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Journal articles on the topic 'Heat shock proteins'

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Author: Grafiati

Published: 4 June 2021

Last updated: 26 July 2024

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1

&NA;. "Heat Shock Proteins." Clinical Pulmonary Medicine 1, no. 6 (November 1994): 386. http://dx.doi.org/10.1097/00045413-199411000-00009.

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2

Villar, Jesus, Sergio Ribeiro, and Arthur S. Slutsky. "HEAT SHOCK PROTEINS." Shock 4, Supplement (December 1995): 9. http://dx.doi.org/10.1097/00024382-199512001-00036.

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3

Kaufmann, Stefan H. E. "Heat-shock proteins." Current Opinion in Rheumatology 2, no. 3 (June 1990): 430–35. http://dx.doi.org/10.1097/00002281-199002030-00003.

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4

Schlesinger, M. J. "Heat shock proteins." Journal of Biological Chemistry 265, no. 21 (July 1990): 12111–14. http://dx.doi.org/10.1016/s0021-9258(19)38314-0.

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5

Latchman, DavidS. "Heat-shock proteins." Lancet 337, no. 8738 (February 1991): 424. http://dx.doi.org/10.1016/0140-6736(91)91196-2.

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6

Burdon, R. H. "Heat shock and the heat shock proteins." Biochemical Journal 240, no. 2 (December 1, 1986): 313–24. http://dx.doi.org/10.1042/bj2400313.

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7

Ünver, Ramazan, Figen Deveci, Gamze Kırkıl, Selda Telo, Dilara Kaman, and Mutlu Kuluöztürk. "Serum Heat Shock Protein Levels and the Relationship of Heat Shock Proteins with Various Parameters in Chronic Obstructive Pulmonary Disease Patients." Turkish Thoracic Journal 17, no. 4 (October 10, 2016): 153–59. http://dx.doi.org/10.5578/ttj.30518.

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8

AL-Taee, Anwaar F., and Jamella H. Rasheed. "Expression of Heat Shock Protein HSP90 in Genomic-DNA of Chickpea (Cicer arietinum L.) Callus by Heat Shock Treatment." Academic Journal of Research and Scientific Publishing 3, no. 33 (January 5, 2022): 121–39. http://dx.doi.org/10.52132/ajrsp.e.2022.33.6.

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This study was able to detect of the expression activity of heat shock proteins HSP90 and heat transcription factors HSFs for the first time in callus cultures of chickpea, Cicer arietinum L., that exposed to abiotic shocks, grown on MS medium supplemented with 1.0 mg L-1 naphthalene acetic acid (NAA) and 2.0 mg L-1 benzyl adenine (BA). Heat shock proteins HSPs were constructed for increase of withstand long-term physical shocks, and production of resistant to heat chickpeas plants, this shock was enhancement of tolerance of chickpea callus to abiotic stresses (high - temperatures). Results enhanced the ability of chickpea callus to abiotic stresses bearing and induce of HSF genes to heat shock proteins HSP90 production quickly to removing denatured proteins, avoid apoptosis, thus, supporting tolerance to the sudden action of these shocks. Expression activity of heat shock genes and transcription factors by determined based on polymerase chain reaction qPCR, that explained the gene activity increasing at shocks intensity increased

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9

Kuibida, V. V., P. P. Kokhanets, and V. V. Lopatynska. "Heat shock proteins in adaptation to physical activity." Ukrainian Biochemical Journal 94, no. 2 (July 11, 2022): 5–14. http://dx.doi.org/10.15407/ubj94.02.005.

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The review article presents the author’s model of one of the blocks of the integrated adaptation mechanism to physical activity and the accompanying moderate heat effects. The participation of heat shock proteins in the stabilization of the tertiary structure and in the restoration of the function of proteins damaged by temperature and physical stressors but performing catalytic, transport, reception or protective role and being involved in the processes of contraction- relaxation and muscle and bone tissue remodeling is discussed.

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10

McCallum, Kirk L., John J. Heikkila, and William E. Inniss. "Temperature-dependent pattern of heat shock protein synthesis in psychrophilic and psychrotrophic microorganisms." Canadian Journal of Microbiology 32, no. 6 (June 1, 1986): 516–21. http://dx.doi.org/10.1139/m86-094.

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The patterns of proteins synthesized by the arctic psychrophilic bacterium Res-10 and the psychrotroph Bacillus psychrophilus during various heat shocks up to 32 °C were examined. Both microorganisms were found to display temperature-dependent patterns of heat shock protein synthesis. Elevation of the incubation temperature of the arctic psychrophile from 0 to 15, 20, 25, or 32 °C induced the synthesis of at least 19 heat shock proteins. Imposing similar heat shock upon cells of the psychrotroph resulted in the induction of at least 25 heat shock proteins. Examination of the effect of the transcriptional inhibitor rifampicin on the synthesis of heat shock proteins revealed that the primary control of heat shock protein synthesis lies at the transcriptional level in both microorganisms.

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11

De Maio, Antonio, and Daniel Vazquez. "Extracellular Heat Shock Proteins." Shock 40, no. 4 (October 2013): 239–46. http://dx.doi.org/10.1097/shk.0b013e3182a185ab.

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12

KUKINA, I., T. MIKULOVICH, and O. KULAEVA. "Chloroplast heat shock proteins." Cell Biology International Reports 14 (September 1990): 208. http://dx.doi.org/10.1016/0309-1651(90)90932-o.

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13

Lindquist, S., and E. A. Craig. "The Heat-Shock Proteins." Annual Review of Genetics 22, no. 1 (December 1988): 631–77. http://dx.doi.org/10.1146/annurev.ge.22.120188.003215.

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14

Burdon, R. H. "The heat shock proteins." Endeavour 12, no. 3 (January 1988): 133–38. http://dx.doi.org/10.1016/0160-9327(88)90134-2.

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15

Benjamin, Ivor J., and D. Randy McMillan. "Stress (Heat Shock) Proteins." Circulation Research 83, no. 2 (July 27, 1998): 117–32. http://dx.doi.org/10.1161/01.res.83.2.117.

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16

Kelly, Stephen, and Midori A. Yenari. "Neuroprotection: Heat Shock Proteins." Current Medical Research and Opinion 18, sup2 (January 2002): s55—s60. http://dx.doi.org/10.1185/030079902125000732.

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17

Newport, G., J. Culpepper, and N. Agabian. "Parasite heat-shock proteins." Parasitology Today 4, no. 11 (November 1988): 306–12. http://dx.doi.org/10.1016/0169-4758(88)90111-1.

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18

Feige, U., and J. Mollenhauer. "Heat shock proteins. Introduction." Experientia 48, no. 7 (July 1992): 621–22. http://dx.doi.org/10.1007/bf02118305.

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19

Shan, Qiang, Fengtao Ma, Jingya Wei, Hongyang Li, Hui Ma, and Peng Sun. "Physiological Functions of Heat Shock Proteins." Current Protein & Peptide Science 21, no. 8 (November 9, 2020): 751–60. http://dx.doi.org/10.2174/1389203720666191111113726.

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Heat shock proteins (HSPs) are molecular chaperones involved in a variety of life activities. HSPs function in the refolding of misfolded proteins, thereby contributing to the maintenance of cellular homeostasis. Heat shock factor (HSF) is activated in response to environmental stresses and binds to heat shock elements (HSEs), promoting HSP translation and thus the production of high levels of HSPs to prevent damage to the organism. Here, we summarize the role of molecular chaperones as anti-heat stress molecules and their involvement in immune responses and the modulation of apoptosis. In addition, we review the potential application of HSPs to cancer therapy, general medicine, and the treatment of heart disease.

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20

Giudice, Giovanni. "Heat Shock Proteins in Sea Urchin Embryos. (heat shock proteins/sea urchin embryos)." Development, Growth and Differentiation 31, no. 2 (April 1989): 103–6. http://dx.doi.org/10.1111/j.1440-169x.1989.00103.x.

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21

KNOWLTON, ANNE A. "Heat-Shock Proteins, Stress, and the Heart." Annals of the New York Academy of Sciences 723, no. 1 (June 1994): 128–37. http://dx.doi.org/10.1111/j.1749-6632.1994.tb36722.x.

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22

Öncel, Müfide. "Heat Shock Proteins and Cancer." European Journal of Basic Medical Sciences 2, no. 1 (March 1, 2012): 16–23. http://dx.doi.org/10.21601/ejbms/9171.

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23

Zininga, Tawanda, Lebogang Ramatsui, and Addmore Shonhai. "Heat Shock Proteins as Immunomodulants." Molecules 23, no. 11 (November 1, 2018): 2846. http://dx.doi.org/10.3390/molecules23112846.

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Heat shock proteins (Hsps) are conserved molecules whose main role is to facilitate folding of other proteins. Most Hsps are generally stress-inducible as they play a particularly important cytoprotective role in cells exposed to stressful conditions. Initially, Hsps were generally thought to occur intracellulary. However, recent work has shown that some Hsps are secreted to the cell exterior particularly in response to stress. For this reason, they are generally regarded as danger signaling biomarkers. In this way, they prompt the immune system to react to prevailing adverse cellular conditions. For example, their enhanced secretion by cancer cells facilitate targeting of these cells by natural killer cells. Notably, Hsps are implicated in both pro-inflammatory and anti-inflammatory responses. Their effects on immune cells depends on a number of aspects such as concentration of the respective Hsp species. In addition, various Hsp species exert unique effects on immune cells. Because of their conservation, Hsps are implicated in auto-immune diseases. Here we discuss the various metabolic pathways in which various Hsps manifest immune modulation. In addition, we discuss possible experimental variations that may account for contradictory reports on the immunomodulatory function of some Hsps.

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24

Tutar, Lutfi, and Yusuf Tutar. "Heat Shock Proteins; An Overview." Current Pharmaceutical Biotechnology 11, no. 2 (February 1, 2010): 216–22. http://dx.doi.org/10.2174/138920110790909632.

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25

Talalaev, O. S. "Plant small heat shock proteins." Biopolymers and Cell 21, no. 5 (September 20, 2005): 392–99. http://dx.doi.org/10.7124/bc.000701.

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26

SHERMAN, M., and G. MULTHOFF. "Heat Shock Proteins in Cancer." Annals of the New York Academy of Sciences 1113, no. 1 (May 18, 2007): 192–201. http://dx.doi.org/10.1196/annals.1391.030.

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27

Peetermans, W. E. "Heat-Shock Proteins in Medicine." Acta Clinica Belgica 50, no. 3 (January 1995): 131–36. http://dx.doi.org/10.1080/17843286.1995.11718436.

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28

Moudgil, Kamal D., Stephen J. Thompson, Fabiana Geraci, Boel De Paepe, and Yehuda Shoenfeld. "Heat-Shock Proteins in Autoimmunity." Autoimmune Diseases 2013 (2013): 1–3. http://dx.doi.org/10.1155/2013/621417.

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29

Streips, U. N., and F. W. Polio. "Heat shock proteins in bacilli." Journal of Bacteriology 162, no. 1 (1985): 434–37. http://dx.doi.org/10.1128/jb.162.1.434-437.1985.

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30

Dana, Richard C., William J. Welch, and Leonard J. Deftos. "Heat shock proteins bind calcitonin." Endocrinology 126, no. 1 (January 1990): 672–74. http://dx.doi.org/10.1210/endo-126-1-672.

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31

Xu, Q. "Heat shock proteins and atherosclerosis." European Journal of Clinical Investigation 31, no. 4 (April 2001): 283–84. http://dx.doi.org/10.1046/j.1365-2362.2001.00820.x.

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32

Kalinina, Lidia V., Irina A. Khrebtukova, Olga L. Podgornaya, Anna Wasik, and Jerzy Sikora. "Heat shock proteins in Amoeba." European Journal of Protistology 24, no. 1 (December 1988): 64–68. http://dx.doi.org/10.1016/s0932-4739(88)80010-5.

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33

Wu, Jianming, Tuoen Liu, Zechary Rios, Qibing Mei, Xiukun Lin, and Shousong Cao. "Heat Shock Proteins and Cancer." Trends in Pharmacological Sciences 38, no. 3 (March 2017): 226–56. http://dx.doi.org/10.1016/j.tips.2016.11.009.

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34

Res, Pieter C. M., Jelle E. R. Thole, and René R. P. de Vries. "Heat shock proteins in immunopathology." Current Opinion in Immunology 3, no. 6 (December 1991): 924–29. http://dx.doi.org/10.1016/s0952-7915(05)80015-9.

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35

Yang, Isaac, Shanna Fang, and Andrew T. Parsa. "Heat Shock Proteins in Glioblastomas." Neurosurgery Clinics of North America 21, no. 1 (January 2010): 111–23. http://dx.doi.org/10.1016/j.nec.2009.09.002.

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36

Res, Pieter C. M., Jelle E. R. Thole, and RenéR P. de Vries. "Heat shock proteins in immunopathology." Current Biology 2, no. 2 (February 1992): 74. http://dx.doi.org/10.1016/0960-9822(92)90203-m.

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37

Ali, Najma, and Naheed Banu. "Heat shock proteins: Molecular chaperones." Biochemical Education 19, no. 4 (October 1991): 166–72. http://dx.doi.org/10.1016/0307-4412(91)90087-o.

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38

Zilaee, Marzie, and Saeed Shirali. "Heat Shock Proteins and Diabetes." Canadian Journal of Diabetes 40, no. 6 (December 2016): 594–602. http://dx.doi.org/10.1016/j.jcjd.2016.05.016.

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39

Bachelet, M., C. Adrie, and B. S. Polla. "Macrophages and heat shock proteins." Research in Immunology 149, no. 7-8 (September 1998): 727–32. http://dx.doi.org/10.1016/s0923-2494(99)80047-9.

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40

Polla, Barbara S., and Douglas Young. "Heat shock proteins and immunity." Immunology Today 10, no. 12 (December 1989): 393–94. http://dx.doi.org/10.1016/0167-5699(89)90029-7.

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41

Martine, Pierre, and Cédric Rébé. "Heat Shock Proteins and Inflammasomes." International Journal of Molecular Sciences 20, no. 18 (September 12, 2019): 4508. http://dx.doi.org/10.3390/ijms20184508.

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Heat shock proteins (HSP) regulate inflammation in many physiological contexts. However, inflammation is a broad process, involving numerous cytokines produced by different molecular pathways with multiple functions. In this review, we focused on the particular role of HSP on the inflammasomes intracellular platforms activated by danger signals and that enable activation of inflammatory caspases, mainly caspase-1, leading to the production of the pro-inflammatory cytokine IL-1β. Interestingly, some members of the HSP family favor inflammasomes activation whereas others inhibit it, suggesting that HSP modulators for therapeutic purposes, must be carefully chosen.

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42

Bernstein, R. M. "HEAT-SHOCK PROTEINS AND ARTHRITIS." Rheumatology 28, no. 5 (1989): 369–71. http://dx.doi.org/10.1093/rheumatology/28.5.369.

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43

Chen, Grace Y., and Gabriel Nuñez. "Are heat shock proteins DAMPs?" Nature Reviews Immunology 11, no. 8 (July 25, 2011): 565. http://dx.doi.org/10.1038/nri2873-c2.

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44

Catapano, A. L., W. Zhu, and P. Roma. "Heat shock proteins in atherosclerosis." Atherosclerosis 109, no. 1-2 (September 1994): 348–49. http://dx.doi.org/10.1016/0021-9150(94)94396-6.

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45

Hideaki, Itoh, and Tashima Yohtalou. "The stress (heat shock) proteins." International Journal of Biochemistry 23, no. 11 (January 1991): 1185–91. http://dx.doi.org/10.1016/0020-711x(91)90214-8.

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46

Dubois, P. "Heat shock proteins and immunity." Research in Immunology 140, no. 7 (January 1989): 653–59. http://dx.doi.org/10.1016/0923-2494(89)90019-9.

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47

Bolhassani, Azam, and Elnaz Agi. "Heat shock proteins in infection." Clinica Chimica Acta 498 (November 2019): 90–100. http://dx.doi.org/10.1016/j.cca.2019.08.015.

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48

Malyshev, I. Yu, and E. V. Malysheva. "Heat-shock proteins and cardioprotection." Bulletin of Experimental Biology and Medicine 126, no. 6 (December 1998): 1177–83. http://dx.doi.org/10.1007/bf02447143.

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49

Wang, Wen-Ming, and Hong-Zhong Jin. "Heat shock proteins and psoriasis." European Journal of Dermatology 29, no. 2 (March 2019): 121–25. http://dx.doi.org/10.1684/ejd.2019.3526.

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50

Moon, Yang Soo. "Heat Shock Proteins in Heat Stressed Chickens." Korean Journal of Poultry Science 47, no. 4 (December 2020): 219–77. http://dx.doi.org/10.5536/kjps.2020.47.4.219.

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