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Showing 1 to 11 of 11 entries
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Differential Targeting of Hsp70 Heat Shock Proteins HSPA6 and HSPA1A with Components of a Protein Disaggregation/Refolding Machine in Differentiated Human Neuronal Cells following Thermal Stress.

Frontiers in neuroscience

Deane CAS, Brown IR.
PMID: 28484369
Front Neurosci. 2017 Apr 24;11:227. doi: 10.3389/fnins.2017.00227. eCollection 2017.

Heat shock proteins (Hsps) co-operate in multi-protein machines that counter protein misfolding and aggregation and involve DNAJ (Hsp40), HSPA (Hsp70), and HSPH (Hsp105α). The HSPA family is a multigene family composed of inducible and constitutively expressed members. Inducible HSPA6...

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Deane CAS, Brown IR. Differential Targeting of Hsp70 Heat Shock Proteins HSPA6 and HSPA1A with Components of a Protein Disaggregation/Refolding Machine in Differentiated Human Neuronal Cells following Thermal Stress. Front Neurosci. 2017;11:227doi: 10.3389/fnins.2017.00227.
Deane, C. A. S., & Brown, I. R. (2017). Differential Targeting of Hsp70 Heat Shock Proteins HSPA6 and HSPA1A with Components of a Protein Disaggregation/Refolding Machine in Differentiated Human Neuronal Cells following Thermal Stress. Frontiers in neuroscience, 11227. https://doi.org/10.3389/fnins.2017.00227
Deane, Catherine A S, and Brown, Ian R. "Differential Targeting of Hsp70 Heat Shock Proteins HSPA6 and HSPA1A with Components of a Protein Disaggregation/Refolding Machine in Differentiated Human Neuronal Cells following Thermal Stress." Frontiers in neuroscience vol. 11 (2017): 227. doi: https://doi.org/10.3389/fnins.2017.00227
Deane CAS, Brown IR. Differential Targeting of Hsp70 Heat Shock Proteins HSPA6 and HSPA1A with Components of a Protein Disaggregation/Refolding Machine in Differentiated Human Neuronal Cells following Thermal Stress. Front Neurosci. 2017 Apr 24;11:227. doi: 10.3389/fnins.2017.00227. eCollection 2017. PMID: 28484369; PMCID: PMC5401876.
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DNAJs: more than substrate delivery to HSPA.

Frontiers in molecular biosciences

Dekker SL, Kampinga HH, Bergink S.
PMID: 26176011
Front Mol Biosci. 2015 Jun 30;2:35. doi: 10.3389/fmolb.2015.00035. eCollection 2015.

Proteins are essential components of cellular life, as building blocks, but also to guide and execute all cellular processes. Proteins require a three-dimensional folding, which is constantly being challenged by their environment. Challenges including elevated temperatures or redox changes...

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Dekker SL, Kampinga HH, Bergink S. DNAJs: more than substrate delivery to HSPA. Front Mol Biosci. 2015;2:35doi: 10.3389/fmolb.2015.00035.
Dekker, S. L., Kampinga, H. H., & Bergink, S. (2015). DNAJs: more than substrate delivery to HSPA. Frontiers in molecular biosciences, 235. https://doi.org/10.3389/fmolb.2015.00035
Dekker, Suzanne L, et al. "DNAJs: more than substrate delivery to HSPA." Frontiers in molecular biosciences vol. 2 (2015): 35. doi: https://doi.org/10.3389/fmolb.2015.00035
Dekker SL, Kampinga HH, Bergink S. DNAJs: more than substrate delivery to HSPA. Front Mol Biosci. 2015 Jun 30;2:35. doi: 10.3389/fmolb.2015.00035. eCollection 2015. PMID: 26176011; PMCID: PMC4485348.
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HSP70 heat shock proteins and environmental stress in Antarctic marine organisms: A mini-review.

Marine genomics

Clark MS, Peck LS.
PMID: 21798167
Mar Genomics. 2009 Mar;2(1):11-8. doi: 10.1016/j.margen.2009.03.003. Epub 2009 Mar 26.

No abstract available.

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Clark MS, Peck LS. HSP70 heat shock proteins and environmental stress in Antarctic marine organisms: A mini-review. Mar Genomics. 2009;2(1):11-8doi: 10.1016/j.margen.2009.03.003.
Clark, M. S., & Peck, L. S. (2009). HSP70 heat shock proteins and environmental stress in Antarctic marine organisms: A mini-review. Marine genomics, 2(1), 11-8. https://doi.org/10.1016/j.margen.2009.03.003
Clark, Melody S, and Peck, Lloyd S. "HSP70 heat shock proteins and environmental stress in Antarctic marine organisms: A mini-review." Marine genomics vol. 2,1 (2009): 11-8. doi: https://doi.org/10.1016/j.margen.2009.03.003
Clark MS, Peck LS. HSP70 heat shock proteins and environmental stress in Antarctic marine organisms: A mini-review. Mar Genomics. 2009 Mar;2(1):11-8. doi: 10.1016/j.margen.2009.03.003. Epub 2009 Mar 26. PMID: 21798167.
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Prognostic significance of heat shock protein 70 expression in early gastric carcinoma.

Korean journal of pathology

Kang Y, Jung WY, Lee H, Jung W, Lee E, Shin BK, Kim A, Kim HK, Kim BH.
PMID: 23837014
Korean J Pathol. 2013 Jun;47(3):219-26. doi: 10.4132/KoreanJPathol.2013.47.3.219. Epub 2013 Jun 25.

BACKGROUND: Overexpression of heat shock protein 70 (HSP70) has been observed in many types of cancer including gastric adenocarcinomas, although the exact role of HSP70 in carcinogenesis remains unclear.METHODS: The study analyzed a total of 458 radical gastrectomy specimens...

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Kang Y, Jung WY, Lee H, et al. Prognostic significance of heat shock protein 70 expression in early gastric carcinoma. Korean J Pathol. 2013;47(3):219-26doi: 10.4132/KoreanJPathol.2013.47.3.219.
Kang, Y., Jung, W. Y., Lee, H., Jung, W., Lee, E., Shin, B. K., Kim, A., Kim, H. K., & Kim, B. H. (2013). Prognostic significance of heat shock protein 70 expression in early gastric carcinoma. Korean journal of pathology, 47(3), 219-26. https://doi.org/10.4132/KoreanJPathol.2013.47.3.219
Kang, Youngran, et al. "Prognostic significance of heat shock protein 70 expression in early gastric carcinoma." Korean journal of pathology vol. 47,3 (2013): 219-26. doi: https://doi.org/10.4132/KoreanJPathol.2013.47.3.219
Kang Y, Jung WY, Lee H, Jung W, Lee E, Shin BK, Kim A, Kim HK, Kim BH. Prognostic significance of heat shock protein 70 expression in early gastric carcinoma. Korean J Pathol. 2013 Jun;47(3):219-26. doi: 10.4132/KoreanJPathol.2013.47.3.219. Epub 2013 Jun 25. PMID: 23837014; PMCID: PMC3701817.
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The expression of FAS-associated factor 1 and heat shock protein 70 in ovarian cancer.

Obstetrics & gynecology science

Kang HJ, Moon HS, Chung HW.
PMID: 25105101
Obstet Gynecol Sci. 2014 Jul;57(4):281-90. doi: 10.5468/ogs.2014.57.4.281. Epub 2014 Jul 15.

OBJECTIVE: In this study, we evaluated the expression of FAS-associated factor 1 (FAF1) and heat shock protein 70 (HSP70) in normal ovary and ovarian cancer, and also analyzed the correlation between FAF1 and HSP70 in ovarian cancer.METHODS: The patient...

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Kang HJ, Moon HS, Chung HW. The expression of FAS-associated factor 1 and heat shock protein 70 in ovarian cancer. Obstet Gynecol Sci. 2014;57(4):281-90doi: 10.5468/ogs.2014.57.4.281.
Kang, H. J., Moon, H. S., & Chung, H. W. (2014). The expression of FAS-associated factor 1 and heat shock protein 70 in ovarian cancer. Obstetrics & gynecology science, 57(4), 281-90. https://doi.org/10.5468/ogs.2014.57.4.281
Kang, Hye-Ju, et al. "The expression of FAS-associated factor 1 and heat shock protein 70 in ovarian cancer." Obstetrics & gynecology science vol. 57,4 (2014): 281-90. doi: https://doi.org/10.5468/ogs.2014.57.4.281
Kang HJ, Moon HS, Chung HW. The expression of FAS-associated factor 1 and heat shock protein 70 in ovarian cancer. Obstet Gynecol Sci. 2014 Jul;57(4):281-90. doi: 10.5468/ogs.2014.57.4.281. Epub 2014 Jul 15. PMID: 25105101; PMCID: PMC4124089.
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Cellular chaperones and folding enzymes are vital contributors to membrane bound replication and movement complexes during plant RNA virus infection.

Frontiers in plant science

Verchot J.
PMID: 23230447
Front Plant Sci. 2012 Dec 06;3:275. doi: 10.3389/fpls.2012.00275. eCollection 2012.

Cellular chaperones and folding enzymes play central roles in the formation of positive-strand and negative-strand RNA virus infection. This article examines the key cellular chaperones and discusses evidence that these factors are diverted from their cellular functions to play...

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Verchot J. Cellular chaperones and folding enzymes are vital contributors to membrane bound replication and movement complexes during plant RNA virus infection. Front Plant Sci. 2012;3:275doi: 10.3389/fpls.2012.00275.
Verchot, J. (2012). Cellular chaperones and folding enzymes are vital contributors to membrane bound replication and movement complexes during plant RNA virus infection. Frontiers in plant science, 3275. https://doi.org/10.3389/fpls.2012.00275
Verchot, Jeanmarie. "Cellular chaperones and folding enzymes are vital contributors to membrane bound replication and movement complexes during plant RNA virus infection." Frontiers in plant science vol. 3 (2012): 275. doi: https://doi.org/10.3389/fpls.2012.00275
Verchot J. Cellular chaperones and folding enzymes are vital contributors to membrane bound replication and movement complexes during plant RNA virus infection. Front Plant Sci. 2012 Dec 06;3:275. doi: 10.3389/fpls.2012.00275. eCollection 2012. PMID: 23230447; PMCID: PMC3515963.
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Pain Relief with Wet Cupping Therapy in Rats is Mediated by Heat Shock Protein 70 and ß-Endorphin.

Iranian journal of medical sciences

Subadi I, Nugraha B, Laswati H, Josomuljono H.
PMID: 28761205
Iran J Med Sci. 2017 Jul;42(4):384-391.

BACKGROUND: Wet cupping therapy is a complementary therapy in pain management. The mechanism of this therapy, however, needs further elucidation. Cells injured by wet cupping therapy seem to stimulate the expression of heat shock protein 70 (HSP70). Its benefit...

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Subadi I, Nugraha B, Laswati H, et al. Pain Relief with Wet Cupping Therapy in Rats is Mediated by Heat Shock Protein 70 and ß-Endorphin. Iran J Med Sci. 2017;42(4):384-391
Subadi, I., Nugraha, B., Laswati, H., & Josomuljono, H. (2017). Pain Relief with Wet Cupping Therapy in Rats is Mediated by Heat Shock Protein 70 and ß-Endorphin. Iranian journal of medical sciences, 42(4), 384-391.
Subadi, Imam, et al. "Pain Relief with Wet Cupping Therapy in Rats is Mediated by Heat Shock Protein 70 and ß-Endorphin." Iranian journal of medical sciences vol. 42,4 (2017): 384-391.
Subadi I, Nugraha B, Laswati H, Josomuljono H. Pain Relief with Wet Cupping Therapy in Rats is Mediated by Heat Shock Protein 70 and ß-Endorphin. Iran J Med Sci. 2017 Jul;42(4):384-391. PMID: 28761205; PMCID: PMC5523046.
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Effects of heme oxygenase-1 upregulation on isoproterenol-induced myocardial infarction.

The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology

Eltobshy SAG, Hussein AM, Elmileegy AA, Askar MH, Khater Y, Metias EF, Helal GM.
PMID: 31080351
Korean J Physiol Pharmacol. 2019 May;23(3):203-217. doi: 10.4196/kjpp.2019.23.3.203. Epub 2019 Apr 24.

The present study was designed to examine the effect of heme oxygenase-1 (HO-1) induction by cobalt protoporphyrin (CoPP) on the cardiac functions and morphology, electrocardiogram (ECG) changes, myocardial antioxidants (superoxide dismutase [SOD] and glutathione [GSH]), and expression of heat...

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Eltobshy SAG, Hussein AM, Elmileegy AA, et al. Effects of heme oxygenase-1 upregulation on isoproterenol-induced myocardial infarction. Korean J Physiol Pharmacol. 2019;23(3):203-217doi: 10.4196/kjpp.2019.23.3.203.
Eltobshy, S. A. G., Hussein, A. M., Elmileegy, A. A., Askar, M. H., Khater, Y., Metias, E. F., & Helal, G. M. (2019). Effects of heme oxygenase-1 upregulation on isoproterenol-induced myocardial infarction. The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology, 23(3), 203-217. https://doi.org/10.4196/kjpp.2019.23.3.203
Eltobshy, Somaia A G, et al. "Effects of heme oxygenase-1 upregulation on isoproterenol-induced myocardial infarction." The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology vol. 23,3 (2019): 203-217. doi: https://doi.org/10.4196/kjpp.2019.23.3.203
Eltobshy SAG, Hussein AM, Elmileegy AA, Askar MH, Khater Y, Metias EF, Helal GM. Effects of heme oxygenase-1 upregulation on isoproterenol-induced myocardial infarction. Korean J Physiol Pharmacol. 2019 May;23(3):203-217. doi: 10.4196/kjpp.2019.23.3.203. Epub 2019 Apr 24. PMID: 31080351; PMCID: PMC6488703.
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Eukaryotic DNAJ/K Database: A Comprehensive Phylogenomic Analysis Platform for the DNAJ/K Family.

Genomics & informatics

Cheong K, Choi J, Choi J, Park J, Jang S, Lee YH.
PMID: 23613683
Genomics Inform. 2013 Mar;11(1):52-4. doi: 10.5808/GI.2013.11.1.52. Epub 2013 Mar 31.

Proteins in DNAJ/K families are ubiquitous, from prokaryotes to eukaryotes, and function as molecular chaperones. For systematic phylogenomics of the DNAJ/K families, we developed the Eukaryotic DNAJ/K Database (EDD). A total of 12,908 DNAJs and 4,886 DNAKs were identified...

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Cheong K, Choi J, Choi J, et al. Eukaryotic DNAJ/K Database: A Comprehensive Phylogenomic Analysis Platform for the DNAJ/K Family. Genomics Inform. 2013;11(1):52-4doi: 10.5808/GI.2013.11.1.52.
Cheong, K., Choi, J., Choi, J., Park, J., Jang, S., & Lee, Y. H. (2013). Eukaryotic DNAJ/K Database: A Comprehensive Phylogenomic Analysis Platform for the DNAJ/K Family. Genomics & informatics, 11(1), 52-4. https://doi.org/10.5808/GI.2013.11.1.52
Cheong, Kyeongchae, et al. "Eukaryotic DNAJ/K Database: A Comprehensive Phylogenomic Analysis Platform for the DNAJ/K Family." Genomics & informatics vol. 11,1 (2013): 52-4. doi: https://doi.org/10.5808/GI.2013.11.1.52
Cheong K, Choi J, Choi J, Park J, Jang S, Lee YH. Eukaryotic DNAJ/K Database: A Comprehensive Phylogenomic Analysis Platform for the DNAJ/K Family. Genomics Inform. 2013 Mar;11(1):52-4. doi: 10.5808/GI.2013.11.1.52. Epub 2013 Mar 31. PMID: 23613683; PMCID: PMC3630386.
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Serum Hsp70 Antigen: Early Diagnosis Marker in Perinatal Asphyxia.

Iranian journal of pediatrics

Boskabadi H, Omidian M, Tavallai S, Mohammadi S, Parizadeh M, Ghayour Mobarhan M, Ferns GA.
PMID: 26196004
Iran J Pediatr. 2015 Apr;25(2):e381. doi: 10.5812/ijp.381. Epub 2015 Apr 18.

BACKGROUND: Perinatal asphyxia is an important cause of mortality and permanent neurological and developmental deficit. Early and accurate diagnosis would help to establish the likely prognosis and may also help in determining the most appropriate treatment. Studies in experimental...

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Boskabadi H, Omidian M, Tavallai S, et al. Serum Hsp70 Antigen: Early Diagnosis Marker in Perinatal Asphyxia. Iran J Pediatr. 2015;25(2):e381doi: 10.5812/ijp.381.
Boskabadi, H., Omidian, M., Tavallai, S., Mohammadi, S., Parizadeh, M., Ghayour Mobarhan, M., & Ferns, G. A. (2015). Serum Hsp70 Antigen: Early Diagnosis Marker in Perinatal Asphyxia. Iranian journal of pediatrics, 25(2), e381. https://doi.org/10.5812/ijp.381
Boskabadi, Hassan, et al. "Serum Hsp70 Antigen: Early Diagnosis Marker in Perinatal Asphyxia." Iranian journal of pediatrics vol. 25,2 (2015): e381. doi: https://doi.org/10.5812/ijp.381
Boskabadi H, Omidian M, Tavallai S, Mohammadi S, Parizadeh M, Ghayour Mobarhan M, Ferns GA. Serum Hsp70 Antigen: Early Diagnosis Marker in Perinatal Asphyxia. Iran J Pediatr. 2015 Apr;25(2):e381. doi: 10.5812/ijp.381. Epub 2015 Apr 18. PMID: 26196004; PMCID: PMC4506008.
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Insights into the molecular mechanism of allostery in Hsp70s.

Frontiers in molecular biosciences

Mayer MP, Kityk R.
PMID: 26539440
Front Mol Biosci. 2015 Oct 20;2:58. doi: 10.3389/fmolb.2015.00058. eCollection 2015.

Hsp70s chaperone an amazing number and variety of cellular protein folding processes. Key to their versatility is the recognition of a short degenerate sequence motif, present in practically all polypeptides, and a bidirectional allosteric intramolecular regulation mechanism linking their...

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Mayer MP, Kityk R. Insights into the molecular mechanism of allostery in Hsp70s. Front Mol Biosci. 2015;2:58doi: 10.3389/fmolb.2015.00058.
Mayer, M. P., & Kityk, R. (2015). Insights into the molecular mechanism of allostery in Hsp70s. Frontiers in molecular biosciences, 258. https://doi.org/10.3389/fmolb.2015.00058
Mayer, Matthias P, and Kityk, Roman. "Insights into the molecular mechanism of allostery in Hsp70s." Frontiers in molecular biosciences vol. 2 (2015): 58. doi: https://doi.org/10.3389/fmolb.2015.00058
Mayer MP, Kityk R. Insights into the molecular mechanism of allostery in Hsp70s. Front Mol Biosci. 2015 Oct 20;2:58. doi: 10.3389/fmolb.2015.00058. eCollection 2015. PMID: 26539440; PMCID: PMC4611139.
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