Relevant bibliographies by topics / Y74C

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  1. Journal articles
  2. Book chapters
  3. Conference papers

Academic literature on the topic 'Y74C'

Author: Grafiati
Published: 6 September 2023

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Journal articles on the topic "Y74C"

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Tweardy, David John, Xu Xuejun, Naijie Jing, and Huang Shao. "Structural Determinants for Signal Transducer and Activator of Transcription (STAT) 3 Recruitment and Activation by the Granulocyte Colony-Stimulating Factor Receptor (G-CSFR) at Phosphotyrosine Ligands 704 and 744." Blood 104, no. 11 (2004): 2169. http://dx.doi.org/10.1182/blood.v104.11.2169.2169.

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Abstract Four tyrosine (Y) residues within the cytoplasmic domain of the G-CSFR (Y704, Y228, Y744 and Y764 in the human receptor; Y703, Y227, Y743 and Y763 in the murine receptor) become phosphorylated by Jak kinases upon ligand binding leading to recruitment of Src homology (SH) 2 domain-containing proteins that link to programs for myeloid cell survival and differentiation (Stat3 recruitment to Y704 and Y744) and proliferation (SHP-2 and PI3K recruitment to Y04; Grb2, Shc and SHP-2 recruitment to Y764). While the preference of SH2 domain binding to specific phospho (p) Y peptide ligands was
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2

Stojanovic, Aleksandra, Panagiotis Flevaris, Xiaodong Xi та ін. "Tyrosine Phosphorylation of the Integrin β3 Subunit Regulates β3 Cleavage by Calpain." Blood 108, № 11 (2006): 1524. http://dx.doi.org/10.1182/blood.v108.11.1524.1524.

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Abstract Outside-in signaling of β3 integrins induces and requires phosphorylation at tyrosine-747 (Y747) and tyrosine-759 (Y759) of the β3 subunit, but the mechanism for this requirement is unclear. On the other hand, a key consequence of integrin signaling, cell spreading, is inhibited by calpain cleavage of β3 cytoplasmic domain. Here we show that tyrosine phosphorylation in the synthetic β3 cytoplasmic domain peptide inhibits calpain cleavage. In platelets, tyrosine phosphates inhibitor, sodium vanadate, enhances thrombin-induced phosphorylation at Y747 and Y759, which is associated with t
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Chakraborty, Arup, Kevin F. Dyer, Michael Cascio, Timothy A. Mietzner, and David J. Tweardy. "Identification of a Novel Stat3 Recruitment and Activation Motif Within the Granulocyte Colony-Stimulating Factor Receptor." Blood 93, no. 1 (1999): 15–24. http://dx.doi.org/10.1182/blood.v93.1.15.

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Abstract Stat3 is essential for early embryonic development and for myeloid differentiation induced by the cytokines granulocyte colony-stimulating factor (G-CSF) and interleukin-6 (IL-6). Two isoforms of Stat3 have been identified,  (p92) and β (p83), which have distinct transcriptional and biological functions. Activation of both Stat3 and Stat3β requires the distal cytoplasmic domain of the G-CSFR, which contains four Tyr at positions 704, 729, 744, and 764. The studies reported here were undertaken to determine which, if any, of these tyrosine residues participated in Stat3/β recruitmen
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Chakraborty, Arup, Kevin F. Dyer, Michael Cascio, Timothy A. Mietzner, and David J. Tweardy. "Identification of a Novel Stat3 Recruitment and Activation Motif Within the Granulocyte Colony-Stimulating Factor Receptor." Blood 93, no. 1 (1999): 15–24. http://dx.doi.org/10.1182/blood.v93.1.15.401a46_15_24.

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Stat3 is essential for early embryonic development and for myeloid differentiation induced by the cytokines granulocyte colony-stimulating factor (G-CSF) and interleukin-6 (IL-6). Two isoforms of Stat3 have been identified,  (p92) and β (p83), which have distinct transcriptional and biological functions. Activation of both Stat3 and Stat3β requires the distal cytoplasmic domain of the G-CSFR, which contains four Tyr at positions 704, 729, 744, and 764. The studies reported here were undertaken to determine which, if any, of these tyrosine residues participated in Stat3/β recruitment and act
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5

Yoon, Jeong Hyun, Min-Kyu Song, and Jang-Yeon Kwon. "Detection of Proton Carriers in Tyrosine-Rich Peptide Thin Film." ECS Meeting Abstracts MA2022-01, no. 18 (2022): 1048. http://dx.doi.org/10.1149/ma2022-01181048mtgabs.

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Traditional Von Neumann structure, where memory and computational units are separated, is now facing significant difficulties in terms of power consumption and computing speed in big data era. Therefore, human brain-like computing architecture is now paid attention in research field owing to its high parallelism, fault tolerance and robustness1-2. In this biological system, synaptic weight which plays crucial role in memory and learning is modulated by ionic species, especially protons transmitted between synapses. Here, we focused on short length peptide Y7C (YYACAYY) thin film which induces
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6

Boettiger, David, Francois Huber, Laura Lynch та Scott Blystone. "Activation of αvβ3-Vitronectin Binding Is a Multistage Process in which Increases in Bond Strength Are Dependent on Y747 and Y759 in the Cytoplasmic Domain of β3". Molecular Biology of the Cell 12, № 5 (2001): 1227–37. http://dx.doi.org/10.1091/mbc.12.5.1227.

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Integrin receptors serve as mechanical links between the cell and its structural environment. Using αvβ3 integrin expressed in K562 cells as a model system, the process by which the mechanical connection between αvβ3 and vitronectin develops was analyzed by measuring the resistance of these bonds to mechanical separation. Three distinct stages of activation, as defined by increases in the αvβ3-vitronectinbinding strength, were defined by mutational, biochemical, and biomechanical analyses. Activation to the low binding strength stage 1 occurs through interaction with the vitronectin ligand and
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7

Xi, Xiaodong, Richard J. Bodnar, Zhenyu Li, Stephen C. T. Lam та Xiaoping Du. "Critical roles for the COOH-terminal NITY and RGT sequences of the integrin β3 cytoplasmic domain in inside-out and outside-in signaling". Journal of Cell Biology 162, № 2 (2003): 329–39. http://dx.doi.org/10.1083/jcb.200303120.

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Bidirectional signaling of integrin αIIbβ3 requires the β3 cytoplasmic domain. To determine the sequence in the β3 cytoplasmic domain that is critical to integrin signaling, cell lines were established that coexpress the platelet receptor for von Willebrand factor (vWF), glycoprotein Ib-IX, integrin αIIb, and mutants of β3 with truncations at sites COOH terminal to T741, Y747, F754, and Y759. Truncation at Y759 did not affect integrin activation, as indicated by vWF-induced fibrinogen binding, but affected cell spreading and stable adhesion. Thus, the COOH-terminal RGT sequence of β3 is import
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Katayama, Takane, Hideyuki Suzuki, Takashi Koyanagi, and Hidehiko Kumagai. "Cloning and Random Mutagenesis of the Erwinia herbicola tyrR Gene for High-Level Expression of Tyrosine Phenol-Lyase." Applied and Environmental Microbiology 66, no. 11 (2000): 4764–71. http://dx.doi.org/10.1128/aem.66.11.4764-4771.2000.

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ABSTRACT Tyrosine phenol-lyase (Tpl), which can synthesize 3,4-dihydroxyphenylalanine from pyruvate, ammonia, and catechol, is a tyrosine-inducible enzyme. Previous studies demonstrated that thetpl promoter of Erwinia herbicola is activated by the TyrR protein of Escherichia coli. In an attempt to create a high-Tpl-expressing strain, we cloned the tyrRgene of E. herbicola and then randomly mutagenized it. Mutant TyrR proteins with enhanced ability to activate tplwere screened for by use of the lac reporter system inE. coli. The most increased transcription oftpl was observed for the strain wit
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9

García-Peydró, Marina, Alberto Paradela, José R. Lamas, and José A. López de Castro. "Peptide Presentation to an Alloreactive CTL Clone Is Modulated Through Multiple Mechanisms Involving Polymorphic and Conserved Residues in HLA-B27." Journal of Immunology 163, no. 11 (1999): 6060–64. http://dx.doi.org/10.4049/jimmunol.163.11.6060.

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Abstract This study addressed the mechanisms by which HLA class I polymorphism modulates allorecognition. CTL 27S69 is an alloreactive clone raised against HLA-B*2705, with a known peptide epitope. This CTL cross-reacts with B*2702, which differs from B*2705 in the D77N, T80I, and L81A changes, but not with B*2701, which has D74Y, D77N, and L81A changes. To explain this differential recognition, B*2705 mutants mimicking subtype changes were used. The A81 mutant was not recognized, despite binding the natural epitope in vivo, suggesting that, when bound to this mutant, this peptide adopts an in
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10

de Koning, John P., Amrita A. Soede-Bobok, Anita M. Schelen, et al. "Proliferation Signaling and Activation of Shc, p21Ras, and Myc Via Tyrosine 764 of Human Granulocyte Colony-Stimulating Factor Receptor." Blood 91, no. 6 (1998): 1924–33. http://dx.doi.org/10.1182/blood.v91.6.1924.

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Abstract The membrane-distal region of the cytoplasmic domain of human granulocyte colony-stimulating factor receptor (G-CSF-R) contains four conserved tyrosine residues: Y704, Y729, Y744, and Y764. Three of these (Y729, Y744, and Y764) are located in the C-terminal part of G-CSF-R, previously shown to be essential for induction of neutrophilic differentiation. To determine the role of the tyrosines in G-CSF–mediated responses, we constructed tyrosine-to-phenylalanine (Y-to-F) substitution mutants and expressed these in a differentiation competent subclone of 32D cells that lacks endogenous G-
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Book chapters on the topic "Y74C"

1

"Y74 Accessories for electrical services." In Spon's Estimating Costs Guide to Electrical Works. Spon Press, 2007. http://dx.doi.org/10.1201/9781482266375-12.

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"Y74 Accessories for Electrical Services." In Spon's Estimating Costs Guide to Electrical Works. Spon Press, 2003. http://dx.doi.org/10.4324/9781482265323-12.

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Conference papers on the topic "Y74C"

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Borodin, Evgeniy. "SEARCH FOR POTENTIAL LIGANDS FOR TRPM8 WITH THE HELP OF COMPUTER DESIGN." In XIV International Scientific Conference "System Analysis in Medicine". Far Eastern Scientific Center of Physiology and Pathology of Respiration, 2020. http://dx.doi.org/10.12737/conferencearticle_5fe01d9b2fdca3.97577371.

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A search was carried out for potential ligands to TRPM8 - a representative of the family of cationic channels with a transient receptor potential involved in the development of bronchial hypersensitivity and the occurrence of bronchospasm in response to low temperatures. We used a structural design and molecular docking using the autodock software package (http://autodock.scripps.edu/), which allows automated testing of many potential ligands for TRPM8. Docking was carried out with tyrosine 745 (Y745) amino acid residue as a critical residue for channel sensitivity to menthol, a classic TRPM8
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