutement des phosphatases à domaine SH2 par les RFcyIIB, des récepteurs pour la portion Fc des IgG inhibiteurs de l'activation cellulaire." Paris 5, 2004. http://www.theses.fr/2004PA05N13S.

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Les RFcyIIB sont des régulateurs négatifs de l'activation cellulaire induite par les récepteurs d'antigène. L'inhibition induite par ces récepteus dépend d'un motif intracytoplasmique, appelé ITIM. Lorsqu'il est phosphorylé, ce motif recrute des phosphatases qui sont les effecteurs de l'inhibition. In vitro, des peptides contenant l'ITIM phosphorylé des RFcyIIB se lient à deux types de phosphatases, les SHP et les SHIP. In vivo, les RFcyIIB phosphorylés recrutent sélectivement les SHIP. Ce travail a consisté à déterminer les bases fondamentales du recrutement sélectif des SHIP par les RFcyIIB. Il démontre, 1) que le degré de phosphorylation des RFcyIIB atteint dans des conditions mimant les situations physiologiques est insuffisant pour leur permettre de recruter les SHP, 2) que le cytosquelette d'actine est nécessaire à l'inbition induite par les RFcyIIB parce qu'il coordonne les interactions entre les SHIP et les RFcyIIB par l'intermédiaire d' une protéine, la filamine
FcyRIIB are negative regulators of cell activation induced by antigen receptors. The inhibition induced by these receptors depend on an intracytoplasmic motif, call ITIM. When phosphorylated, this motif is a docking site for phosphatases wich are the effectors of inhibition. In vitro, peptides containing the phosphorylated ITIM of FcyRIIB bind two types of phosphatases, the SHP and the SHIP. In vivo, phosphorylated FcyRIIB selectively recruit the SHP. This work consisted to determine the molecular and cellular bases of the selective recruitment of SHIP by FcyRIIB. It shows, 1) that the level of FcyRIIB phosphorylation reach under physiological conditions is insufficient for the recruitment of SHP-1 by these receptors, 2) that the F-actin cytoskeleton is necessary for FcyRIIB-depend inhibition because it coordinates the interactions between SHIP and FcyRIIBvia a protein called filamin
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Sweeney, Michael Cameron. "Synthetic combinatorial peptide libraries and their application in decoding biological interactions." Connect to resource, 2005. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=osu1118952919.

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Thesis (Ph. D.)--Ohio State University, 2005.
Title from first page of PDF file. Document formatted into pages; contains xv, 151 p.; also includes graphics. Includes bibliographical references (p. 134-151). Available online via OhioLINK's ETD Center
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Arnaud-Arnould, Mary. "Etude du rôle de la protéine adaptatrice p97/Gab2 dans la signalisation de l'interleukine-2 dans des lymphocytes T humains." Paris 11, 2003. http://www.theses.fr/2003PA112075.

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L'interleukine-2 (IL-2) est produite par les lymphocytes T activés et joue un rôle crucial dans les processus de prolifération, de différentiation en cellules effectrices et d'apoptose secondaire à l'activation. Ses fonctions biologiques reposent sur son interaction avec un récepteur membranaire composé de trois chaînes α, β et γc, dont seules β et γ sont nécessaires à la signalisation intracellulaire. Nous nous sommes intéressés à la signalisation précoce en réponse à l'IL-2 dans des lymphocytes T humains, et en particulier au rôle de la protéine adaptatrice plate-forme Gab2. Nous avons montré que cette protéine est tyrosine phosphorylée en réponse à l'IL-2 et qu'elle s'associe à différents partenaires possédant des domaines SH2 comme la tyrosine phosphatase SHP-2, la lipide kinase PI3K et la protéine adaptatrice CrkL. Nous avons choisi d'étudier plus particulièrement l'interaction Gab2/SHP-2. Nous avons montré que le recrutement et l'activation de SHP-2 via son interaction avec Gab2 sont nécessaires en amont de MEK pour l'activation de la voie Ras/ERK MAPK et permettent à SHP-2 une action en parallèle de la voie RhoA/SRF dans la régulation de l'expression du gène c-fos impliqué dans la prolifération cellulaire. Nous avons également montré que ERK est capable de phosphoryler Gab2 sur sa sérine 623. Cette phosphorylation entraîne une diminution de l'interaction Gab2/SHP-2 qui se traduit par une participation à l'inhibition de la voie ERK et une levée de l'inhibition exercée par l'activité phosphatase de SHP-2 sur STAT5, ce qui module la prolifération des lymphocytes. Ces résultats suggèrent l'implication du complexe Gab2/SHP-2 dans la régulation fine du processus de prolifération cellulaire en réponse à l'IL-2. Ces résultats permettent de mieux comprendre les mécanismes de contrôle de la prolifération des cellules leucémiques humaines et identifient la protéine Gab2 comme un élément régulateur central des voies de signalisation activées par l'IL-2
Interleukin-2 (IL-2) is a major growth factor for T lymphocytes which plays a critical role in cellular proliferation, differentiation and activation-induced cell death. The effects of IL-2 on its target cells are mediated through specific cell-surface receptors, which comprise three subunits α, β and γc. Only β and γc are required to trigger downstream signalling events. We were interested in early signalling events in response to IL-2 in human T lymphocytes and have studied the role of scaffolding adaptor protein Gab2. We report here that Gab2 becomes tyrosine-phosphorylated in response to IL-2 and forms multimolecular complexes with SH2 domain-containing partners such as the tyrosine phosphatase SHP-2, the lipid kinase PI3K and the adaptor protein CrkL. 8ince the role of SHP-2 in IL-2 signalling has not been fully elucidated, we investigated in details the function of Gab2/SHP-2 interaction. We have shown here that IL-2 activates SHP-2 via Gab2. Furthermore, SHP-2 appears to be required upstream of MEK in activation of the Ras/ERK pathway and in parallel to the RhoA/SRF pathway for c-fos promoter regulation and therefore cellular proliferation. Moreover, we have shown that ERK phosphorylates Gab2 on a consensus phosphorylation site, Ser 623. This phosphorylation downregulates the interaction between Gab2 and SRP-2 and consequently the activity of SHP-2, which modulates ERK and STAT5 activation. So, at the initiation of the response, Gab2-activated SHP-2 is required for ERK activation. At later time points, secondary to ERK-mediated phosphorylation of Gab2 S-623, decreased SHP-2 activity helps down-regulating ERK, and allows for STAT5 activation to persist. These results demonstrate that ERK-mediated phosphorylation of Gab2 S623 is involved in fine tuning the proliferative response of T-lymphocytes to IL-2. These results provide new insight on the control of human leukemic cell proliferation and on the critical role of Gab2 in IL-2 signal transduction
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Chandler, Brendan. "The SH2 Domain-Containing Adaptor Protein SHD Reversibly Binds the CRKL-SH2 Domain and Knockdown of shdb Impairs Zebrafish Eye Development." ScholarWorks @ UVM, 2018. https://scholarworks.uvm.edu/graddis/878.

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The adaptor protein CT10-Regulator of Kinase (CRK) and the closely related CRK-Like (CRKL) are adaptor proteins that play important roles in many signaling pathways regulating cell proliferation and cell motility. A notable example is their required role in Reelin signaling during development of the laminated structures of the vertebrate central nervous system, including the cerebral cortex, cerebellum, hippocampus, and retina. As adaptors, CRK/CRKL are important in coupling phosphotyrosine signaling to G protein activity to regulate both cell proliferation and changes in the actin cytoskeleton, thereby exerting control over cell motility, and migration. While many proteins that interact with CRK/CRKL have been identified, the diverse roles of these molecules suggest that more remain to be found. Herein is described a novel CRK/CRKL interacting protein, Src Homology 2 domain-containing protein D (SHD), which demonstrates a phosphorylation-dependent interaction with the CRK/CRKL SH2 domain in HEK 293 cells stimulated with hydrogen peroxide, which globally boosts tyrosine phosphorylation by inhibiting tyrosine phosphatases. Treatment with an inhibitor for Src family kinases (SFKs), Src-1, or an inhibitor of Abl/Arg kinases, STI571, reduces peroxide-induced binding of the CRKL-SH2 domain to SHD. We show that overexpression of Abl kinase, but not the SFK Fyn is sufficient to induce binding of the CRKL-SH2 to SHD and that this interaction requires at least one of the five tyrosines in YxxP motifs found in SHD. Using mass spectrometry, we found that Abl phosphorylates SHD on Y144, which is located in a YxxP motif. Mutation of this site to phenylalanine reduces, but does not prevent, Abl-induced binding of SHD to the CRKL-SH2 domain, suggesting that other YxxP sites also facilitate the interaction. A discussion of the cellular consequences of the interaction between SHD and CRK/CRKL is presented. To explore the biological role of SHD, we used the zebrafish to study shdb, a putative ortholog of human SHD. The expression of shdb was unknown and so we performed in situ hybridization and determined that shdb was expressed in the developing nervous system. To study the function of this gene, we used a morpholino to knock down expression of shdb which resulted in significantly reduced eye size. Possible roles of Shdb in eye development are discussed as is future research aimed to elucidate the cellular and developmental mechanisms by which Shdb functions in the developing eye.
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Books on the topic "Domaine SH2"

1

Machida, Kazuya, and Bernard A. Liu, eds. SH2 Domains. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-6762-9.

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Singer, Alex Uriel. Solution structure and electrostatic properties of an SH2 domain/phosphopeptide complex. Ottawa: National Library of Canada = Bibliothèque nationale du Canada, 1998.

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Ray, Avi Andrew. SH3 binding domains in the dopamine D(3) receptor. Ottawa: National Library of Canada, 1999.

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Fang wu chai qian shi wu. Beijing Shi: Fa lü chu ban she, 2002.

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Lambert, Véronique. The Adornes Domain and the Jerusalem Chapel in Bruges. Translated by Ian Connerty. NL Amsterdam: Amsterdam University Press, 2018. http://dx.doi.org/10.5117/9789462989924.

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Bruges, middle of the 15th century. Anselm Adornes, scion of a rich patrician family, creates a magnificent domain in the heart of the city : an elegant mansion, beautiful gardens, several charitable almshouses and the spectacular Chapel of Jerusalem. It is a place that every right-minded resident of Bruges and every tourist must see. The history of the Adornes domain is truly remarkable, remaining in the unbroken possession of the same family for six centuries. It has survived storms and setbacks, the secularism of the French Revolution, the fury of two world wars and inevitable periods of disinterest. 'In this book Véronique Lambert allows us to share in the hopes and fears, joys and sorrows, trials and tribulations that mark the milestones in the Adornes family saga. Within the boundaries of historical interpretation and based on extensive research, she unfolds a fascinating tale of ambitious adventurers, charismatic personalities, flamboyant lords and ordinary mortals, but each imbued with the family's traditional willpower and energy'. Let yourself be enchanted by this fascinating piece of our cultural heritage, which deserves to be more widely known.
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Ostachowicz, W. M. Guided waves in structures for SHM: The time-domain spectral element method. Chichester, West Sussex: Wiley, 2012.

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Xin de ban tu: Xing ai shi, chu qing = The heart domain. Beijing: Zuo jia chu ban she, 2006.

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Northey, Julian G. B. Protein folding determinants and transition state analysis of the Fyn SH3 domain. Ottawa: National Library of Canada, 2001.

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Si fa shi yu xia de Zhongguo zheng di bu chang: Sifa shiyuxia de Zhongguo zhengdi buchang. Beijing Shi: Ren min fa yuan chu ban she, 2011.

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Cheng shi de shang hen: Na xie cheng shi chai qian zhong de liu lang dong wu = The scar of the city. Beijing: Xin hua chu ban she, 2010.

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Book chapters on the topic "Domaine SH2"

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McCarty, Joseph H. "SH2/SH3 Domains." In Encyclopedia of Cancer, 3397–99. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-16483-5_5278.

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McCarty, Joseph H. "SH2/SH3 Domains." In Encyclopedia of Cancer, 1–3. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/978-3-642-27841-9_5278-2.

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McCarty, Joseph H. "SH2/SH3 Domains." In Encyclopedia of Cancer, 4201–3. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/978-3-662-46875-3_5278.

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Mayer, B. J., and R. Gupta. "Functions of SH2 and SH3 Domains." In Protein Modules in Signal Transduction, 1–22. Berlin, Heidelberg: Springer Berlin Heidelberg, 1998. http://dx.doi.org/10.1007/978-3-642-80481-6_1.

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Gopalasingam, Piraveen, Lee Quill, Mark Jeeves, and Michael Overduin. "SH2 Domain Structures and Interactions." In SH Domains, 159–85. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-20098-9_8.

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Buhs, Sophia, and Peter Nollau. "SH2 Domain Histochemistry." In Methods in Molecular Biology, 535–45. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-6762-9_31.

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Mishra, Jayshree, and Narendra Kumar. "Structure and Function of Jak3- SH2 Domain." In SH Domains, 209–27. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-20098-9_10.

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Mayer, Bruce J., and Kalle Saksela. "SH3 Domains." In Modular Protein Domains, 37–58. Weinheim, FRG: Wiley-VCH Verlag GmbH & Co. KGaA, 2005. http://dx.doi.org/10.1002/3527603611.ch2.

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Forman-Kay, Julie D., Steven M. Pascal, Alex U. Singer, Toshio Yamazaki, Ouwen Zhang, Neil A. Farrow, and Lewis E. Kay. "Structural, Dynamic, and Folding Studies of SH2 and SH3 Domains." In NMR as a Structural Tool for Macromolecules, 35–47. Boston, MA: Springer US, 1996. http://dx.doi.org/10.1007/978-1-4613-0387-9_3.

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Pawson, Tony, Gerald D. Gish, and Piers Nash. "The SH2 Domain: A Prototype for Protein Interaction Modules." In Modular Protein Domains, 5–36. Weinheim, FRG: Wiley-VCH Verlag GmbH & Co. KGaA, 2005. http://dx.doi.org/10.1002/3527603611.ch1.

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Conference papers on the topic "Domaine SH2"

1

Ongpeng, Jason Maximino C., Kenneth Guevarra, and Sohichi Hirose. "Air-coupled Nonlinear Ultrasonic Test for Reinforced Concrete Beams." In IABSE Conference, Kuala Lumpur 2018: Engineering the Developing World. Zurich, Switzerland: International Association for Bridge and Structural Engineering (IABSE), 2018. http://dx.doi.org/10.2749/kualalumpur.2018.0992.

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<p>Air-coupled ultrasonic test is a non-destructive test method for investigating damage in material. In this paper, reinforced concrete beams with one 8-mm diameter rounded bar were casted and tested under four-point bending test with water-cement ratio of 40% and 60%. The transducers were placed and focused on the horizontal surface with induced 3mm notch at the midpoint where maximum tension occurred and crack formation was located. Frequency domain waveform was used specifically to analyze second harmonic generation (SHG). There were two metrics used under the SHG, these were: second harmonic amplitude (SHA) and second harmonic ratio (SHR). The SHR proved to be consistent for both water-cement ratio and it behaved increasing as damage in tension increases.</p>
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Tzouvelekis, Argyris, Guoying Yu, Jose Herazo-Maya, Tony Woolard, Yi Zhang, Hojin Lee, Patty Lee, Erica Herzog, Anton Bennett, and Naftali Kaminski. "SH2 domain-containing phosphatase-SHP-2 is a novel anti-fibrotic regulator in pulmonary fibrosis." In ERS International Congress 2016 abstracts. European Respiratory Society, 2016. http://dx.doi.org/10.1183/13993003.congress-2016.oa4979.

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Tzouvelekis, Argyris, Guoyin Yu, Farida Ahangari, Anton Bennett, Theodoros Karampitsakos, Demosthenes Bouros, Evangelos Bouros, and Naftali Kaminski. "SH2 domain-containing Phosphatase-(SHP)-2 blunts fibrotic responses through regulation of fibroblast mitochondrial metabolism and autophagy." In ERS International Congress 2019 abstracts. European Respiratory Society, 2019. http://dx.doi.org/10.1183/13993003.congress-2019.pa583.

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Shen, Kexin, Heather R. Dorman, Haibin Shi, Ravi K. Patel, Jamie A. Moroco, John R. Engen, and Thomas E. Smithgall. "Abstract 2377: The AML linked Src family kinase Fgr is uncoupled from SH2 and SH3 domain regulation and drives oncogenic transformation." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-2377.

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Lu, Haiyun, Shamima Banu Bte Sm Rashid, Hao Li, Wee Kheng Leow, and Yih-Cherng Liou. "Knowledge-Guided Docking of Flexible Ligands to SH2 Domain Proteins." In 2010 IEEE International Conference on BioInformatics and BioEngineering. IEEE, 2010. http://dx.doi.org/10.1109/bibe.2010.37.

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Dhanik, A., J. S. McMurray, and L. Kavraki. "On modeling peptidomimetics in complex with the SH2 domain of Stat3." In 2011 33rd Annual International Conference of the IEEE Engineering in Medicine and Biology Society. IEEE, 2011. http://dx.doi.org/10.1109/iembs.2011.6090878.

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Mandal, Pijus K., Yanhua Yao, Anne R. Bresnick, Jonathan M. Backer, and John S. McMurray. "Abstract 4838: Peptide prodrugs targeting the SH2 domains of p85 block PI3K signaling." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-4838.

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Lesterhuis, W. Joost, Stanleyson V. Hato, Carl G. Figdor, Susumu Takahashi, Cornelis J. A. Punt, Akira Asai, and I. Jolanda M. De Vries. "Abstract 2120: Platinum-based cancer chemotherapeutics inhibit STAT signaling by blocking the SH2 domain." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-2120.

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Giubellino, Alessio, Fa Liu, Terrence Burke, and Donald P. Bottaro. "Abstract A163: Development of Grb2 SH3 domain antagonists." In Abstracts: AACR-NCI-EORTC International Conference: Molecular Targets and Cancer Therapeutics--Nov 15-19, 2009; Boston, MA. American Association for Cancer Research, 2009. http://dx.doi.org/10.1158/1535-7163.targ-09-a163.

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Kong, Ren, Uddalak Bharadwaj, Thomas Kris Eckols, Moses Kasembeli, Mikhail Kolosov, Anh Tran, Oluwatomilona I. Ifelayo, Hong Zhao, Stephen T. Wong, and David J. Tweardy. "Abstract 17: Novel STAT3 inhibitors identified by Structure-Based Virtual Ligand Screening incorporating SH2 domain flexibility." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-17.

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Reports on the topic "Domaine SH2"

1

Margolis, Benjamin L., and Edward Y. Skolnik. Cell Signaling by a Novel SH2 Domain Protein That is Overexpressed with HER2 in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, December 1999. http://dx.doi.org/10.21236/ada395430.

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Margolis, Benjamin L. Cell Signaling by a Novel SH2 Domain Protein that is Overexpressed with Her2 in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, December 1996. http://dx.doi.org/10.21236/ada326383.

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Margolis, Benjamin L. Cell Signalling by a Novel SH2 Domain Protein that is Overexpressed with Her2 in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, January 1996. http://dx.doi.org/10.21236/ada304456.

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Margolis, Benjamin L. Cell Signalling by a Novel SH2 Domain Protein that is Overexpressed with Her2 in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, December 1998. http://dx.doi.org/10.21236/ada378116.

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Eastlake, D. RSA/SHA-1 SIGs and RSA KEYs in the Domain Name System (DNS). RFC Editor, May 2001. http://dx.doi.org/10.17487/rfc3110.

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Kotula, Leszek, Jiliu Xu, Jill A. Macoska, Piotr Kozlowski, and Magdalena Martinka. The Role of Human Spectrin SH3 Domain Binding Protein 1 (HSSH3BPl) in Prostatic Adenocarcinoma. Fort Belvoir, VA: Defense Technical Information Center, September 2004. http://dx.doi.org/10.21236/ada430579.

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Kotula, Leszek, Jiliu XU, Jill A. Macoska, Piotr Kozlowski, and Magdalena Martinka. The Role of Human Spectrin SH3 Domain Binding Protein 1 (HSSH3BP1) in Prostatic Adenocarcinoma. Fort Belvoir, VA: Defense Technical Information Center, September 2002. http://dx.doi.org/10.21236/ada411959.

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Kotula, Leszek, Jiliu Xu, Jill A. Macoska, Piotr Kozlowski, Magdalena Martinka, and Edward C. Jones. The Role of Human Spectrin SH3 Domain Binding Protein 1 (HSSH3BP1) in Prostatic Adenocarcinoma. Fort Belvoir, VA: Defense Technical Information Center, September 2003. http://dx.doi.org/10.21236/ada419543.

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