Relevant bibliographies by topics / Phosphoproteins

Academic literature on the topic 'Phosphoproteins'

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Published: 4 June 2021
Last updated: 6 September 2023

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Journal articles on the topic "Phosphoproteins"

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Qiao, Yuting, Xianrong Liu, Zhi Jia, Peng Zhang, Li Gao, Bingxin Liu, Lijuan Qiao, and Lei Zhang. "In Situ Growth Intercalation Structure MXene@Anatase/Rutile TiO2 Ternary Heterojunction with Excellent Phosphoprotein Detection in Sweat." Biosensors 12, no. 10 (October 12, 2022): 865. http://dx.doi.org/10.3390/bios12100865.

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Abnormal protein phosphorylation may relate to diseases such as Alzheimer’s, schizophrenia, and Parkinson’s. Therefore, the real-time detection of phosphoproteins in sweat was of great significance for the early knowledge, detection, and treatment of neurological diseases. In this work, anatase/rutile TiO2 was in situ grown on the MXene surface to constructing the intercalation structure MXene@anatase/rutile TiO2 ternary heterostructure as a sensing platform for detecting phosphoprotein in sweat. Here, the intercalation structure of MXene acted as electron and diffusion channels for phosphoproteins. The in situ grown anatase/rutile TiO2 with n-n-type heterostructure provided specific adsorption sites for the phosphoproteins. The determination of phosphoprotein covered concentrations in sweat, with linear range from 0.01 to 1 mg/mL, along with a low LOD of 1.52 μM. It is worth noting that, since the macromolecular phosphoprotein was adsorbed on the surface of the material, the electrochemical signal gradually decreased with the increase of phosphoprotein concentration. In addition, the active sites in the MXene@anatase/rutile TiO2 ternary heterojunction and synergistic effect of the heterojunction were verified by first-principle calculations to further realize the response to phosphoproteins. Additionally, the effective diffusion capacity and mobility of phosphoprotein molecules in the ternary heterojunction structure were studied by molecular dynamics simulation. Furthermore, the constructed sensing platform showed high selectivity, repeatability, reproducibility, and stability, and this newly developed sensor can detect for phosphoprotein in actual sweat samples. This satisfactory sensing strategy could be promoted to realize the noninvasive and continuous detection of sweat.
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Rodríguez-Vázquez, Raquel, Daniel Mouzo, and Carlos Zapata. "Phosphoproteome Analysis Using Two-Dimensional Electrophoresis Coupled with Chemical Dephosphorylation." Foods 11, no. 19 (October 7, 2022): 3119. http://dx.doi.org/10.3390/foods11193119.

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Protein phosphorylation is a reversible post-translational modification (PTM) with major regulatory roles in many cellular processes. However, the analysis of phosphoproteins remains the most challenging barrier in the prevailing proteome research. Recent technological advances in two-dimensional electrophoresis (2-DE) coupled to mass spectrometry (MS) have enabled the identification, characterization, and quantification of protein phosphorylation on a global scale. Most research on phosphoproteins with 2-DE has been conducted using phosphostains. Nevertheless, low-abundant and low-phosphorylated phosphoproteins are not necessarily detected using phosphostains and/or MS. In this study, we report a comparative analysis of 2-DE phosphoproteome profiles using Pro-Q Diamond phosphoprotein stain (Pro-Q DPS) and chemical dephosphorylation of proteins with HF-P from longissimus thoracis (LT) muscle samples of the Rubia Gallega cattle breed. We found statistically significant differences in the number of identified phosphoproteins between methods. More specifically, we found a three-fold increase in phosphoprotein detection with the HF-P method. Unlike Pro-Q DPS, phosphoprotein spots with low volume and phosphorylation rate were identified by HF-P technique. This is the first approach to assess meat phosphoproteome maps using HF-P at a global scale. The results open a new window for 2-DE gel-based phosphoproteome analysis.
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Rodriguez Galvan, Joaquin, Brianna Donner, Cat Hoang Veseley, Patrick Reardon, Heather M. Forsythe, Jesse Howe, Gretchen Fujimura, and Elisar Barbar. "Human Parainfluenza Virus 3 Phosphoprotein Is a Tetramer and Shares Structural and Interaction Features with Ebola Phosphoprotein VP35." Biomolecules 11, no. 11 (October 29, 2021): 1603. http://dx.doi.org/10.3390/biom11111603.

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The human parainfluenza virus 3 (HPIV3) poses a risk for pneumonia development in young children and immunocompromised patients. To investigate mechanisms of HPIV3 pathogenesis, we characterized the association state and host protein interactions of HPIV3 phosphoprotein (HPIV3 P), an indispensable viral polymerase cofactor. Sequence analysis and homology modeling predict that HPIV3 P possesses a long, disordered N-terminal tail (PTAIL) a coiled-coil multimerization domain (PMD), similar to the well-characterized paramyxovirus phosphoproteins from measles and Sendai viruses. Using a recombinantly expressed and purified construct of PMD and PTAIL, we show that HPIV3 P in solution is primarily an alpha-helical tetramer that is stable up to 60 °C. Pulldown and isothermal titration calorimetry experiments revealed that HPIV3 P binds the host hub protein LC8, and turbidity experiments demonstrated a new role for LC8 in increasing the solubility of HPIV3 P in the presence of crowding agents such as RNA. For comparison, we show that the multimerization domain of the Zaire Ebola virus phosphoprotein VP35 is also a tetramer and binds LC8 but with significantly higher affinity. Comparative analysis of the domain architecture of various virus phosphoproteins in the order Mononegavirales show multiple predicted and verified LC8 binding motifs, suggesting its prevalence and importance in regulating viral phosphoprotein structures. Our work provides evidence for LC8 binding to phosphoproteins with multiple association states, either tetrameric, as in the HPIV3 and Ebola phosphoproteins shown here, or dimeric as in rabies virus phosphoprotein. Taken together the data suggest that the association states of a virus-specific phosphoprotein and the complex formed by binding of the phosphoprotein to host LC8 are important regulators of viral function.
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Qiao, Yuting, Lijuan Qiao, Peize Zhao, Peng Zhang, Fanbin Wu, Jiahui Zhang, Li Gao, Bingxin Liu, and Lei Zhang. "Phosphoprotein Detection in Sweat Realized by Intercalation Structure 2D@3D g-C3N4@Fe3O4 Wearable Sensitive Motif." Biosensors 12, no. 6 (May 24, 2022): 361. http://dx.doi.org/10.3390/bios12060361.

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Abnormal protein phosphorylation in sweat metabolites is closely related to cancer, cardiovascular disease, and other diseases. The real-time monitoring of phosphoproteins in sweat is significant for early monitoring of disease biomarkers. Here, a high-efficiency electrochemical sensor for phosphoprotein in sweat was realized by 2D@3D g-C3N4@Fe3O4 with intercalation structure. Common phosphoprotein β-Casein was selected to demonstrate the platform’s functionalities. The detection limit of g-C3N4@Fe3O4 could be as low as 9.7 μM, and the detection range was from 0.01 mg/mL to 1 mg/mL. In addition, the sensing platform showed good selectivity, reproducibility, and stability. We also investigated the effects of interface structure on adsorption properties and electronic properties of the g-C3N4 and Fe3O4 heterostructure using DFT. More electrons from Fe3O4 were transferred to g-C3N4, which increased the electrons in the energy band of N atoms and promoted the formation of stable N-H bonds with H atoms in phosphoproteins. We demonstrated phosphoprotein sensor functionality by measuring the phosphoprotein in human sweat during exercising. This work realizes a sensing platform for noninvasive and continuous detection of sweat phosphoproteins in wearable devices.
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Li, Qing, Jiong Zhang, Yi Fang, Yan Dai, Ping Jia, Ziyan Shen, Sujuan Xu, Xiaoqiang Ding, and Feng Zhou. "Phosphoproteome Profiling of uEVs Reveals p-AQP2 and p-GSK3β as Potential Markers for Diabetic Nephropathy." Molecules 28, no. 14 (July 24, 2023): 5605. http://dx.doi.org/10.3390/molecules28145605.

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Diabetic nephropathy (DN) contributes to increased morbidity and mortality among patients with diabetes and presents a considerable global health challenge. However, reliable biomarkers of DN have not yet been established. Phosphorylated proteins are crucial for disease progression. However, their diagnostic potential remains unexplored. In this study, we used ultra-high-sensitivity quantitative phosphoproteomics to identify phosphoproteins in urinary extracellular vesicles (uEVs) as potential biomarkers of DN. We detected 233 phosphopeptides within the uEVs, with 47 phosphoproteins exhibiting significant alterations in patients with DN compared to those in patients with diabetes. From these phosphoproteins, we selected phosphorylated aquaporin-2 (p-AQP2[S256]) and phosphorylated glycogen synthase kinase-3β (p-GSK3β[Y216]) for validation, as they were significantly overrepresented in pathway analyses and previously implicated in DN pathogenesis. Both phosphoproteins were successfully confirmed through Phos-tag western blotting in uEVs and immunohistochemistry staining in kidney sections, suggesting that phosphoprotein alterations in uEVs reflect corresponding changes within the kidney and their potential as candidate biomarkers for DN. Our research proposes the utilization of phosphoproteins in uEVs as a liquid biopsy, presenting a highly feasible diagnostic tool for kidney disease.
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Skubitz, K. M., J. R. Mendiola, and M. S. Collett. "CD15 monoclonal antibodies react with a phosphotyrosine-containing protein on the surface of human neutrophils." Journal of Immunology 141, no. 12 (December 15, 1988): 4318–23. http://dx.doi.org/10.4049/jimmunol.141.12.4318.

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Abstract mAb are useful as probes in the study of the roles of cell-surface components in neutrophil function. Many mAb that bind to human neutrophils react with the oligosaccharide lacto-N-fucopentaose III (CD15 antibodies). These antibodies, as well as several other widely used mAb reactive with human neutrophils, were employed to detect phosphoproteins present on these cells. Immunoprecipitation and subsequent gel electrophoresis of proteins from neutrophils labeled with [gamma-32P]ATP revealed a 170 to 190-kDa phosphoprotein specifically reactive with CD15 antibodies. No phosphoproteins were immunoprecipitated by CD11 or CD18 mAb. Phosphoamino acid analysis of the 170- to 190-kDa protein showed that it contained predominantly phosphotyrosine and a low level of phosphoserine. Recently, it was shown that this phosphoprotein is one of the major substrates of ecto-protein kinase activity on human neutrophils. The roles for the 170- to 190-kDa phosphoprotein and the ecto-protein kinase in neutrophil function remain to be determined.
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Moradi, Atieh, Shuaijian Dai, Emily Oi Ying Wong, Guang Zhu, Fengchao Yu, Hon-Ming Lam, Zhiyong Wang, et al. "Isotopically Dimethyl Labeling-Based Quantitative Proteomic Analysis of Phosphoproteomes of Soybean Cultivars." Biomolecules 11, no. 8 (August 16, 2021): 1218. http://dx.doi.org/10.3390/biom11081218.

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Isotopically dimethyl labeling was applied in a quantitative post-translational modification (PTM) proteomic study of phosphoproteomic changes in the drought responses of two contrasting soybean cultivars. A total of 9457 phosphopeptides were identified subsequently, corresponding to 4571 phosphoprotein groups and 3889 leading phosphoproteins, which contained nine kinase families consisting of 279 kinases. These phosphoproteins contained a total of 8087 phosphosites, 6106 of which were newly identified and constituted 54% of the current soybean phosphosite repository. These phosphosites were converted into the highly conserved kinase docking sites by bioinformatics analysis, which predicted six kinase families that matched with those newly found nine kinase families. The overly post-translationally modified proteins (OPP) occupies 2.1% of these leading phosphoproteins. Most of these OPPs are photoreceptors, mRNA-, histone-, and phospholipid-binding proteins, as well as protein kinase/phosphatases. The subgroup population distribution of phosphoproteins over the number of phosphosites of phosphoproteins follows the exponential decay law, Y = 4.13e−0.098X − 0.04. Out of 218 significantly regulated unique phosphopeptide groups, 188 phosphoproteins were regulated by the drought-tolerant cultivar under the water loss condition. These significantly regulated phosphoproteins (SRP) are mainly enriched in the biological functions of water transport and deprivation, methionine metabolic processes, photosynthesis/light reaction, and response to cadmium ion, osmotic stress, and ABA response. Seventeen and 15 SRPs are protein kinases/phosphatases and transcription factors, respectively. Bioinformatics analysis again revealed that three members of the calcium dependent protein kinase family (CAMK family), GmSRK2I, GmCIPK25, and GmAKINβ1 kinases, constitute a phosphor-relay-mediated signal transduction network, regulating ion channel activities and many nuclear events in this drought-tolerant cultivar, which presumably contributes to the development of the soybean drought tolerance under water deprivation process.
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Pongprayoon, Wasinee, Atikorn Panya, Janthima Jaresitthikunchai, Narumon Phaonakrop, and Sittiruk Roytrakul. "Phosphoprotein Profile of Rice (Oryza sativa L.) Seedlings under Osmotic Stress after Pretreatment with Chitosan." Plants 11, no. 20 (October 15, 2022): 2729. http://dx.doi.org/10.3390/plants11202729.

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This study aims to identify novel chitosan (CTS)-responsive phosphoproteins in Leung Pratew 123 (LPT123) and Khao Dawk Mali 105 (KDML105) as drought-sensitive rice cultivars and differences in the CTS response. Rice seeds were soaked in CTS solution before germination, and 2- and 4-week-old rice seedlings sprayed with CTS before osmotic stress comprised the following four groups: (1) seedlings treated with distilled water; (2) seedlings treated with CTS; (3) seedlings pretreated with distilled water and subjected to osmotic stress; and (4) seedlings pretreated with CTS and subjected to osmotic stress. Phosphoproteins of leaf tissues were enriched using immobilized metal affinity chromatography (IMAC) before tryptic digestion and analysis via LC-MS. Phosphoprotein profiling analyses led to the identification of 4721 phosphoproteins representing 1052 and 1040 unique phosphoproteins in the LPT123 and KDML105 seedlings, respectively. In response to CTS pretreatment before osmotic stress, 22 differently expressed proteins were discovered, of which 10 and 12 were identified in the LPT123 and KDML105, respectively. These proteins are typically involved in signaling, transport, protein folding, protein degradation, and metabolism. This study provides fruitful data to understand the signal transduction mechanisms of rice seedlings pretreated with CTS before exposure to osmotic stress.
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Ganju, RK, RG Shpektor, DG Brenner, and MA Shipp. "CD10/neutral endopeptidase 24.11 is phosphorylated by casein kinase II and coassociates with other phosphoproteins including the lyn src- related kinase." Blood 88, no. 11 (December 1, 1996): 4159–65. http://dx.doi.org/10.1182/blood.v88.11.4159.4159.

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Abstract CD10/neutral endopeptidase 24.11 (NEP) regulates peptidemediated proliferation of lymphoid progenitors and certain epithelial cells and is itself regulated by cellular proliferation. To further characterize mechanisms by which cell-surface signaling might regulate CD10/NEP expression, we determined whether CD10/NEP was phosphorylated and whether the enzyme co-associated with additional cellular phosphoproteins. The CD10/NEP cytoplasmic tall contains two consensus recognition sequences for casein kinase II (CKII), a serine and threonine kinase that increases in activity following peptide signaling. In standard in vitro kinase assays, CKII phosphorylated full-length recombinant CD10/NEP but did not phosphorylate a truncated CD10/NEP protein that lacked the transmembrane region and cytoplasmic tail. To determine whether CD10/NEP might interact with additional cellular phosphoproteins, in vitro kinase assays were performed on CD10/NEP immune complexes from Nalm-6 cells. Three additional tyrosine phosphoproteins of approximately 40 kD, approximately 58 kD, and approximately 75 kD were identified in the CD10/NEP immunoprecipitates. The approximately 56-kD CD10/NEP-associated phosphoprotein was immunoprecipitated with an anti-lyn antibody confirming its identity as the lyn src-related kinase. Taken together, these data indicate that CD10/NEP is itself phosphorylated by CKII and that CD10/NEP co- associates with additional tyrosine phosphoproteins including lyn.
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Ganju, RK, RG Shpektor, DG Brenner, and MA Shipp. "CD10/neutral endopeptidase 24.11 is phosphorylated by casein kinase II and coassociates with other phosphoproteins including the lyn src- related kinase." Blood 88, no. 11 (December 1, 1996): 4159–65. http://dx.doi.org/10.1182/blood.v88.11.4159.bloodjournal88114159.

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CD10/neutral endopeptidase 24.11 (NEP) regulates peptidemediated proliferation of lymphoid progenitors and certain epithelial cells and is itself regulated by cellular proliferation. To further characterize mechanisms by which cell-surface signaling might regulate CD10/NEP expression, we determined whether CD10/NEP was phosphorylated and whether the enzyme co-associated with additional cellular phosphoproteins. The CD10/NEP cytoplasmic tall contains two consensus recognition sequences for casein kinase II (CKII), a serine and threonine kinase that increases in activity following peptide signaling. In standard in vitro kinase assays, CKII phosphorylated full-length recombinant CD10/NEP but did not phosphorylate a truncated CD10/NEP protein that lacked the transmembrane region and cytoplasmic tail. To determine whether CD10/NEP might interact with additional cellular phosphoproteins, in vitro kinase assays were performed on CD10/NEP immune complexes from Nalm-6 cells. Three additional tyrosine phosphoproteins of approximately 40 kD, approximately 58 kD, and approximately 75 kD were identified in the CD10/NEP immunoprecipitates. The approximately 56-kD CD10/NEP-associated phosphoprotein was immunoprecipitated with an anti-lyn antibody confirming its identity as the lyn src-related kinase. Taken together, these data indicate that CD10/NEP is itself phosphorylated by CKII and that CD10/NEP co- associates with additional tyrosine phosphoproteins including lyn.
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Dissertations / Theses on the topic "Phosphoproteins"

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Marciniak, Stefan John. "Phosphoproteins of the zymogen granule membrane." Thesis, University of Cambridge, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.243154.

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Poulain, Fabienne. "Stathmin family phosphoproteins and neuronal morphogenesis." Paris 6, 2007. http://www.theses.fr/2007PA066492.

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Le développement des prolongements neuronaux requiert une réorganisation dynamique des microtubules. Les protéines de la famille de la stathmine (dont SCG10, SCLIP et RB3) participent au contrôle de la dynamique des microtubules en séquestrant la tubuline. Leur profil d’expression dans le système nerveux suggère qu’elles jouent des rôles distincts et complémentaires lors de la morphogenèse neuronale. Cette étude visait à mieux comprendre leur diversité fonctionnelle et a permis de caractériser les fonctions spécifiques de SCLIP dans l’axonogenèse et la dendritogenèse. Nous avons ainsi démontré que SCLIP régule la morphogenèse axonale des neurones d’hippocampe différemment d’SCG10, contrôlant le développement de nouvelles branches et non la surface du cône de croissance. Nous avons de plus révélé que SCLIP est fortement exprimée dans les cellules de Purkinje lors du développement du cervelet et joue un rôle primordial dans leur développement dendritique. Ces résultats ouvrent ainsi de nouvelles perspectives quant aux régulations fonctionnelles des protéines de la famille de la stathmine dans les neurones.
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Sheppard, Vonda Chantal. "Identification and characterization of diatom kinases catalyzing the phosphorylation of biomineral forming proteins." Diss., Georgia Institute of Technology, 2010. http://hdl.handle.net/1853/37227.

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Diatoms are unicellular photosynthetic algae that display intricately patterned cell walls made of amorphous silicon dioxide (silica). Long-chain polyamines and highly phosphorylated proteins, silaffins and silacidins, are believed to play an important role in biosilica formation. The phosphate moieties on silaffins and silacidins play a significant role in biomineral formation, yet no kinase has been identified that phosphorylates these biomineral forming proteins. This dissertation describes the characterization of a novel kinase from the diatom Thalassiosira pseudonana, tpSTK1, which is upregulated during silica formation. A recombinantly expressed histidine-tagged version of tpSTK1 was capable of phosphorylating recombinant silaffins but not recombinant silacidin in vitro. Through establishing methods for subcellular fraction of T. pseudonana membranes in combination with antibody inhibition assay, it was discovered that native tpSTK1 phosphorylates silaffins but not silacidins in vitro (i.e. it exhibits the same substrate specificity as recombinant tpSTK1). As tpSTK1 is an abundant protein in the ER lumen (~ 0.5 % of total ER protein) it seems highly likely to function as a silaffin kinase in vivo. TpSTK1 lacks clear sequence homologs in non-diatom organisms and is the first molecularly characterized kinase that appears to be involved in biomineralization. The predicted kinase domain (KD) of tpSTK2, the only T. pseudonana homolog of tpSTK1, was recombinantly expressed and tested for phosphorylation activity. Recombinant tpSTK2-KD and native tpSTK2 exhibited detectable activity with myelin basic protein, but did not phosphorylate silaffins or silacidins in vitro. Western blot analysis demonstrated that native tpSTK2 was not present in the ER, but associated with the cytosol and Golgi membrane containing subcellular fractions.
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Lei, Xia. "Identification and characterization of endosomal specific phosphoproteins." Thesis, McGill University, 1994. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=28483.

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Endosomal fractions isolated from rat liver homogenates harbor membrane-associated kinases that phosphorylate a 48-kDa extrinsic membrane protein and two integral membrane phosphoproteins of 35 and 31 kDa. These phosphoproteins were not detected in subcellular fractions enriched in plasma membranes, endoplasmic reticulum, lysosomes, coated vesicles and cytosol. Although the same phosphoproteins were also found in a mixed Golgi-endosome fraction (Gi), they were not found in endosome-free, highly purified Golgi fractions and were exclusively restricted to endosomes containing internalized horseradish peroxidase as determined by the diaminobenzidine shift protocol, therefore these phosphoproteins are unique to endosomes. Further characterization studies showed the 48-kDa protein was phosphotylated on threonine and the 35 and 31 kDa proteins were phosphorylated on serine residues. None of them were N-glycosylated. The endosomal protein kinase was independent of Ca$ sp{2+},$ cyclic nucleotide and phospholipids and was inhibited by N-ethylmaleimide (NEM). Both ATP and GTP were phosphate donors, and ATP and GTP phosphorylated identical endosomal phosphoproteins as determined by two-dimensional electrophoresis. Because the phosphorylation was not inhibited by heparin, the corresponding kinase may not be casein kinase II. We also observed that upon in vivo administration of saturating dose of EGF, the in vitro phosphorylation activity of the 48, 35, 31 kDa proteins decreased. The endosomal specific membrane phosphoproteins may mediate phosphorylation dependent processes in endosomes in addition to serving as novel markers for the organelle.
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Staubli, Justin Charles. "Development of a phosphoprotein enrichment method to identify and characterize phosphoproteins within leukemia following treatment with the PP2A activator, FTY720." The Ohio State University, 2012. http://rave.ohiolink.edu/etdc/view?acc_num=osu1338269265.

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Chen, Zhaoyuan. "Development of Methods for the Study of Phosphoproteins." Diss., CLICK HERE for online access, 2006. http://contentdm.lib.byu.edu/ETD/image/etd1629.pdf.

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Goswami, Suranjana. "IDENTIFICATION OF PHOSPHOPROTEINS INVOLVED IN SPERM MATURATION AND FERTILITY." Kent State University / OhioLINK, 2018. http://rave.ohiolink.edu/etdc/view?acc_num=kent1532952768427828.

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Sheehan, M. A. "Phosphoproteins in malignant and non-malignant human-human cell hybrids." Thesis, University of Oxford, 1985. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.355800.

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Rothman, Deborah Maria. "Caged phosphopeptides and phosphoproteins : agents in unraveling complex biological pathways." Thesis, Massachusetts Institute of Technology, 2005. http://hdl.handle.net/1721.1/32429.

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Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Chemistry, 2005.
Vita.
Includes bibliographical references.
Within cellular signaling, protein phosphorylation is the post-translational modification most frequently used to regulate protein activity. Protein kinases and phosphoprotein phosphatases generate and terminate these phosphoryl signals, respectively. Chemical approaches for studying protein phosphorylation and the roles of phosphoproteins include photolabile caged analogs of bioactive species. Caged compounds are ideal chemical probes for studying cellular signaling because they afford researchers spatial and temporal control over the release of targeted effector molecules. Ligands or proteins involved in signal transduction can be chemically caged and subsequently irradiated to release a concentration burst of a specific species, allowing the downstream effects to be monitored without disrupting other aspects of the system. The syntheses and applications of caged phosphopeptides and phosphoproteins have been developed and detailed within this thesis. Two methods to synthesize 1-(2-nitrophenyl)ethyl caged phosphopeptides were developed. These peptides demonstrated good quantum yields of uncaging as compared to literature values of other ortho-nitrobenzyl derived caged compounds. A study in which these caged phosphopeptide tools yielded seminal information about the 14-3-3 protein family's involvement in cell cycle control successfully demonstrated the unique utility of these probes. Furthermore, the synthesis that allowed the extension of the nonsense codon suppression methodology to include caged phosphoproteins was developed.
(cont.) The three most commonly phosphorylated amino acids (serine, threonine, and tyrosine) were each incorporated into a test protein in their caged phosphorylated form. Toward studying cell motility, caged phosphoserine was incorporated into position 153 of mVASP for use in live cell assays.
by Deborah Maria Rothman.
Ph.D.
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Neubauer, Gitte Jackie. "Microcharacterisation of multi-protein complexes and phosphoproteins by nanoelectrospray mass spectrometry." Thesis, University of London, 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.299339.

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Books on the topic "Phosphoproteins"

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L, Khandelwal R., and Wang Jerry H, eds. Reversible protein phosphorylation in cell regulation. Dordrecht: Kluwer Academic Publishers, 1993.

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M, Sefton Bartholomew, and Hunter Tony 1943-, eds. Protein phosphorylation. San Diego, Calif: Academic Press, 1998.

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International Conference on Second Messengers and Phosphoproteins (12th 2004 Montréal, Québec). Second messengers and phosphoprotein signaling: Proceedings of the 12th International Conference on Second Messengers and Phosphoproteins : Montreal, Canada, August 3-7, 2004. Edited by Anand-Srivastava Madhu B, Tremblay Michel, and Srivastava Ashok K. Bologna: Medimond International Proceedings, 2004.

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N, Kochetkova M., and Engelʹgardt, V. A. b. 1894., eds. Rolʹ fosforilirovanii͡a︡ v reguli͡a︡t͡s︡ii kletochnoĭ aktivnosti. Moskva: "Nauka", 1985.

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Annamaria, Torriani-Gorini, Yagil Ezra, and Silver S. (Simon), eds. Phosphate in microorganisms: Cellular and molecular biology. Washington, D.C: ASM Press, 1994.

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Steven, Sikes C., Wheeler A. P, American Chemical Society. Division of Industrial and Engineering Chemistry., and American Chemical Society Meeting, eds. Surface reactive peptides and polymers: Discovery and commercialization : developed from a symposium sponsored by the Division of Industrial and Engineering Chemistry at the 197th National Meeting of the American Chemical Society, Dallas, Texas, April 12-13, 1989. Washington, DC: The Society, 1991.

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J, Fielding Christopher, ed. Lipid rafts and caveolae: From membrane biophysics to cell biology. Weinheim: Wiley-VCH, 2006.

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G, Hardie D., ed. Protein phosphorylation: A practical approach. Oxford: Oxford University Press, 1993.

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John, Solaro R., ed. Protein phosphorylation in heart muscle. Boca Raton, Fla: CRC Press, 1986.

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Nam, Yesi. Partial purification and characterization of human sublingual gland protein kinase(s) responsible for phosphorylating secreted salivary phosphoproteins. Ottawa: National Library of Canada, 1996.

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Book chapters on the topic "Phosphoproteins"

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Greengard, Paul. "Neuronal Phosphoproteins." In Molecular Neurobiology, 81–119. Totowa, NJ: Humana Press, 1988. http://dx.doi.org/10.1007/978-1-4612-4604-6_5.

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Puente, Lawrence G., and Lynn A. Megeney. "Isolation of Phosphoproteins." In Methods in Molecular Biology™, 365–72. Totowa, NJ: Humana Press, 2008. http://dx.doi.org/10.1007/978-1-60327-064-9_28.

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Sanz Ressel, Berenice L., and Alfredo A. Molinolo. "Immunohistochemical Techniques for Phosphoproteins." In Methods in Molecular Biology, 259–64. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2811-9_17.

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Veis, Arthur. "Phosphoproteins From Teeth and Bone." In Ciba Foundation Symposium 136 - Cell and Molecular Biology of Vertebrate Hard Tissues, 161–77. Chichester, UK: John Wiley & Sons, Ltd., 2007. http://dx.doi.org/10.1002/9780470513637.ch11.

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Veis, Arthur, Boris Sabsay, and Chou Bing Wu. "Phosphoproteins as Mediators of Biomineralization." In ACS Symposium Series, 1–12. Washington, DC: American Chemical Society, 1991. http://dx.doi.org/10.1021/bk-1991-0444.ch001.

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Rokka, Anne, Eva-Mari Aro, and Alexander V. Vener. "Thylakoid Phosphoproteins: Identification of Phosphorylation Sites." In Methods in Molecular Biology, 171–86. Totowa, NJ: Humana Press, 2010. http://dx.doi.org/10.1007/978-1-60761-925-3_15.

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Holt, C., and R. T. Bailey. "Interaction of Phosphoproteins with Calcium Phosphate." In Springer Series in Biophysics, 169–70. Berlin, Heidelberg: Springer Berlin Heidelberg, 1989. http://dx.doi.org/10.1007/978-3-642-73925-5_33.

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Volovik, O. I., T. T. Nosenko, and S. K. Sytnik. "Control of Chloroplast Electron Transport by Phosphoproteins." In Photosynthesis: Mechanisms and Effects, 2063–66. Dordrecht: Springer Netherlands, 1998. http://dx.doi.org/10.1007/978-94-011-3953-3_483.

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Henjes, Frauke, Frank Götschel, Anika Jöcker, and Ulrike Korf. "Quantitative Analysis of Phosphoproteins Using Microspot Immunoassays." In Methods in Molecular Biology, 191–201. Totowa, NJ: Humana Press, 2011. http://dx.doi.org/10.1007/978-1-61779-286-1_13.

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Bank, B., D. L. Chute, and J. Gurd. "Vertebrate Memory Models: Alterations in Neuronal Phosphoproteins." In Brain Plasticity, Learning, and Memory, 544. Boston, MA: Springer US, 1985. http://dx.doi.org/10.1007/978-1-4684-5003-3_54.

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Conference papers on the topic "Phosphoproteins"

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Baldelli, Elisa, Vienna Ludovini, Lucio Crinò, Lance Liotta, Emanuel Petricoin, and Mariaelena Pierobon. "Abstract 1994: Impact of laser capture microdissection on cancer signaling proteins and phosphoproteins." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-1994.

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Gao, Ming, Ta-Chen Huang, Chi-Long Chen, Hui-Ching Tu, Wen-Chi Feng, Yen-Shen Lu, Pei-Yen Yeh, et al. "Abstract 3761: Tissue processing time affects the expression of phosphoproteins after breast cancer resection." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-3761.

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Mueller, Claudius, Lorenzo Colarossi, Antonella Chiechi, Rosa I. Gallagher, Amy VanMeter, Kirsten H. Edmiston, Frankie A. Holmes, Yasir Nagarwala, Lance A. Liotta, and Virginia A. Espina. "Abstract 1265: Tissue is alive: Preserving phosphoproteins and tissue morphology in clinical trial samples." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-1265.

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Sidhanth, C., Manoj Garg, P. Manasa, S. Krishna Priya, S. Bindhya, S. Sneha, R. P. Nagare, S. Shirley, M. Kanchan, and Trivadi S. Ganesan. "Abstract 212: Identification by mass spectrometry of unique phosphoproteins subsequent to signaling through c-ErbB2." 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.am2017-212.

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Kilmer, Greg, Krishna Vattem, Eric Hommema, Ken Maas, Atul Deshpande, and Brian L. Webb. "Abstract LB-119: Production of functionally active glycoproteins and phosphoproteins based on a novel human in vitro expression system." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-lb-119.

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Hofmann, Marco H., and Klaus-Peter Kuenkele. "Abstract 710: Kinetic of phosphoproteins in the PI3K and MAPK pathway reflect responsiveness of Ewing's Sarcoma cells to R1507, a human IgG1 Mab that binds IGF-IR." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-710.

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Imaoka, T., and T. Asaji. "FUNCTION OF PLATELET 47K PHOSPHOPROTEIN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644634.

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Abstract:
Secretion of platelet granule constituents is closely associated with the phosphorylation of a cytosol polypeptide that we called P47 of Mr 47,000 (Imaoka, T. and Haslam, R.J., J. Biol. Chem. 258, 11404, 1983), by protein kinase C. Since the identity and function remains to be known, we purified protein kinase C, unphosphorylated and phosphorylated P47 to homogeneity from human platelets. Then precise phosphorylation reaction of P47 in vitro and a biological function of P47 were studied. Protein kinase C catalysed the phosphorylation reaction of P47 protein, platelet myosin light chain, histone III-S with Km of 0.8±0.2, 4.2±0.5, 4.7±0.7μM, and Vmax of 0.312, 0.189, 0.874 nmole/min/mg, respectively. Some data previously obtained in this laboratory and others utilizing histone III-S as substrate are consistent with the synergistic effect by diacylglycerol (DG) in the presence of Ca++ , phosphatidylserine (PS). Using P47 as substrate, the enzyme required both Ca++ and PS, but not DG for activity. 125I labelled unphosphorylated P47 had an ability to bind with platelet membrane fraction in the presense of phosphatidylserine. Effect of diacylglycerol was inhibitory in this PS dependent P47 binding with membrane. Unphosphorylated P47 had a inhibitory activity in platelet actin polymerization. Molar ratio to inhibit actin polymerization was 1:8(P47:actin). These activities were Ca++ independent. Purified 32P-labelled P47 lost the binding ability with membrane, also the inhibitory activity in actin polymerization.Therefore, we propose the hypothesis that unphosphorylated P47 may loosely bind with the inside of plasma membrane of platelet and inhibit actin polymerization as a modulator, when stimulated, protein Kinase C rapidly phosphorylate P47 and induce the activation of cytoskeletal network and subsequently release reaction. On the other hand, whether DG in fact can act as a second messenger remain uncertain, (supported by MESC of Japan)
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Psallidas, Ioannis, Keparesia Karabela, Davina Simoes, Sophia Magkouta, Charis Roussos, Ioannis Kalomenidis, and Georgios T. Stathopoulos. "Secreted Phosphoprotein-1 Enhances Urethane-induced Lung Carcinogenesis." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a2521.

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Merlin, J.-L., M. Lion, J. Wong, T. Bachelot, F. André, I. Treilleux, D. Loussouarn, et al. "Abstract P1-08-27: Quantitative analysis of tumor expression of phosphoproteins from PI3-kinase and MAP-kinase signaling pathways as biomarkers of the biological and clinical activity of trastuzumab and everolimus in breast cancer: Unicancer RADHER phase II trial results." In Abstracts: Thirty-Sixth Annual CTRC-AACR San Antonio Breast Cancer Symposium - Dec 10-14, 2013; San Antonio, TX. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/0008-5472.sabcs13-p1-08-27.

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Seewaldt, Victoria L., Catherine Ibarra-Drendall, Patrick Pilie, William Barry, Gloria Broadwater, and Emanuel Petricoin. "Abstract A108: Phosphoprotein network activation during breast cancer initiation." In Abstracts: AACR International Conference on Frontiers in Cancer Prevention Research‐‐ Nov 7-10, 2010; Philadelphia, PA. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1940-6207.prev-10-a108.

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Reports on the topic "Phosphoproteins"

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Routtenberg, Aryeh. Phosphoprotein Regulation of Behavioral Reactivity. Fort Belvoir, VA: Defense Technical Information Center, April 1992. http://dx.doi.org/10.21236/ada250400.

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Routtenberg, Aryeh. Phosphoprotein Regulation of Synaptic Reactivity. Fort Belvoir, VA: Defense Technical Information Center, May 1991. http://dx.doi.org/10.21236/ada237849.

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Routtenberg, Aryeh. Phosphoprotein Regulation of Behavioral Reactivity. Fort Belvoir, VA: Defense Technical Information Center, July 1990. http://dx.doi.org/10.21236/ada228751.

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Kristjansdottir, Kolbrun. Differential Phosphoprotein Profiling of Tamoxifen Response. Fort Belvoir, VA: Defense Technical Information Center, August 2008. http://dx.doi.org/10.21236/ada502498.

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Kristjansdottir, Kolbrun, Stephen J. Kron, and Geoffrey L. Greene. Differential Phosphoprotein Profiling of Tamoxifen Response. Fort Belvoir, VA: Defense Technical Information Center, August 2009. http://dx.doi.org/10.21236/ada524493.

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Kristjansdottir, Kolbrun. Differential Phosphoprotein Profiling of Tamoxifen Response. Fort Belvoir, VA: Defense Technical Information Center, August 2010. http://dx.doi.org/10.21236/ada549243.

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Routtenberg, Aryeh. Phosphoprotein Regulation of Synaptic Reactivity: Enhancement and Control of a Molecular Gating Mechanism. Fort Belvoir, VA: Defense Technical Information Center, February 1987. http://dx.doi.org/10.21236/ada179463.

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Routtenberg, A. Phosphoprotein Regulation of Synaptic Reactivity: Enhancement and Control of a Molecular Gating Mechanism. Fort Belvoir, VA: Defense Technical Information Center, March 1985. http://dx.doi.org/10.21236/ada154511.

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Routtenberg, Aryeh. Phosphoprotein Regulation of Synaptic Reactivity: Enhancement and Control of a Molecular Gating Mechanism. Fort Belvoir, VA: Defense Technical Information Center, April 1985. http://dx.doi.org/10.21236/ada217196.

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