Relevant bibliographies by topics / Phosphorylation motif

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Academic literature on the topic 'Phosphorylation motif'

Author: Grafiati
Published: 4 June 2021
Last updated: 5 February 2022

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Journal articles on the topic "Phosphorylation motif"

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NEWTON, Alexandra C. "Regulation of the ABC kinases by phosphorylation: protein kinase C as a paradigm." Biochemical Journal 370, no. 2 (2003): 361–71. http://dx.doi.org/10.1042/bj20021626.

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Phosphorylation plays a central role in regulating the activation and signalling lifetime of protein kinases A, B (also known as Akt) and C. These kinases share three conserved phosphorylation motifs: the activation loop segment, the turn motif and the hydrophobic motif. This review focuses on how phosphorylation at each of these sites regulates the maturation, signalling and down-regulation of PKC as a paradigm for how these sites control the function of the ABC kinases.
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Fu, Zheng, Melanie J. Schroeder, Jeffrey Shabanowitz, et al. "Activation of a Nuclear Cdc2-Related Kinase within a Mitogen-Activated Protein Kinase-Like TDY Motif by Autophosphorylation and Cyclin-Dependent Protein Kinase-Activating Kinase." Molecular and Cellular Biology 25, no. 14 (2005): 6047–64. http://dx.doi.org/10.1128/mcb.25.14.6047-6064.2005.

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ABSTRACT Male germ cell-associated kinase (MAK) and intestinal cell kinase (ICK) are nuclear Cdc2-related kinases with nearly identical N-terminal catalytic domains and more divergent C-terminal noncatalytic domains. The catalytic domain is also related to mitogen-activated protein kinases (MAPKs) and contains a corresponding TDY motif. Nuclear localization of ICK requires subdomain XI and interactions of the conserved Arg-272, but not kinase activity or, surprisingly, any of the noncatalytic domain. Further, nuclear localization of ICK is required for its activation. ICK is activated by dual
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Das, Rahul K., Yongqi Huang, Aaron H. Phillips, Richard W. Kriwacki, and Rohit V. Pappu. "Cryptic sequence features within the disordered protein p27Kip1 regulate cell cycle signaling." Proceedings of the National Academy of Sciences 113, no. 20 (2016): 5616–21. http://dx.doi.org/10.1073/pnas.1516277113.

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Peptide motifs embedded within intrinsically disordered regions (IDRs) of proteins are often the sites of posttranslational modifications that control cell-signaling pathways. How do IDR sequences modulate the functionalities of motifs? We answer this question using the polyampholytic C-terminal IDR of the cell cycle inhibitory protein p27Kip1 (p27). Phosphorylation of Thr-187 (T187) within the p27 IDR controls entry into S phase of the cell division cycle. Additionally, the conformational properties of polyampholytic sequences are predicted to be influenced by the linear patterning of opposit
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Adams, Peter D., Xiaotong Li, William R. Sellers, et al. "Retinoblastoma Protein Contains a C-terminal Motif That Targets It for Phosphorylation by Cyclin-cdk Complexes." Molecular and Cellular Biology 19, no. 2 (1999): 1068–80. http://dx.doi.org/10.1128/mcb.19.2.1068.

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ABSTRACT Stable association of certain proteins, such as E2F1 and p21, with cyclin-cdk2 complexes is dependent upon a conserved cyclin-cdk2 binding motif that contains the core sequence ZRXL, where Z and X are usually basic. In vitro phosphorylation of the retinoblastoma tumor suppressor protein, pRB, by cyclin A-cdk2 and cyclin E-cdk2 was inhibited by a short peptide spanning the cyclin-cdk2 binding motif present in E2F1. Examination of the pRB C terminus revealed that it contained sequence elements related to ZRXL. Site-directed mutagenesis of one of these sequences, beginning at residue 870
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Baffi, Timothy R., Gema Lordén, Jacob M. Wozniak, et al. "mTORC2 controls the activity of PKC and Akt by phosphorylating a conserved TOR interaction motif." Science Signaling 14, no. 678 (2021): eabe4509. http://dx.doi.org/10.1126/scisignal.abe4509.

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The complex mTORC2 is accepted to be the kinase that controls the phosphorylation of the hydrophobic motif, a key regulatory switch for AGC kinases, although whether mTOR directly phosphorylates this motif remains controversial. Here, we identified an mTOR-mediated phosphorylation site that we termed the TOR interaction motif (TIM; F-x3-F-pT), which controls the phosphorylation of the hydrophobic motif of PKC and Akt and the activity of these kinases. The TIM is invariant in mTORC2-dependent AGC kinases, is evolutionarily conserved, and coevolved with mTORC2 components. Mutation of this motif
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Hiraoka, D., E. Okumura, and T. Kishimoto. "Turn motif phosphorylation negatively regulates activation loop phosphorylation in Akt." Oncogene 30, no. 44 (2011): 4487–97. http://dx.doi.org/10.1038/onc.2011.155.

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García-Martínez, Juan M., and Dario R. Alessi. "mTOR complex 2 (mTORC2) controls hydrophobic motif phosphorylation and activation of serum- and glucocorticoid-induced protein kinase 1 (SGK1)." Biochemical Journal 416, no. 3 (2008): 375–85. http://dx.doi.org/10.1042/bj20081668.

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SGK1 (serum- and glucocorticoid-induced protein kinase 1) is a member of the AGC (protein kinase A/protein kinase G/protein kinase C) family of protein kinases and is activated by agonists including growth factors. SGK1 regulates diverse effects of extracellular agonists by phosphorylating regulatory proteins that control cellular processes such as ion transport and growth. Like other AGC family kinases, activation of SGK1 is triggered by phosphorylation of a threonine residue within the T-loop of the kinase domain and a serine residue lying within the C-terminal hydrophobic motif (Ser422 in S
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Hayashi, Fumio, Noriyo Itoh, Tatsuya Uzumaki, et al. "Roles of Two ATPase-Motif-containing Domains in Cyanobacterial Circadian Clock Protein KaiC." Journal of Biological Chemistry 279, no. 50 (2004): 52331–37. http://dx.doi.org/10.1074/jbc.m406604200.

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Cyanobacterial clock protein KaiC has a hexagonal, pot-shaped structure composed of six identical dumbbell-shaped subunits. Each subunit has duplicated domains, and each domain has a set of ATPase motifs. The two spherical regions of the dumbbell are likely to correspond to two domains. We examined the role of the two sets of ATPase motifs by analyzing thein vitroactivity of ATPγS binding, AMPPNP-induced hexamerization, thermostability, and phosphorylation of KaiC and byin vivorhythm assays both in wild type KaiC (KaiCWT) and KaiCs carrying mutations in either Walker motif A or deduced catalyt
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Pollitt, Alice Y., Beata Grygielska, Bertrand Leblond, Laurent Désiré, Johannes A. Eble, and Steve P. Watson. "Phosphorylation of CLEC-2 is dependent on lipid rafts, actin polymerization, secondary mediators, and Rac." Blood 115, no. 14 (2010): 2938–46. http://dx.doi.org/10.1182/blood-2009-12-257212.

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Abstract The C-type lectin-like receptor 2 (CLEC-2) activates platelets through Src and Syk tyrosine kinases via a single cytoplasmic YxxL motif known as a hem immunoreceptor tyrosine-based activation motif (hemITAM). Here, we demonstrate using sucrose gradient ultracentrifugation and methyl-β-cyclodextrin treatment that CLEC-2 translocates to lipid rafts upon ligand engagement and that translocation is essential for hemITAM phosphorylation and signal initiation. HemITAM phosphorylation, but not translocation, is also critically dependent on actin polymerization, Rac1 activation, and release o
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Ikeda, Masato, Akiko Ikeda, and Richard Longnecker. "PY Motifs of Epstein-Barr Virus LMP2A Regulate Protein Stability and Phosphorylation of LMP2A-Associated Proteins." Journal of Virology 75, no. 12 (2001): 5711–18. http://dx.doi.org/10.1128/jvi.75.12.5711-5718.2001.

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ABSTRACT Latent membrane protein 2A (LMP2A) is expressed in latent Epstein-Barr virus (EBV) infection. We have demonstrated that Nedd4 family ubiquitin-protein ligases (E3s), AIP4, WWP2/AIP2, and Nedd4, bind specifically to two PY motifs present within the LMP2A amino-terminal domain. In this study, LMP2A PY motif mutant viruses were constructed to investigate the role of the LMP2A PY motifs. AIP4 was found to specifically associate with the LMP2A PY motifs in EBV-transformed lymphoblastoid cell lines (LCLs), extending our original observation to EBV-infected cells. Mutation of both of the LMP
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Dissertations / Theses on the topic "Phosphorylation motif"

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Mijakovic̀, Ivan. "Protéine kinases avec un motif Walker A chez Bacillus subtilis." Paris 11, 2003. http://www.theses.fr/2003PA112152.

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La phosphorylation des protéines est un phénomène omniprésent dans le monde du vivant, observé chez les trois grands règnes: Bacteria, Eukarya et Archaea. Les protéines capables de catalyser la formation d'une liaison covalente entre le phosphate et la chaîne latérale d'un acide aminé d'une protéine s'appellent protéine kinases. En revanche, les phospho-protéine phosphatases sont les protéines capables de dé-modifier une protéine phosphorylée, en catalysant l'hydrolyse du lien covalent entre la protéine et le phosphate. L'état de phosphorylation d'une protéine à un instant donné est alors déte
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Ahn, Jeong H. Lee Myeongwoo. "The functional analysis of NPXY motif in [beta] integrin in vivo." Waco, Tex. : Baylor University, 2008. http://hdl.handle.net/2104/5275.

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Coadou, Gaël. "Etude par RMN et Modélisation Moléculaire du motif de phosphorylation de la protéine Vpu du VIH-1 en interaction avec la β-TrCP". Paris 6, 2004. http://www.theses.fr/2004PA066408.

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Durek, Pawel, Christian Schudoma, Wolfram Weckwerth, Joachim Selbig, and Dirk Walther. "Detection and characterization of 3D-signature phosphorylation site motifs and their contribution towards improved phosphorylation site prediction in proteins." Universität Potsdam, 2009. http://opus.kobv.de/ubp/volltexte/2010/4512/.

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Background: Phosphorylation of proteins plays a crucial role in the regulation and activation of metabolic and signaling pathways and constitutes an important target for pharmaceutical intervention. Central to the phosphorylation process is the recognition of specific target sites by protein kinases followed by the covalent attachment of phosphate groups to the amino acids serine, threonine, or tyrosine. The experimental identification as well as computational prediction of phosphorylation sites (P-sites) has proved to be a challenging problem. Computational methods have focused primarily on
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Balakrishnan, Shalini. "Development of novel switchable motifs and new strategies to build functionally privileged structures." Access to citation, abstract and download form provided by ProQuest Information and Learning Company; downloadable PDF file, 220 p, 2007. http://proquest.umi.com/pqdweb?did=1464120641&sid=2&Fmt=2&clientId=8331&RQT=309&VName=PQD.

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Stein, Amelie. "Peptime-mediated interactions in high-resolution 3-dimensional structures." Doctoral thesis, Universitat Pompeu Fabra, 2010. http://hdl.handle.net/10803/7218.

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Proteins and protein interactions are involved in virtually all processes of life. Here we study interactions between globular domains and short linear motifs, which form a small interface ideal for transient interactions. Despite the small number of contacts involved, these domain-motif interactions (DMIs) are known to be highly specific in vivo. We have identified hundreds of instances of DMIs in high-resolution 3-dimensional (3D) structures to analyze the molecular basis of their high specificity. Furthermore, we have derived structural parameters to identify DMIs in 3D structures in a mor
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Petzhold, Daria. "Funktionelle Untersuchungen von Ahnak durch Protein-Protein-Wechselwirkungen und in Ahnak-Defizienzmodellen." Doctoral thesis, Humboldt-Universität zu Berlin, Mathematisch-Naturwissenschaftliche Fakultät I, 2007. http://dx.doi.org/10.18452/15694.

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Ahnak ist ein ubiquitäres Protein, das an einer Vielzahl biologischer Prozesse beteiligt ist. In der Herzmuskelzelle ist Ahnak überwiegend am Sarkolemma lokalisiert und bindet an Aktin und an die regulatorischen Beta2-Untereinheit des L-Typ-Kalzium-Kanals. Das Ziel dieser Arbeit war die Funktion von Ahnak im Herzen mit Hilfe eines Knock-out-Maus-Modells und in Bindungsstudien zu untersuchen. Morphologische Untersuchungen zeigten, dass das Längenwachstum adulter Kardiomyozyten bei Ahnakdefizienz signifikant reduziert war. Die Kontraktionseigenschaften adulter isolierter Ahnak-defizienter Kardi
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Champeyroux, Chloé. "Caractérisation fonctionnelle de protéines en interaction avec l'aquaporine PIP2;1." Thesis, Montpellier, 2017. http://www.theses.fr/2017MONTT120.

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La conductivité hydraulique racinaire (Lpr) traduit la capacité de transport d’eau de la racine. Lors de son trajet du sol vers le xylème, l’eau diffuse au sein de l’apoplasme ou au travers des cellules (voie de cellule-à-cellule). Au niveau de l’endoderme, la diffusion apoplasmique de l’eau est bloquée par le cadre de Caspari et des lamelles de subérine. La voie de cellule-à-cellule dépend principalement de l’activité des aquaporines régulées en partie par des interactions protéiques. Ce travail caractérise de nouveaux interactants de l’aquaporine racinaire PIP2;1 : le récepteur kinase RKL1 e
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Filipe, Josina. "Rôle de la proteine NRP/Optineurine dans l'activation de NF-kB induite par Tax1 et dans la réponse antivirale médiée par IRF3." Paris 7, 2009. http://www.theses.fr/2009PA077239.

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L'objectif de ce travail a été de réaliser une étude fonctionnelle de la protéine NRP (NEMO-related protein). NRP est une protéine homologue à NEMO, l'élément essentiel de la voie de signalisation NF-KB qui joue un rôle important au niveau des systèmes immunitaire et inflammatoire et des mécanismes antiapoptotiques. Dans un premier travail, réalisé en collaboration, nous avons montré que NRP était un interactant de la protéine Tax du virus HTLV-1. L'activation de NF-KB par Tax est nécessaire à la survie des cellules infectées par HTLV-1 et nous avons montré qu'elle est potentialisée par NRP qu
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Sessa, Gaetana. "Role of the Interaction of BRCA2 and DDX5 in the DNA Damage Response BRCA2 promotes DNA-RNA hybrid resolution by DDX5 at DNA double strand breaks to facilitate homologous recombination Proper chromosome alignment depends on BRCA2 phosphorylation by PLK1." Thesis, université Paris-Saclay, 2020. http://www.theses.fr/2020UPASS116.

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Un nombre croissant d’études soutiennent le fait que les protéines majeures du métabolisme des ARN, telles que les hélicases ARN, sont impliquées dans la réponse aux dommages à l’ADN. Cette activité est généralement accomplie par leur interaction avec des facteurs de réparation de l’ADN. BRCA2, une protéine suppressive de tumeurs, joue un rôle crucial dans la réparation des cassures double-brin (CDB) de l'ADN par recombinaison homologue (RH) et donc, est un facteur essentiel pour l’intégrité du génome. Les cellules déficientes pour BRCA2 accumulent des hybrides ADN-ARN ou R-loops, une source d
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Books on the topic "Phosphorylation motif"

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Aitken, Alastair. Identification of protein consensus sequences: Active site motifs, phosphorylation, and other post-translational modifications. Ellis Horwood, 1990.

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Aitken, Alastair. Identification of protein consensus sequences: Active site motifs, phosphorylation, and other post-translational modifications. Ellis Horwood, 1990.

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Identification of Protein Consensus Sequences: Active Site Motifs, Phosphorylation, and Other Posttranslational Modifications (Ellis Horwood Books in the Biological Sciences). Ellis Horwood Ltd, 1990.

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Book chapters on the topic "Phosphorylation motif"

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Tsai, Chia-Feng, Wei-Chi Ku, Yu-Ju Chen, and Yasushi Ishihama. "Absolute Phosphorylation Stoichiometry Analysis by Motif-Targeting Quantitative Mass Spectrometry." In Methods in Molecular Biology. Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-7154-1_20.

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Simon, Márton A., and László Nyitray. "Dynamic Control of Signaling by Phosphorylation of PDZ Binding Motifs." In Methods in Molecular Biology. Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-1166-1_11.

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Xi, Lin, Zhaoxia Zhang, Sandra Herold, Sarah Kassem, Xu Na Wu, and Waltraud X. Schulze. "Phosphorylation Site Motifs in Plant Protein Kinases and Their Substrates." In Plant Phosphoproteomics. Springer US, 2021. http://dx.doi.org/10.1007/978-1-0716-1625-3_1.

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Leung, Genie C., James M. Murphy, Doug Briant, and Frank Sicheri. "Characterization of Kinase Target Phosphorylation Consensus Motifs Using Peptide SPOT Arrays." In Peptide Microarrays. Humana Press, 2009. http://dx.doi.org/10.1007/978-1-60327-394-7_7.

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Miller, Chad J., and Benjamin E. Turk. "Rapid Identification of Protein Kinase Phosphorylation Site Motifs Using Combinatorial Peptide Libraries." In Methods in Molecular Biology. Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-3073-9_15.

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He, Zengyou. "Phosphorylation motif discovery." In Data Mining for Bioinformatics Applications. Elsevier, 2015. http://dx.doi.org/10.1016/b978-0-08-100100-4.00003-x.

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Jans, David A. "Phosphorylation-mediated regulation of signal-dependent nuclear protein transport: The “CcN motif”." In Membrane Protein Transport. Elsevier, 1995. http://dx.doi.org/10.1016/s1874-592x(06)80008-9.

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Simons, Peter, and Charlotte M. Vines. "Analysis of GTP-Binding Protein–Coupled Receptor Assemblies by Flow Cytometry." In Flow Cytometry for Biotechnology. Oxford University Press, 2005. http://dx.doi.org/10.1093/oso/9780195183146.003.0022.

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GTP-binding protein–coupled receptors (GPCRs) represent the largest family of integral membrane signal-transducing molecules in the human genome, with estimates of at least 600 members. As such, they represent the targets of approximately 30%–50% of the prescription drugs on the market. They are involved in virtually every physiological process in the human body, with ligands including light, odorants, amines, peptides, proteins, lipids, and nucleotides. Binding of these ligands on the extracellular surface of the receptor leads to conformational changes within the receptor, resulting in a multitude of cellular responses. GPCRs, as their name implies, function through the actions of heterotrimeric GTP-binding proteins (G proteins). These G proteins then couple to a diverse array of effector molecules at the cell surface and inside the cell. GPCRs contain a common structural motif, with seven transmembrane alpha helices. With the recent description of the three-dimensional crystal structure of rhodopsin in its inactive state, a greater, though still incomplete, understanding of the functions of this receptor family has been achieved. In addition to the activation of G proteins, GPCRs undergo extensive regulation mediated primarily by a variety of kinases, including second messenger kinases and the family of G protein–coupled receptor kinases (GRKs). Following receptor phosphorylation by GRKs, additional proteins named arrestins associate with GPCRs. The traditional role of these molecules has been to serve as desensitizing agents, preventing further association of the receptor with G proteins. However, recent studies have demonstrated that arrestins can serve as adapters in the process of receptor internalization as well as scaffolds in the activation of numerous kinase pathways. Interactions between GPCRs and cellular proteins such as adaptins, rab GTPases, phosphatases, and ion channels have also been described. Thus, it has become apparent that understanding the interactions between GPCRs and their associated proteins is critical for any detailed understanding of receptor function. An overview of the activation and regulation of GPCRs is shown in figure 17.1 to provide a context for the approaches to be described in the remainder of this chapter.
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Pearson, Richard B., and Bruce E. Kemp. "[3] Protein kinase phosphorylation site sequences and consensus specificity motifs: Tabulations." In Methods in Enzymology. Elsevier, 1991. http://dx.doi.org/10.1016/0076-6879(91)00127-i.

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Conference papers on the topic "Phosphorylation motif"

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Cho, Hongkwan, Abdul Sheikh, and Daria A. Narmoneva. "Non-Specific Endothelial Cell Interactions With the Substrate Result in Cell Activation and Angiogenesis In Vitro." In ASME 2010 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2010. http://dx.doi.org/10.1115/sbc2010-19094.

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Vascularization is critical for success of tissue engineering applications. Previous studies by us and others have shown that self-assembling peptide nanoscaffold RAD16-II promotes de novo capillary formation (angiogenesis) in vitro and neovascularization in vivo, and is a promising material for tissue engineering applications [1, 2]. However, the molecular mechanisms for cell interactions with this material are not known. Angiogenesis is mediated via interactions between integrins, which are expressed on the surface of activated endothelial cells (ECs), and extracellular matrix proteins. Amon
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