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Recurrent Sleep Fragmentation Induces Insulin and Neuroprotective Mechanisms in Middle-Aged Flies.

Frontiers in aging neuroscience

Williams MJ, Perland E, Eriksson MM, Carlsson J, Erlandsson D, Laan L, Mahebali T, Potter E, Frediksson R, Benedict C, Schiöth HB.
PMID: 27531979
Front Aging Neurosci. 2016 Aug 02;8:180. doi: 10.3389/fnagi.2016.00180. eCollection 2016.

Lack of quality sleep increases central nervous system oxidative stress and impairs removal of neurotoxic soluble metabolites from brain parenchyma. During aging poor sleep quality, caused by sleep fragmentation, increases central nervous system cellular stress. Currently, it is not...

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Williams MJ, Perland E, Eriksson MM, et al. Recurrent Sleep Fragmentation Induces Insulin and Neuroprotective Mechanisms in Middle-Aged Flies. Front Aging Neurosci. 2016;8:180doi: 10.3389/fnagi.2016.00180.
Williams, M. J., Perland, E., Eriksson, M. M., Carlsson, J., Erlandsson, D., Laan, L., Mahebali, T., Potter, E., Frediksson, R., Benedict, C., & Schiöth, H. B. (2016). Recurrent Sleep Fragmentation Induces Insulin and Neuroprotective Mechanisms in Middle-Aged Flies. Frontiers in aging neuroscience, 8180. https://doi.org/10.3389/fnagi.2016.00180
Williams, Michael J, et al. "Recurrent Sleep Fragmentation Induces Insulin and Neuroprotective Mechanisms in Middle-Aged Flies." Frontiers in aging neuroscience vol. 8 (2016): 180. doi: https://doi.org/10.3389/fnagi.2016.00180
Williams MJ, Perland E, Eriksson MM, Carlsson J, Erlandsson D, Laan L, Mahebali T, Potter E, Frediksson R, Benedict C, Schiöth HB. Recurrent Sleep Fragmentation Induces Insulin and Neuroprotective Mechanisms in Middle-Aged Flies. Front Aging Neurosci. 2016 Aug 02;8:180. doi: 10.3389/fnagi.2016.00180. eCollection 2016. PMID: 27531979; PMCID: PMC4969361.
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The Diverse AAA+ Machines that Repair Inhibited Rubisco Active Sites.

Frontiers in molecular biosciences

Mueller-Cajar O.
PMID: 28580359
Front Mol Biosci. 2017 May 19;4:31. doi: 10.3389/fmolb.2017.00031. eCollection 2017.

Gaseous carbon dioxide enters the biosphere almost exclusively via the active site of the enzyme ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco). This highly conserved catalyst has an almost universal propensity to non-productively interact with its substrate ribulose 1,5-bisphosphate, leading to the...

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Mueller-Cajar O. The Diverse AAA+ Machines that Repair Inhibited Rubisco Active Sites. Front Mol Biosci. 2017;4:31doi: 10.3389/fmolb.2017.00031.
Mueller-Cajar, O. (2017). The Diverse AAA+ Machines that Repair Inhibited Rubisco Active Sites. Frontiers in molecular biosciences, 431. https://doi.org/10.3389/fmolb.2017.00031
Mueller-Cajar, Oliver. "The Diverse AAA+ Machines that Repair Inhibited Rubisco Active Sites." Frontiers in molecular biosciences vol. 4 (2017): 31. doi: https://doi.org/10.3389/fmolb.2017.00031
Mueller-Cajar O. The Diverse AAA+ Machines that Repair Inhibited Rubisco Active Sites. Front Mol Biosci. 2017 May 19;4:31. doi: 10.3389/fmolb.2017.00031. eCollection 2017. PMID: 28580359; PMCID: PMC5437159.
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Multifunctional DDX3: dual roles in various cancer development and its related signaling pathways.

American journal of cancer research

Zhao L, Mao Y, Zhou J, Zhao Y, Cao Y, Chen X.
PMID: 27186411
Am J Cancer Res. 2016 Jan 15;6(2):387-402. eCollection 2016.

DEAD-box RNA helicase 3 (DDX3) is a highly conserved family member of DEAD-box protein, which is a cluster of ATP-dependent and the largest family of RNA helicase. DEAD-box family is characterized by the regulation of ATPase and helicase activities,...

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Zhao L, Mao Y, Zhou J, et al. Multifunctional DDX3: dual roles in various cancer development and its related signaling pathways. Am J Cancer Res. 2016;6(2):387-402
Zhao, L., Mao, Y., Zhou, J., Zhao, Y., Cao, Y., & Chen, X. (2016). Multifunctional DDX3: dual roles in various cancer development and its related signaling pathways. American journal of cancer research, 6(2), 387-402.
Zhao, Luqing, et al. "Multifunctional DDX3: dual roles in various cancer development and its related signaling pathways." American journal of cancer research vol. 6,2 (2016): 387-402.
Zhao L, Mao Y, Zhou J, Zhao Y, Cao Y, Chen X. Multifunctional DDX3: dual roles in various cancer development and its related signaling pathways. Am J Cancer Res. 2016 Jan 15;6(2):387-402. eCollection 2016. PMID: 27186411; PMCID: PMC4859668.
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Ototoxicity-induced loss of hearing and inner hair cells is attenuated by HSP70 gene transfer.

Molecular therapy. Methods & clinical development

Takada Y, Takada T, Lee MY, Swiderski DL, Kabara LL, Dolan DF, Raphael Y.
PMID: 26029729
Mol Ther Methods Clin Dev. 2015 May 27;2:15019. doi: 10.1038/mtm.2015.19. eCollection 2015.

The most common reason for sensorineural deafness is death of hair cells (HCs). Heat shock proteins (HSPs) are molecular chaperones that participate in folding, targeting, and degrading proteins. HSP expression is increased in response to various environmental stresses to...

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Takada Y, Takada T, Lee MY, et al. Ototoxicity-induced loss of hearing and inner hair cells is attenuated by HSP70 gene transfer. Mol Ther Methods Clin Dev. 2015;2:15019doi: 10.1038/mtm.2015.19.
Takada, Y., Takada, T., Lee, M. Y., Swiderski, D. L., Kabara, L. L., Dolan, D. F., & Raphael, Y. (2015). Ototoxicity-induced loss of hearing and inner hair cells is attenuated by HSP70 gene transfer. Molecular therapy. Methods & clinical development, 215019. https://doi.org/10.1038/mtm.2015.19
Takada, Yohei, et al. "Ototoxicity-induced loss of hearing and inner hair cells is attenuated by HSP70 gene transfer." Molecular therapy. Methods & clinical development vol. 2 (2015): 15019. doi: https://doi.org/10.1038/mtm.2015.19
Takada Y, Takada T, Lee MY, Swiderski DL, Kabara LL, Dolan DF, Raphael Y. Ototoxicity-induced loss of hearing and inner hair cells is attenuated by HSP70 gene transfer. Mol Ther Methods Clin Dev. 2015 May 27;2:15019. doi: 10.1038/mtm.2015.19. eCollection 2015. PMID: 26029729; PMCID: PMC4445521.
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The role of s-nitrosylation and s-glutathionylation of protein disulphide isomerase in protein misfolding and neurodegeneration.

International journal of cell biology

Halloran M, Parakh S, Atkin JD.
PMID: 24348565
Int J Cell Biol. 2013;2013:797914. doi: 10.1155/2013/797914. Epub 2013 Nov 18.

Neurodegenerative diseases involve the progressive loss of neurons, and a pathological hallmark is the presence of abnormal inclusions containing misfolded proteins. Although the precise molecular mechanisms triggering neurodegeneration remain unclear, endoplasmic reticulum (ER) stress, elevated oxidative and nitrosative stress,...

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Halloran M, Parakh S, Atkin JD. The role of s-nitrosylation and s-glutathionylation of protein disulphide isomerase in protein misfolding and neurodegeneration. Int J Cell Biol. 2013;2013:797914doi: 10.1155/2013/797914.
Halloran, M., Parakh, S., & Atkin, J. D. (2013). The role of s-nitrosylation and s-glutathionylation of protein disulphide isomerase in protein misfolding and neurodegeneration. International journal of cell biology, 2013797914. https://doi.org/10.1155/2013/797914
Halloran, M, et al. "The role of s-nitrosylation and s-glutathionylation of protein disulphide isomerase in protein misfolding and neurodegeneration." International journal of cell biology vol. 2013 (2013): 797914. doi: https://doi.org/10.1155/2013/797914
Halloran M, Parakh S, Atkin JD. The role of s-nitrosylation and s-glutathionylation of protein disulphide isomerase in protein misfolding and neurodegeneration. Int J Cell Biol. 2013;2013:797914. doi: 10.1155/2013/797914. Epub 2013 Nov 18. PMID: 24348565; PMCID: PMC3852308.
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Conditional Depletion of the Chlamydomonas Chloroplast ClpP Protease Activates Nuclear Genes Involved in Autophagy and Plastid Protein Quality Control.

The Plant cell

Ramundo S, Casero D, Mühlhaus T, Hemme D, Sommer F, Crèvecoeur M, Rahire M, Schroda M, Rusch J, Goodenough U, Pellegrini M, Perez-Perez ME, Crespo JL, Schaad O, Civic N, Rochaix JD.
PMID: 24879428
Plant Cell. 2014 May;26(5):2201-2222. doi: 10.1105/tpc.114.124842. Epub 2014 May 30.

Plastid protein homeostasis is critical during chloroplast biogenesis and responses to changes in environmental conditions. Proteases and molecular chaperones involved in plastid protein quality control are encoded by the nucleus except for the catalytic subunit of ClpP, an evolutionarily...

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Ramundo S, Casero D, Mühlhaus T, et al. Conditional Depletion of the Chlamydomonas Chloroplast ClpP Protease Activates Nuclear Genes Involved in Autophagy and Plastid Protein Quality Control. Plant Cell. 2014;26(5):2201-2222doi: 10.1105/tpc.114.124842.
Ramundo, S., Casero, D., Mühlhaus, T., Hemme, D., Sommer, F., Crèvecoeur, M., Rahire, M., Schroda, M., Rusch, J., Goodenough, U., Pellegrini, M., Perez-Perez, M. E., Crespo, J. L., Schaad, O., Civic, N., & Rochaix, J. D. (2014). Conditional Depletion of the Chlamydomonas Chloroplast ClpP Protease Activates Nuclear Genes Involved in Autophagy and Plastid Protein Quality Control. The Plant cell, 26(5), 2201-2222. https://doi.org/10.1105/tpc.114.124842
Ramundo, Silvia, et al. "Conditional Depletion of the Chlamydomonas Chloroplast ClpP Protease Activates Nuclear Genes Involved in Autophagy and Plastid Protein Quality Control." The Plant cell vol. 26,5 (2014): 2201-2222. doi: https://doi.org/10.1105/tpc.114.124842
Ramundo S, Casero D, Mühlhaus T, Hemme D, Sommer F, Crèvecoeur M, Rahire M, Schroda M, Rusch J, Goodenough U, Pellegrini M, Perez-Perez ME, Crespo JL, Schaad O, Civic N, Rochaix JD. Conditional Depletion of the Chlamydomonas Chloroplast ClpP Protease Activates Nuclear Genes Involved in Autophagy and Plastid Protein Quality Control. Plant Cell. 2014 May;26(5):2201-2222. doi: 10.1105/tpc.114.124842. Epub 2014 May 30. PMID: 24879428; PMCID: PMC4079378.
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The α-Crystallin Domain Containing Genes: Identification, Phylogeny and Expression Profiling in Abiotic Stress, Phytohormone Response and Development in Tomato (Solanum lycopersicum).

Frontiers in plant science

Paul A, Rao S, Mathur S.
PMID: 27066058
Front Plant Sci. 2016 Mar 31;7:426. doi: 10.3389/fpls.2016.00426. eCollection 2016.

The α-crystallin domain (ACD) is an ancient domain conserved among all kingdoms. Plant ACD proteins have roles in abiotic stresses, transcriptional regulation, inhibiting virus movement, and DNA demethylation. An exhaustive in-silico analysis using Hidden Markov Model-based conserved motif search...

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Paul A, Rao S, Mathur S. The α-Crystallin Domain Containing Genes: Identification, Phylogeny and Expression Profiling in Abiotic Stress, Phytohormone Response and Development in Tomato (Solanum lycopersicum). Front Plant Sci. 2016;7:426doi: 10.3389/fpls.2016.00426.
Paul, A., Rao, S., & Mathur, S. (2016). The α-Crystallin Domain Containing Genes: Identification, Phylogeny and Expression Profiling in Abiotic Stress, Phytohormone Response and Development in Tomato (Solanum lycopersicum). Frontiers in plant science, 7426. https://doi.org/10.3389/fpls.2016.00426
Paul, Asosii, et al. "The α-Crystallin Domain Containing Genes: Identification, Phylogeny and Expression Profiling in Abiotic Stress, Phytohormone Response and Development in Tomato (Solanum lycopersicum)." Frontiers in plant science vol. 7 (2016): 426. doi: https://doi.org/10.3389/fpls.2016.00426
Paul A, Rao S, Mathur S. The α-Crystallin Domain Containing Genes: Identification, Phylogeny and Expression Profiling in Abiotic Stress, Phytohormone Response and Development in Tomato (Solanum lycopersicum). Front Plant Sci. 2016 Mar 31;7:426. doi: 10.3389/fpls.2016.00426. eCollection 2016. PMID: 27066058; PMCID: PMC4814718.
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Engineering and Evolution of Molecular Chaperones and Protein Disaggregases with Enhanced Activity.

Frontiers in molecular biosciences

Mack KL, Shorter J.
PMID: 27014702
Front Mol Biosci. 2016 Mar 15;3:8. doi: 10.3389/fmolb.2016.00008. eCollection 2016.

Cells have evolved a sophisticated proteostasis network to ensure that proteins acquire and retain their native structure and function. Critical components of this network include molecular chaperones and protein disaggregases, which function to prevent and reverse deleterious protein misfolding....

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Mack KL, Shorter J. Engineering and Evolution of Molecular Chaperones and Protein Disaggregases with Enhanced Activity. Front Mol Biosci. 2016;3:8doi: 10.3389/fmolb.2016.00008.
Mack, K. L., & Shorter, J. (2016). Engineering and Evolution of Molecular Chaperones and Protein Disaggregases with Enhanced Activity. Frontiers in molecular biosciences, 38. https://doi.org/10.3389/fmolb.2016.00008
Mack, Korrie L, and Shorter, James. "Engineering and Evolution of Molecular Chaperones and Protein Disaggregases with Enhanced Activity." Frontiers in molecular biosciences vol. 3 (2016): 8. doi: https://doi.org/10.3389/fmolb.2016.00008
Mack KL, Shorter J. Engineering and Evolution of Molecular Chaperones and Protein Disaggregases with Enhanced Activity. Front Mol Biosci. 2016 Mar 15;3:8. doi: 10.3389/fmolb.2016.00008. eCollection 2016. PMID: 27014702; PMCID: PMC4791398.
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The nucleotide exchange factors of Hsp70 molecular chaperones.

Frontiers in molecular biosciences

Bracher A, Verghese J.
PMID: 26913285
Front Mol Biosci. 2015 Apr 07;2:10. doi: 10.3389/fmolb.2015.00010. eCollection 2015.

Molecular chaperones of the Hsp70 family form an important hub in the cellular protein folding networks in bacteria and eukaryotes, connecting translation with the downstream machineries of protein folding and degradation. The Hsp70 folding cycle is driven by two...

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Bracher A, Verghese J. The nucleotide exchange factors of Hsp70 molecular chaperones. Front Mol Biosci. 2015;2:10doi: 10.3389/fmolb.2015.00010.
Bracher, A., & Verghese, J. (2015). The nucleotide exchange factors of Hsp70 molecular chaperones. Frontiers in molecular biosciences, 210. https://doi.org/10.3389/fmolb.2015.00010
Bracher, Andreas, and Verghese, Jacob. "The nucleotide exchange factors of Hsp70 molecular chaperones." Frontiers in molecular biosciences vol. 2 (2015): 10. doi: https://doi.org/10.3389/fmolb.2015.00010
Bracher A, Verghese J. The nucleotide exchange factors of Hsp70 molecular chaperones. Front Mol Biosci. 2015 Apr 07;2:10. doi: 10.3389/fmolb.2015.00010. eCollection 2015. PMID: 26913285; PMCID: PMC4753570.
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The quantitative changes in the yeast Hsp70 and Hsp90 interactomes upon DNA damage.

Data in brief

Truman AW, Kristjansdottir K, Wolfgeher D, Ricco N, Mayampurath A, Volchenboum SL, Clotet J, Kron SJ.
PMID: 26217697
Data Brief. 2014 Nov 07;2:12-5. doi: 10.1016/j.dib.2014.10.006. eCollection 2015 Mar.

The molecular chaperones Hsp70 and Hsp90 participate in many important cellular processes, including how cells respond to DNA damage. Here we show the results of applied quantitative affinity-purification mass spectrometry (AP-MS) proteomics to understand the protein network through which...

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Truman AW, Kristjansdottir K, Wolfgeher D, et al. The quantitative changes in the yeast Hsp70 and Hsp90 interactomes upon DNA damage. Data Brief. 2014;2:12-5doi: 10.1016/j.dib.2014.10.006.
Truman, A. W., Kristjansdottir, K., Wolfgeher, D., Ricco, N., Mayampurath, A., Volchenboum, S. L., Clotet, J., & Kron, S. J. (2015). The quantitative changes in the yeast Hsp70 and Hsp90 interactomes upon DNA damage. Data in brief, 212-5. https://doi.org/10.1016/j.dib.2014.10.006
Truman, Andrew W, et al. "The quantitative changes in the yeast Hsp70 and Hsp90 interactomes upon DNA damage." Data in brief vol. 2 (2015): 12-5. doi: https://doi.org/10.1016/j.dib.2014.10.006
Truman AW, Kristjansdottir K, Wolfgeher D, Ricco N, Mayampurath A, Volchenboum SL, Clotet J, Kron SJ. The quantitative changes in the yeast Hsp70 and Hsp90 interactomes upon DNA damage. Data Brief. 2014 Nov 07;2:12-5. doi: 10.1016/j.dib.2014.10.006. eCollection 2015 Mar. PMID: 26217697; PMCID: PMC4459869.
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Tyrosine 601 of Bacillus subtilis DnaK Undergoes Phosphorylation and Is Crucial for Chaperone Activity and Heat Shock Survival.

Frontiers in microbiology

Shi L, Ravikumar V, Derouiche A, Macek B, Mijakovic I.
PMID: 27148221
Front Microbiol. 2016 Apr 19;7:533. doi: 10.3389/fmicb.2016.00533. eCollection 2016.

In order to screen for cellular substrates of the Bacillus subtilis BY-kinase PtkA, and its cognate phosphotyrosine-protein phosphatase PtpZ, we performed a triple Stable Isotope Labeling by Amino acids in Cell culture-based quantitative phosphoproteome analysis. Detected tyrosine phosphorylation sites...

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Shi L, Ravikumar V, Derouiche A, et al. Tyrosine 601 of Bacillus subtilis DnaK Undergoes Phosphorylation and Is Crucial for Chaperone Activity and Heat Shock Survival. Front Microbiol. 2016;7:533doi: 10.3389/fmicb.2016.00533.
Shi, L., Ravikumar, V., Derouiche, A., Macek, B., & Mijakovic, I. (2016). Tyrosine 601 of Bacillus subtilis DnaK Undergoes Phosphorylation and Is Crucial for Chaperone Activity and Heat Shock Survival. Frontiers in microbiology, 7533. https://doi.org/10.3389/fmicb.2016.00533
Shi, Lei, et al. "Tyrosine 601 of Bacillus subtilis DnaK Undergoes Phosphorylation and Is Crucial for Chaperone Activity and Heat Shock Survival." Frontiers in microbiology vol. 7 (2016): 533. doi: https://doi.org/10.3389/fmicb.2016.00533
Shi L, Ravikumar V, Derouiche A, Macek B, Mijakovic I. Tyrosine 601 of Bacillus subtilis DnaK Undergoes Phosphorylation and Is Crucial for Chaperone Activity and Heat Shock Survival. Front Microbiol. 2016 Apr 19;7:533. doi: 10.3389/fmicb.2016.00533. eCollection 2016. PMID: 27148221; PMCID: PMC4835898.
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Evolutionary and acclimation-induced variation in the heat-shock responses of congeneric marine snails (genus Tegula) from different thermal habitats: implications for limits of thermotolerance and biogeography.

The Journal of experimental biology

Tomanek L, Somero GN.
PMID: 10518474
J Exp Biol. 1999;202:2925-2936.

Heat stress sufficient to cause cellular damage triggers the heat-shock response, the enhanced expression of a group of molecular chaperones called heat-shock proteins (hsps). We compared the heat-shock responses of four species of marine snails of the genus Tegula...

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Tomanek L, Somero GN. Evolutionary and acclimation-induced variation in the heat-shock responses of congeneric marine snails (genus Tegula) from different thermal habitats: implications for limits of thermotolerance and biogeography. J Exp Biol. 1999;202:2925-2936
Tomanek, L., & Somero, G. N. (1999). Evolutionary and acclimation-induced variation in the heat-shock responses of congeneric marine snails (genus Tegula) from different thermal habitats: implications for limits of thermotolerance and biogeography. The Journal of experimental biology, 2022925-2936.
Tomanek, and Somero. "Evolutionary and acclimation-induced variation in the heat-shock responses of congeneric marine snails (genus Tegula) from different thermal habitats: implications for limits of thermotolerance and biogeography." The Journal of experimental biology vol. 202 (1999): 2925-2936.
Tomanek L, Somero GN. Evolutionary and acclimation-induced variation in the heat-shock responses of congeneric marine snails (genus Tegula) from different thermal habitats: implications for limits of thermotolerance and biogeography. J Exp Biol. 1999;202:2925-2936. PMID: 10518474.
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Showing 1 to 12 of 528 entries