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Extracellular vesicles - biomarkers and effectors of the cellular interactome in cancer.

Frontiers in pharmacology

Rak J.
PMID: 23508692
Front Pharmacol. 2013 Mar 06;4:21. doi: 10.3389/fphar.2013.00021. eCollection 2013.

In multicellular organisms both health and disease are defined by patterns of communication between the constituent cells. In addition to networks of soluble mediators, cells are also programed to exchange complex messages pre-assembled as multimolecular cargo of membraneous structures...

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Rak J. Extracellular vesicles - biomarkers and effectors of the cellular interactome in cancer. Front Pharmacol. 2013;4:21doi: 10.3389/fphar.2013.00021.
Rak, J. (2013). Extracellular vesicles - biomarkers and effectors of the cellular interactome in cancer. Frontiers in pharmacology, 421. https://doi.org/10.3389/fphar.2013.00021
Rak, Janusz. "Extracellular vesicles - biomarkers and effectors of the cellular interactome in cancer." Frontiers in pharmacology vol. 4 (2013): 21. doi: https://doi.org/10.3389/fphar.2013.00021
Rak J. Extracellular vesicles - biomarkers and effectors of the cellular interactome in cancer. Front Pharmacol. 2013 Mar 06;4:21. doi: 10.3389/fphar.2013.00021. eCollection 2013. PMID: 23508692; PMCID: PMC3589665.
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Autoantibody Repertoire in APECED Patients Targets Two Distinct Subgroups of Proteins.

Frontiers in immunology

Fishman D, Kisand K, Hertel C, Rothe M, Remm A, Pihlap M, Adler P, Vilo J, Peet A, Meloni A, Podkrajsek KT, Battelino T, Bruserud Ø, Wolff ASB, Husebye ES, Kluger N, Krohn K, Ranki A, Peterson H, Hayday A, Peterson P.
PMID: 28861084
Front Immunol. 2017 Aug 16;8:976. doi: 10.3389/fimmu.2017.00976. eCollection 2017.

High titer autoantibodies produced by B lymphocytes are clinically important features of many common autoimmune diseases. APECED patients with deficient autoimmune regulator (AIRE) gene collectively display a broad repertoire of high titer autoantibodies, including some which are pathognomonic for...

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Fishman D, Kisand K, Hertel C, et al. Autoantibody Repertoire in APECED Patients Targets Two Distinct Subgroups of Proteins. Front Immunol. 2017;8:976doi: 10.3389/fimmu.2017.00976.
Fishman, D., Kisand, K., Hertel, C., Rothe, M., Remm, A., Pihlap, M., Adler, P., Vilo, J., Peet, A., Meloni, A., Podkrajsek, K. T., Battelino, T., Bruserud, �. �., Wolff, A. S. B., Husebye, E. S., Kluger, N., Krohn, K., Ranki, A., Peterson, H., Hayday, A., & Peterson, P. (2017). Autoantibody Repertoire in APECED Patients Targets Two Distinct Subgroups of Proteins. Frontiers in immunology, 8976. https://doi.org/10.3389/fimmu.2017.00976
Fishman, Dmytro, et al. "Autoantibody Repertoire in APECED Patients Targets Two Distinct Subgroups of Proteins." Frontiers in immunology vol. 8 (2017): 976. doi: https://doi.org/10.3389/fimmu.2017.00976
Fishman D, Kisand K, Hertel C, Rothe M, Remm A, Pihlap M, Adler P, Vilo J, Peet A, Meloni A, Podkrajsek KT, Battelino T, Bruserud Ø, Wolff ASB, Husebye ES, Kluger N, Krohn K, Ranki A, Peterson H, Hayday A, Peterson P. Autoantibody Repertoire in APECED Patients Targets Two Distinct Subgroups of Proteins. Front Immunol. 2017 Aug 16;8:976. doi: 10.3389/fimmu.2017.00976. eCollection 2017. PMID: 28861084; PMCID: PMC5561390.
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Thylakoid-protein phosphorylation during the life cycle of Scenedesmus obliquus in synchronous culture.

Planta

Hei WG, Senger H.
PMID: 24241856
Planta. 1986 Feb;167(2):233-9. doi: 10.1007/BF00391420.

The phosphorylation of thylakoid proteins, which comprise apoproteins of the light-harvesting chlorophyll a/b-protein complex (LHCP), was investigated in vivo and in vitro during the development of Scenedesmus obliquus in synchronous cultures. The in-vitro and in-vivo protein phosphorylation exhibited a...

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Hei WG, Senger H. Thylakoid-protein phosphorylation during the life cycle of Scenedesmus obliquus in synchronous culture. Planta. 1986;167(2):233-9doi: 10.1007/BF00391420.
Hei, W. G., & Senger, H. (1986). Thylakoid-protein phosphorylation during the life cycle of Scenedesmus obliquus in synchronous culture. Planta, 167(2), 233-9. https://doi.org/10.1007/BF00391420
Hei, W G, and Senger, H. "Thylakoid-protein phosphorylation during the life cycle of Scenedesmus obliquus in synchronous culture." Planta vol. 167,2 (1986): 233-9. doi: https://doi.org/10.1007/BF00391420
Hei WG, Senger H. Thylakoid-protein phosphorylation during the life cycle of Scenedesmus obliquus in synchronous culture. Planta. 1986 Feb;167(2):233-9. doi: 10.1007/BF00391420. PMID: 24241856.
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Global comparison of phosphoproteins in human and rodent hearts: implications for translational studies of myosin light chain and troponin phosphorylations.

SpringerPlus

Kotlo K, Samarel AM, Chen HY, Aldstadt J, Danziger RS.
PMID: 27390648
Springerplus. 2016 Jun 21;5(1):808. doi: 10.1186/s40064-016-2469-x. eCollection 2016.

Cardiac remodeling and failure are regulated by a myriad of cardiac protein phosphorylations. In the present study, cardiac phosphoprotein patterns were examined in rodent and human hearts Left ventricular tissue samples were obtained from human systolic failing (n =...

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Kotlo K, Samarel AM, Chen HY, et al. Global comparison of phosphoproteins in human and rodent hearts: implications for translational studies of myosin light chain and troponin phosphorylations. Springerplus. 2016;5(1):808doi: 10.1186/s40064-016-2469-x.
Kotlo, K., Samarel, A. M., Chen, H. Y., Aldstadt, J., & Danziger, R. S. (2016). Global comparison of phosphoproteins in human and rodent hearts: implications for translational studies of myosin light chain and troponin phosphorylations. SpringerPlus, 5(1), 808. https://doi.org/10.1186/s40064-016-2469-x
Kotlo, K, et al. "Global comparison of phosphoproteins in human and rodent hearts: implications for translational studies of myosin light chain and troponin phosphorylations." SpringerPlus vol. 5,1 (2016): 808. doi: https://doi.org/10.1186/s40064-016-2469-x
Kotlo K, Samarel AM, Chen HY, Aldstadt J, Danziger RS. Global comparison of phosphoproteins in human and rodent hearts: implications for translational studies of myosin light chain and troponin phosphorylations. Springerplus. 2016 Jun 21;5(1):808. doi: 10.1186/s40064-016-2469-x. eCollection 2016. PMID: 27390648; PMCID: PMC4916117.
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Comparative composition and antioxidant activity of Peptide fractions obtained by ultrafiltration of egg yolk protein enzymatic hydrolysates.

Membranes

Chay Pak Ting BP, Mine Y, Juneja LR, Okubo T, Gauthier SF, Pouliot Y.
PMID: 24957729
Membranes (Basel). 2011 Jul 06;1(3):149-61. doi: 10.3390/membranes1030149.

The objective of the study was to compare the antioxidant activity of two distinct hydrolysates and their peptide fractions prepared by ultrafiltration (UF) using membranes with molecular weight cut-off of 5 and 1 kDa. The hydrolysates were a delipidated...

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Chay Pak Ting BP, Mine Y, Juneja LR, et al. Comparative composition and antioxidant activity of Peptide fractions obtained by ultrafiltration of egg yolk protein enzymatic hydrolysates. Membranes (Basel). 2011;1(3):149-61doi: 10.3390/membranes1030149.
Chay Pak Ting, B. P., Mine, Y., Juneja, L. R., Okubo, T., Gauthier, S. F., & Pouliot, Y. (2011). Comparative composition and antioxidant activity of Peptide fractions obtained by ultrafiltration of egg yolk protein enzymatic hydrolysates. Membranes, 1(3), 149-61. https://doi.org/10.3390/membranes1030149
Chay Pak Ting, Bertrand P, et al. "Comparative composition and antioxidant activity of Peptide fractions obtained by ultrafiltration of egg yolk protein enzymatic hydrolysates." Membranes vol. 1,3 (2011): 149-61. doi: https://doi.org/10.3390/membranes1030149
Chay Pak Ting BP, Mine Y, Juneja LR, Okubo T, Gauthier SF, Pouliot Y. Comparative composition and antioxidant activity of Peptide fractions obtained by ultrafiltration of egg yolk protein enzymatic hydrolysates. Membranes (Basel). 2011 Jul 06;1(3):149-61. doi: 10.3390/membranes1030149. PMID: 24957729; PMCID: PMC4021898.
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Protein kinase activity associated with isolated ribosomes from peas and lemna.

Plant physiology

Keates RA, Trewavas AJ.
PMID: 16658845
Plant Physiol. 1974 Jul;54(1):95-9. doi: 10.1104/pp.54.1.95.

Protein kinase (ATP:protein phosphokinase) has been found associated with ribosomes prepared from 5-day-old etiolated pea shoots and sterile cultures of Lemna minor. The enzyme catalyzes the phosphorylation of ribosomal proteins in vitro and may be involved in the formation...

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Keates RA, Trewavas AJ. Protein kinase activity associated with isolated ribosomes from peas and lemna. Plant Physiol. 1974;54(1):95-9doi: 10.1104/pp.54.1.95.
Keates, R. A., & Trewavas, A. J. (1974). Protein kinase activity associated with isolated ribosomes from peas and lemna. Plant physiology, 54(1), 95-9. https://doi.org/10.1104/pp.54.1.95
Keates, R A, and Trewavas, A J. "Protein kinase activity associated with isolated ribosomes from peas and lemna." Plant physiology vol. 54,1 (1974): 95-9. doi: https://doi.org/10.1104/pp.54.1.95
Keates RA, Trewavas AJ. Protein kinase activity associated with isolated ribosomes from peas and lemna. Plant Physiol. 1974 Jul;54(1):95-9. doi: 10.1104/pp.54.1.95. PMID: 16658845; PMCID: PMC541509.
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Phosphorylation of Photosystem II Components, CP43 Apoprotein, D1, D2, and 10 to 11 Kilodalton Protein in Chloroplast Thylakoids of Higher Plants.

Plant physiology

Ikeuchi M, Plumley FG, Inoue Y, Schmidt GW.
PMID: 16665752
Plant Physiol. 1987 Nov;85(3):638-42. doi: 10.1104/pp.85.3.638.

Phosphorylated thylakoid proteins of spinach (Spinacia oleracea L.) and pea (Pisum sativum L.) were solubilized, fractionated by sucrose density gradient centrifugation, and analyzed by gel electrophoresis and crossed immunoelectrophoresis to identify the phosphoproteins. It was found that in addition...

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Ikeuchi M, Plumley FG, Inoue Y, et al. Phosphorylation of Photosystem II Components, CP43 Apoprotein, D1, D2, and 10 to 11 Kilodalton Protein in Chloroplast Thylakoids of Higher Plants. Plant Physiol. 1987;85(3):638-42doi: 10.1104/pp.85.3.638.
Ikeuchi, M., Plumley, F. G., Inoue, Y., & Schmidt, G. W. (1987). Phosphorylation of Photosystem II Components, CP43 Apoprotein, D1, D2, and 10 to 11 Kilodalton Protein in Chloroplast Thylakoids of Higher Plants. Plant physiology, 85(3), 638-42. https://doi.org/10.1104/pp.85.3.638
Ikeuchi, M, et al. "Phosphorylation of Photosystem II Components, CP43 Apoprotein, D1, D2, and 10 to 11 Kilodalton Protein in Chloroplast Thylakoids of Higher Plants." Plant physiology vol. 85,3 (1987): 638-42. doi: https://doi.org/10.1104/pp.85.3.638
Ikeuchi M, Plumley FG, Inoue Y, Schmidt GW. Phosphorylation of Photosystem II Components, CP43 Apoprotein, D1, D2, and 10 to 11 Kilodalton Protein in Chloroplast Thylakoids of Higher Plants. Plant Physiol. 1987 Nov;85(3):638-42. doi: 10.1104/pp.85.3.638. PMID: 16665752; PMCID: PMC1054314.
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Hypoxic stress-induced changes in ribosomes of maize seedling roots.

Plant physiology

Bailey-Serres J, Freeling M.
PMID: 16667823
Plant Physiol. 1990 Nov;94(3):1237-43. doi: 10.1104/pp.94.3.1237.

The hypoxic stress response of Zea mays L. seedling roots involves regulation of gene expression at transcriptional and posttranscriptional levels. We investigated the effect of hypoxia on the translational machinery of seedling roots. The levels of monoribosomes and ribosomal...

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Bailey-Serres J, Freeling M. Hypoxic stress-induced changes in ribosomes of maize seedling roots. Plant Physiol. 1990;94(3):1237-43doi: 10.1104/pp.94.3.1237.
Bailey-Serres, J., & Freeling, M. (1990). Hypoxic stress-induced changes in ribosomes of maize seedling roots. Plant physiology, 94(3), 1237-43. https://doi.org/10.1104/pp.94.3.1237
Bailey-Serres, J, and Freeling, M. "Hypoxic stress-induced changes in ribosomes of maize seedling roots." Plant physiology vol. 94,3 (1990): 1237-43. doi: https://doi.org/10.1104/pp.94.3.1237
Bailey-Serres J, Freeling M. Hypoxic stress-induced changes in ribosomes of maize seedling roots. Plant Physiol. 1990 Nov;94(3):1237-43. doi: 10.1104/pp.94.3.1237. PMID: 16667823; PMCID: PMC1077368.
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The distribution of phosphoproteins in tissues: Part II.

The Journal of physiology

Plimmer RH, Kaya R.
PMID: 16992971
J Physiol. 1909 Jul 23;39(1):45-51. doi: 10.1113/jphysiol.1909.sp001326.

No abstract available.

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Plimmer RH, Kaya R. The distribution of phosphoproteins in tissues: Part II. J Physiol. 1909;39(1):45-51doi: 10.1113/jphysiol.1909.sp001326.
Plimmer, R. H., & Kaya, R. (1909). The distribution of phosphoproteins in tissues: Part II. The Journal of physiology, 39(1), 45-51. https://doi.org/10.1113/jphysiol.1909.sp001326
Plimmer, R H, and Kaya, R. "The distribution of phosphoproteins in tissues: Part II." The Journal of physiology vol. 39,1 (1909): 45-51. doi: https://doi.org/10.1113/jphysiol.1909.sp001326
Plimmer RH, Kaya R. The distribution of phosphoproteins in tissues: Part II. J Physiol. 1909 Jul 23;39(1):45-51. doi: 10.1113/jphysiol.1909.sp001326. PMID: 16992971; PMCID: PMC1533675.
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Evidence against roles for phorbol binding protein Munc13-1, ADAM adaptor Eve-1, or vesicle trafficking phosphoproteins Munc18 or NSF as phospho-state-sensitive modulators of phorbol/PKC-activated Alzheimer APP ectodomain shedding.

Molecular neurodegeneration

Ikin AF, Causevic M, Pedrini S, Benson LS, Buxbaum JD, Suzuki T, Lovestone S, Higashiyama S, Mustelin T, Burgoyne RD, Gandy S.
PMID: 18067682
Mol Neurodegener. 2007 Dec 09;2:23. doi: 10.1186/1750-1326-2-23.

BACKGROUND: Shedding of the Alzheimer amyloid precursor protein (APP) ectodomain can be accelerated by phorbol esters, compounds that act via protein kinase C (PKC) or through unconventional phorbol-binding proteins such as Munc13-1. We have previously demonstrated that application of...

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Ikin AF, Causevic M, Pedrini S, et al. Evidence against roles for phorbol binding protein Munc13-1, ADAM adaptor Eve-1, or vesicle trafficking phosphoproteins Munc18 or NSF as phospho-state-sensitive modulators of phorbol/PKC-activated Alzheimer APP ectodomain shedding. Mol Neurodegener. 2007;2:23doi: 10.1186/1750-1326-2-23.
Ikin, A. F., Causevic, M., Pedrini, S., Benson, L. S., Buxbaum, J. D., Suzuki, T., Lovestone, S., Higashiyama, S., Mustelin, T., Burgoyne, R. D., & Gandy, S. (2007). Evidence against roles for phorbol binding protein Munc13-1, ADAM adaptor Eve-1, or vesicle trafficking phosphoproteins Munc18 or NSF as phospho-state-sensitive modulators of phorbol/PKC-activated Alzheimer APP ectodomain shedding. Molecular neurodegeneration, 223. https://doi.org/10.1186/1750-1326-2-23
Ikin, Annat F, et al. "Evidence against roles for phorbol binding protein Munc13-1, ADAM adaptor Eve-1, or vesicle trafficking phosphoproteins Munc18 or NSF as phospho-state-sensitive modulators of phorbol/PKC-activated Alzheimer APP ectodomain shedding." Molecular neurodegeneration vol. 2 (2007): 23. doi: https://doi.org/10.1186/1750-1326-2-23
Ikin AF, Causevic M, Pedrini S, Benson LS, Buxbaum JD, Suzuki T, Lovestone S, Higashiyama S, Mustelin T, Burgoyne RD, Gandy S. Evidence against roles for phorbol binding protein Munc13-1, ADAM adaptor Eve-1, or vesicle trafficking phosphoproteins Munc18 or NSF as phospho-state-sensitive modulators of phorbol/PKC-activated Alzheimer APP ectodomain shedding. Mol Neurodegener. 2007 Dec 09;2:23. doi: 10.1186/1750-1326-2-23. PMID: 18067682; PMCID: PMC2211485.
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A novel phosphoprotein analysis scheme for assessing changes in premalignant and malignant breast cell lines using 2D liquid separations, protein microarrays and tandem mass spectrometry.

Proteomics. Clinical applications

Patwa TH, Wang Y, Miller FR, Goodison S, Pennathur S, Barder TJ, Lubman DM.
PMID: 19194518
Proteomics Clin Appl. 2008;3(1):51-66. doi: 10.1002/prca.200800097.

An analysis of phosphorylation changes that occur during cancer progression would provide insights into the molecular pathways responsible for a malignant phenotype. In this study we employed a novel coupling of 2D-liquid separations and protein microarray technology to reveal...

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Patwa TH, Wang Y, Miller FR, et al. A novel phosphoprotein analysis scheme for assessing changes in premalignant and malignant breast cell lines using 2D liquid separations, protein microarrays and tandem mass spectrometry. Proteomics Clin Appl. 2008;3(1):51-66doi: 10.1002/prca.200800097.
Patwa, T. H., Wang, Y., Miller, F. R., Goodison, S., Pennathur, S., Barder, T. J., & Lubman, D. M. (2008). A novel phosphoprotein analysis scheme for assessing changes in premalignant and malignant breast cell lines using 2D liquid separations, protein microarrays and tandem mass spectrometry. Proteomics. Clinical applications, 3(1), 51-66. https://doi.org/10.1002/prca.200800097
Patwa, Tasneem H, et al. "A novel phosphoprotein analysis scheme for assessing changes in premalignant and malignant breast cell lines using 2D liquid separations, protein microarrays and tandem mass spectrometry." Proteomics. Clinical applications vol. 3,1 (2008): 51-66. doi: https://doi.org/10.1002/prca.200800097
Patwa TH, Wang Y, Miller FR, Goodison S, Pennathur S, Barder TJ, Lubman DM. A novel phosphoprotein analysis scheme for assessing changes in premalignant and malignant breast cell lines using 2D liquid separations, protein microarrays and tandem mass spectrometry. Proteomics Clin Appl. 2008;3(1):51-66. doi: 10.1002/prca.200800097. PMID: 19194518; PMCID: PMC2633720.
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Tissue is alive: New technologies are needed to address the problems of protein biomarker pre-analytical variability.

Proteomics. Clinical applications

Espina V, Mueller C, Edmiston K, Sciro M, Petricoin EF, Liotta LA.
PMID: 20871745
Proteomics Clin Appl. 2009 Aug 01;3(8):874-882. doi: 10.1002/prca.200800001.

Instability of tissue protein biomarkers is a critical issue for molecular profiling. Pre-analytical variables during tissue procurement, such as time delays during which the tissue remains stored at room temperature, can cause significant variability and bias in downstream molecular...

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Espina V, Mueller C, Edmiston K, et al. Tissue is alive: New technologies are needed to address the problems of protein biomarker pre-analytical variability. Proteomics Clin Appl. 2009;3(8):874-882doi: 10.1002/prca.200800001.
Espina, V., Mueller, C., Edmiston, K., Sciro, M., Petricoin, E. F., & Liotta, L. A. (2009). Tissue is alive: New technologies are needed to address the problems of protein biomarker pre-analytical variability. Proteomics. Clinical applications, 3(8), 874-882. https://doi.org/10.1002/prca.200800001
Espina, Virginia, et al. "Tissue is alive: New technologies are needed to address the problems of protein biomarker pre-analytical variability." Proteomics. Clinical applications vol. 3,8 (2009): 874-882. doi: https://doi.org/10.1002/prca.200800001
Espina V, Mueller C, Edmiston K, Sciro M, Petricoin EF, Liotta LA. Tissue is alive: New technologies are needed to address the problems of protein biomarker pre-analytical variability. Proteomics Clin Appl. 2009 Aug 01;3(8):874-882. doi: 10.1002/prca.200800001. PMID: 20871745; PMCID: PMC2944287.
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Showing 1 to 12 of 293 entries