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Showing 1 to 12 of 673 entries
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Interaction of peroxiredoxin V with dihydrolipoamide branched chain transacylase E2 (DBT) in mouse kidney under hypoxia.

Proteome science

Ahn SH, Yang HY, Tran GB, Kwon J, Son KY, Kim S, Dinh QT, Jung S, Lee HM, Cho KO, Lee TH.
PMID: 25670924
Proteome Sci. 2015 Feb 05;13:4. doi: 10.1186/s12953-014-0061-2. eCollection 2015.

BACKGROUND: Peroxiredoxin V (Prdx V) plays a major role in preventing oxidative damage as an effective antioxidant protein within a variety of cells through peroxidase activity. However, the function of Prdx V is not limited to peroxidase enzymatic activity...

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Ahn SH, Yang HY, Tran GB, et al. Interaction of peroxiredoxin V with dihydrolipoamide branched chain transacylase E2 (DBT) in mouse kidney under hypoxia. Proteome Sci. 2015;13:4doi: 10.1186/s12953-014-0061-2.
Ahn, S. H., Yang, H. Y., Tran, G. B., Kwon, J., Son, K. Y., Kim, S., Dinh, Q. T., Jung, S., Lee, H. M., Cho, K. O., & Lee, T. H. (2015). Interaction of peroxiredoxin V with dihydrolipoamide branched chain transacylase E2 (DBT) in mouse kidney under hypoxia. Proteome science, 134. https://doi.org/10.1186/s12953-014-0061-2
Ahn, Sun Hee, et al. "Interaction of peroxiredoxin V with dihydrolipoamide branched chain transacylase E2 (DBT) in mouse kidney under hypoxia." Proteome science vol. 13 (2015): 4. doi: https://doi.org/10.1186/s12953-014-0061-2
Ahn SH, Yang HY, Tran GB, Kwon J, Son KY, Kim S, Dinh QT, Jung S, Lee HM, Cho KO, Lee TH. Interaction of peroxiredoxin V with dihydrolipoamide branched chain transacylase E2 (DBT) in mouse kidney under hypoxia. Proteome Sci. 2015 Feb 05;13:4. doi: 10.1186/s12953-014-0061-2. eCollection 2015. PMID: 25670924; PMCID: PMC4323032.
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Proteomic analysis of early salt stress responsive proteins in alfalfa roots and shoots.

Proteome science

Xiong J, Sun Y, Yang Q, Tian H, Zhang H, Liu Y, Chen M.
PMID: 29093645
Proteome Sci. 2017 Oct 30;15:19. doi: 10.1186/s12953-017-0127-z. eCollection 2017.

BACKGROUND: Alfalfa (METHOD: A two-dimensional gel electrophoresis (2-DE)-based proteomic technique was employed to identify the differentially abundant proteins (DAPs) from salt-treated alfalfa roots and shoots of the salt tolerance cultivars Zhongmu No 1 cultivar, which was subjected to a...

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Xiong J, Sun Y, Yang Q, et al. Proteomic analysis of early salt stress responsive proteins in alfalfa roots and shoots. Proteome Sci. 2017;15:19doi: 10.1186/s12953-017-0127-z.
Xiong, J., Sun, Y., Yang, Q., Tian, H., Zhang, H., Liu, Y., & Chen, M. (2017). Proteomic analysis of early salt stress responsive proteins in alfalfa roots and shoots. Proteome science, 1519. https://doi.org/10.1186/s12953-017-0127-z
Xiong, Junbo, et al. "Proteomic analysis of early salt stress responsive proteins in alfalfa roots and shoots." Proteome science vol. 15 (2017): 19. doi: https://doi.org/10.1186/s12953-017-0127-z
Xiong J, Sun Y, Yang Q, Tian H, Zhang H, Liu Y, Chen M. Proteomic analysis of early salt stress responsive proteins in alfalfa roots and shoots. Proteome Sci. 2017 Oct 30;15:19. doi: 10.1186/s12953-017-0127-z. eCollection 2017. PMID: 29093645; PMCID: PMC5663070.
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The effect of microbial challenge on the intestinal proteome of broiler chickens.

Proteome science

O'Reilly EL, Burchmore RJ, Sparks NH, Eckersall PD.
PMID: 28572745
Proteome Sci. 2017 May 30;15:10. doi: 10.1186/s12953-017-0118-0. eCollection 2016.

BACKGROUND: In poultry production intestinal health and function is paramount to achieving efficient feed utilisation and growth. Uncovering the localised molecular mechanisms that occur during the early and important periods of growth that allow birds to grow optimally is...

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O'Reilly EL, Burchmore RJ, Sparks NH, et al. The effect of microbial challenge on the intestinal proteome of broiler chickens. Proteome Sci. 2017;15:10doi: 10.1186/s12953-017-0118-0.
O'Reilly, E. L., Burchmore, R. J., Sparks, N. H., & Eckersall, P. D. (2016). The effect of microbial challenge on the intestinal proteome of broiler chickens. Proteome science, 1510. https://doi.org/10.1186/s12953-017-0118-0
O'Reilly, Emily L, et al. "The effect of microbial challenge on the intestinal proteome of broiler chickens." Proteome science vol. 15 (2016): 10. doi: https://doi.org/10.1186/s12953-017-0118-0
O'Reilly EL, Burchmore RJ, Sparks NH, Eckersall PD. The effect of microbial challenge on the intestinal proteome of broiler chickens. Proteome Sci. 2017 May 30;15:10. doi: 10.1186/s12953-017-0118-0. eCollection 2016. PMID: 28572745; PMCID: PMC5450085.
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Spatial proteomic and phospho-proteomic organization in three prototypical cell migration modes.

Proteome science

Fengos G, Schmidt A, Martin K, Fluri E, Aebersold R, Iber D, Pertz O.
PMID: 24987309
Proteome Sci. 2014 May 01;12:23. doi: 10.1186/1477-5956-12-23. eCollection 2014.

BACKGROUND: Tight spatio-temporal signaling of cytoskeletal and adhesion dynamics is required for localized membrane protrusion that drives directed cell migration. Different ensembles of proteins are therefore likely to get recruited and phosphorylated in membrane protrusions in response to specific...

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Fengos G, Schmidt A, Martin K, et al. Spatial proteomic and phospho-proteomic organization in three prototypical cell migration modes. Proteome Sci. 2014;12:23doi: 10.1186/1477-5956-12-23.
Fengos, G., Schmidt, A., Martin, K., Fluri, E., Aebersold, R., Iber, D., & Pertz, O. (2014). Spatial proteomic and phospho-proteomic organization in three prototypical cell migration modes. Proteome science, 1223. https://doi.org/10.1186/1477-5956-12-23
Fengos, Georgios, et al. "Spatial proteomic and phospho-proteomic organization in three prototypical cell migration modes." Proteome science vol. 12 (2014): 23. doi: https://doi.org/10.1186/1477-5956-12-23
Fengos G, Schmidt A, Martin K, Fluri E, Aebersold R, Iber D, Pertz O. Spatial proteomic and phospho-proteomic organization in three prototypical cell migration modes. Proteome Sci. 2014 May 01;12:23. doi: 10.1186/1477-5956-12-23. eCollection 2014. PMID: 24987309; PMCID: PMC4077045.
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Plasma protein profiling of Mild Cognitive Impairment and Alzheimer's disease using iTRAQ quantitative proteomics.

Proteome science

Song F, Poljak A, Kochan NA, Raftery M, Brodaty H, Smythe GA, Sachdev PS.
PMID: 24433274
Proteome Sci. 2014 Jan 17;12(1):5. doi: 10.1186/1477-5956-12-5.

BACKGROUND: With the promise of disease modifying treatments, there is a need for more specific diagnosis and prognosis of Alzheimer's disease (AD) and mild cognitive impairment (MCI). Plasma biomarkers are likely to be utilised to increase diagnostic accuracy and...

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Song F, Poljak A, Kochan NA, et al. Plasma protein profiling of Mild Cognitive Impairment and Alzheimer's disease using iTRAQ quantitative proteomics. Proteome Sci. 2014;12(1):5doi: 10.1186/1477-5956-12-5.
Song, F., Poljak, A., Kochan, N. A., Raftery, M., Brodaty, H., Smythe, G. A., & Sachdev, P. S. (2014). Plasma protein profiling of Mild Cognitive Impairment and Alzheimer's disease using iTRAQ quantitative proteomics. Proteome science, 12(1), 5. https://doi.org/10.1186/1477-5956-12-5
Song, Fei, et al. "Plasma protein profiling of Mild Cognitive Impairment and Alzheimer's disease using iTRAQ quantitative proteomics." Proteome science vol. 12,1 (2014): 5. doi: https://doi.org/10.1186/1477-5956-12-5
Song F, Poljak A, Kochan NA, Raftery M, Brodaty H, Smythe GA, Sachdev PS. Plasma protein profiling of Mild Cognitive Impairment and Alzheimer's disease using iTRAQ quantitative proteomics. Proteome Sci. 2014 Jan 17;12(1):5. doi: 10.1186/1477-5956-12-5. PMID: 24433274; PMCID: PMC3898732.
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The Lottia gigantea shell matrix proteome: re-analysis including MaxQuant iBAQ quantitation and phosphoproteome analysis.

Proteome science

Mann K, Edsinger E.
PMID: 25018669
Proteome Sci. 2014 May 18;12:28. doi: 10.1186/1477-5956-12-28. eCollection 2014.

BACKGROUND: Although the importance of proteins of the biomineral organic matrix and their posttranslational modifications for biomineralization is generally recognized, the number of published matrix proteomes is still small. This is mostly due to the lack of comprehensive sequence...

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Mann K, Edsinger E. The Lottia gigantea shell matrix proteome: re-analysis including MaxQuant iBAQ quantitation and phosphoproteome analysis. Proteome Sci. 2014;12:28doi: 10.1186/1477-5956-12-28.
Mann, K., & Edsinger, E. (2014). The Lottia gigantea shell matrix proteome: re-analysis including MaxQuant iBAQ quantitation and phosphoproteome analysis. Proteome science, 1228. https://doi.org/10.1186/1477-5956-12-28
Mann, Karlheinz, and Edsinger, Eric. "The Lottia gigantea shell matrix proteome: re-analysis including MaxQuant iBAQ quantitation and phosphoproteome analysis." Proteome science vol. 12 (2014): 28. doi: https://doi.org/10.1186/1477-5956-12-28
Mann K, Edsinger E. The Lottia gigantea shell matrix proteome: re-analysis including MaxQuant iBAQ quantitation and phosphoproteome analysis. Proteome Sci. 2014 May 18;12:28. doi: 10.1186/1477-5956-12-28. eCollection 2014. PMID: 25018669; PMCID: PMC4094399.
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Photo-affinity labeling (PAL) in chemical proteomics: a handy tool to investigate protein-protein interactions (PPIs).

Proteome science

Murale DP, Hong SC, Haque MM, Lee JS.
PMID: 28652856
Proteome Sci. 2017 Jun 24;15:14. doi: 10.1186/s12953-017-0123-3. eCollection 2016.

Protein-protein interactions (PPIs) trigger a wide range of biological signaling pathways that are crucial for biomedical research and drug discovery. Various techniques have been used to study specific proteins, including affinity chromatography, activity-based probes, affinity-based probes and photo-affinity labeling...

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Murale DP, Hong SC, Haque MM, et al. Photo-affinity labeling (PAL) in chemical proteomics: a handy tool to investigate protein-protein interactions (PPIs). Proteome Sci. 2017;15:14doi: 10.1186/s12953-017-0123-3.
Murale, D. P., Hong, S. C., Haque, M. M., & Lee, J. S. (2016). Photo-affinity labeling (PAL) in chemical proteomics: a handy tool to investigate protein-protein interactions (PPIs). Proteome science, 1514. https://doi.org/10.1186/s12953-017-0123-3
Murale, Dhiraj P, et al. "Photo-affinity labeling (PAL) in chemical proteomics: a handy tool to investigate protein-protein interactions (PPIs)." Proteome science vol. 15 (2016): 14. doi: https://doi.org/10.1186/s12953-017-0123-3
Murale DP, Hong SC, Haque MM, Lee JS. Photo-affinity labeling (PAL) in chemical proteomics: a handy tool to investigate protein-protein interactions (PPIs). Proteome Sci. 2017 Jun 24;15:14. doi: 10.1186/s12953-017-0123-3. eCollection 2016. PMID: 28652856; PMCID: PMC5483283.
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Proteomic profiling of HBV infected liver biopsies with different fibrotic stages.

Proteome science

Katrinli S, Ozdil K, Sahin A, Ozturk O, Kir G, Baykal AT, Akgun E, Sarac OS, Sokmen M, Doğanay HL, Dinler Doğanay G.
PMID: 28439208
Proteome Sci. 2017 Apr 20;15:7. doi: 10.1186/s12953-017-0114-4. eCollection 2016.

BACKGROUND: Hepatitis B virus (HBV) is a global health problem, and infected patients if left untreated may develop cirrhosis and eventually hepatocellular carcinoma. This study aims to enlighten pathways associated with HBV related liver fibrosis for delineation of potential...

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Katrinli S, Ozdil K, Sahin A, et al. Proteomic profiling of HBV infected liver biopsies with different fibrotic stages. Proteome Sci. 2017;15:7doi: 10.1186/s12953-017-0114-4.
Katrinli, S., Ozdil, K., Sahin, A., Ozturk, O., Kir, G., Baykal, A. T., Akgun, E., Sarac, O. S., Sokmen, M., Doğanay, H. L., & Dinler Doğanay, G. (2016). Proteomic profiling of HBV infected liver biopsies with different fibrotic stages. Proteome science, 157. https://doi.org/10.1186/s12953-017-0114-4
Katrinli, Seyma, et al. "Proteomic profiling of HBV infected liver biopsies with different fibrotic stages." Proteome science vol. 15 (2016): 7. doi: https://doi.org/10.1186/s12953-017-0114-4
Katrinli S, Ozdil K, Sahin A, Ozturk O, Kir G, Baykal AT, Akgun E, Sarac OS, Sokmen M, Doğanay HL, Dinler Doğanay G. Proteomic profiling of HBV infected liver biopsies with different fibrotic stages. Proteome Sci. 2017 Apr 20;15:7. doi: 10.1186/s12953-017-0114-4. eCollection 2016. PMID: 28439208; PMCID: PMC5399407.
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Differential effects of dopamine signalling on long-term memory formation and consolidation in rodent brain.

Proteome science

Reichenbach N, Herrmann U, Kähne T, Schicknick H, Pielot R, Naumann M, Dieterich DC, Gundelfinger ED, Smalla KH, Tischmeyer W.
PMID: 25852303
Proteome Sci. 2015 Mar 18;13:13. doi: 10.1186/s12953-015-0069-2. eCollection 2015.

BACKGROUND: Using auditory discrimination learning in gerbils, we have previously shown that activation of auditory-cortical D1/D5 dopamine receptors facilitates mTOR-mediated, protein synthesis-dependent mechanisms of memory consolidation and anterograde memory formation. To understand molecular mechanisms of this facilitatory effect, we...

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Reichenbach N, Herrmann U, Kähne T, et al. Differential effects of dopamine signalling on long-term memory formation and consolidation in rodent brain. Proteome Sci. 2015;13:13doi: 10.1186/s12953-015-0069-2.
Reichenbach, N., Herrmann, U., Kähne, T., Schicknick, H., Pielot, R., Naumann, M., Dieterich, D. C., Gundelfinger, E. D., Smalla, K. H., & Tischmeyer, W. (2015). Differential effects of dopamine signalling on long-term memory formation and consolidation in rodent brain. Proteome science, 1313. https://doi.org/10.1186/s12953-015-0069-2
Reichenbach, Nicole, et al. "Differential effects of dopamine signalling on long-term memory formation and consolidation in rodent brain." Proteome science vol. 13 (2015): 13. doi: https://doi.org/10.1186/s12953-015-0069-2
Reichenbach N, Herrmann U, Kähne T, Schicknick H, Pielot R, Naumann M, Dieterich DC, Gundelfinger ED, Smalla KH, Tischmeyer W. Differential effects of dopamine signalling on long-term memory formation and consolidation in rodent brain. Proteome Sci. 2015 Mar 18;13:13. doi: 10.1186/s12953-015-0069-2. eCollection 2015. PMID: 25852303; PMCID: PMC4387680.
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Secretome analysis of rice suspension-cultured cells infected by Xanthomonas oryzae pv.oryza (Xoo).

Proteome science

Chen X, Deng Z, Yu C, Yan C, Chen J.
PMID: 26839515
Proteome Sci. 2016 Feb 02;14:2. doi: 10.1186/s12953-016-0091-z. eCollection 2016.

BACKGROUND: Rice bacterial blight (BB) caused by Xanthomonas oryzae pv.oryzae (Xoo) is one of the most devastating bacterial diseases in rice-growing regions worldwide. The rice-Xoo interaction is a classical model for studying the interaction between plants and pathogens. Secreted...

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Chen X, Deng Z, Yu C, et al. Secretome analysis of rice suspension-cultured cells infected by Xanthomonas oryzae pv.oryza (Xoo). Proteome Sci. 2016;14:2doi: 10.1186/s12953-016-0091-z.
Chen, X., Deng, Z., Yu, C., Yan, C., & Chen, J. (2016). Secretome analysis of rice suspension-cultured cells infected by Xanthomonas oryzae pv.oryza (Xoo). Proteome science, 142. https://doi.org/10.1186/s12953-016-0091-z
Chen, Xian, et al. "Secretome analysis of rice suspension-cultured cells infected by Xanthomonas oryzae pv.oryza (Xoo)." Proteome science vol. 14 (2016): 2. doi: https://doi.org/10.1186/s12953-016-0091-z
Chen X, Deng Z, Yu C, Yan C, Chen J. Secretome analysis of rice suspension-cultured cells infected by Xanthomonas oryzae pv.oryza (Xoo). Proteome Sci. 2016 Feb 02;14:2. doi: 10.1186/s12953-016-0091-z. eCollection 2016. PMID: 26839515; PMCID: PMC4735954.
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Label-free quantitative phosphorylation analysis of human transgelin2 in Jurkat T cells reveals distinct phosphorylation patterns under PKA and PKC activation conditions.

Proteome science

Jang SH, Jun CD, Park ZY.
PMID: 25844069
Proteome Sci. 2015 Mar 26;13:14. doi: 10.1186/s12953-015-0070-9. eCollection 2015.

BACKGROUND: Transgelin2, one of cytoskeletal actin binding proteins has recently been suggested to be involved in the formation of immune synapses. Although detailed function of transgelin2 is largely unknown, interactions between transgelin2 and actin appear to be important in...

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Jang SH, Jun CD, Park ZY. Label-free quantitative phosphorylation analysis of human transgelin2 in Jurkat T cells reveals distinct phosphorylation patterns under PKA and PKC activation conditions. Proteome Sci. 2015;13:14doi: 10.1186/s12953-015-0070-9.
Jang, S. H., Jun, C. D., & Park, Z. Y. (2015). Label-free quantitative phosphorylation analysis of human transgelin2 in Jurkat T cells reveals distinct phosphorylation patterns under PKA and PKC activation conditions. Proteome science, 1314. https://doi.org/10.1186/s12953-015-0070-9
Jang, Se Hwan, et al. "Label-free quantitative phosphorylation analysis of human transgelin2 in Jurkat T cells reveals distinct phosphorylation patterns under PKA and PKC activation conditions." Proteome science vol. 13 (2015): 14. doi: https://doi.org/10.1186/s12953-015-0070-9
Jang SH, Jun CD, Park ZY. Label-free quantitative phosphorylation analysis of human transgelin2 in Jurkat T cells reveals distinct phosphorylation patterns under PKA and PKC activation conditions. Proteome Sci. 2015 Mar 26;13:14. doi: 10.1186/s12953-015-0070-9. eCollection 2015. PMID: 25844069; PMCID: PMC4384351.
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Comparative proteomics of Bt-transgenic and non-transgenic cotton leaves.

Proteome science

Wang L, Wang X, Jin X, Jia R, Huang Q, Tan Y, Guo A.
PMID: 25949214
Proteome Sci. 2015 May 02;13:15. doi: 10.1186/s12953-015-0071-8. eCollection 2015.

BACKGROUND: As the rapid growth of the commercialized acreage in genetically modified (GM) crops, the unintended effects of GM crops' biosafety assessment have been given much attention. To investigate whether transgenic events cause unintended effects, comparative proteomics of cotton...

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Wang L, Wang X, Jin X, et al. Comparative proteomics of Bt-transgenic and non-transgenic cotton leaves. Proteome Sci. 2015;13:15doi: 10.1186/s12953-015-0071-8.
Wang, L., Wang, X., Jin, X., Jia, R., Huang, Q., Tan, Y., & Guo, A. (2015). Comparative proteomics of Bt-transgenic and non-transgenic cotton leaves. Proteome science, 1315. https://doi.org/10.1186/s12953-015-0071-8
Wang, Limin, et al. "Comparative proteomics of Bt-transgenic and non-transgenic cotton leaves." Proteome science vol. 13 (2015): 15. doi: https://doi.org/10.1186/s12953-015-0071-8
Wang L, Wang X, Jin X, Jia R, Huang Q, Tan Y, Guo A. Comparative proteomics of Bt-transgenic and non-transgenic cotton leaves. Proteome Sci. 2015 May 02;13:15. doi: 10.1186/s12953-015-0071-8. eCollection 2015. PMID: 25949214; PMCID: PMC4422549.
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Showing 1 to 12 of 673 entries