The DOI matches its Crossref record; 145 of the 148 references it cites were found in a registry or an index.
Releasing signals, secretory pathways, and immune function of endogenous extracellular heat shock protein 72
Abstract
Heat shock proteins (Hsp) were first characterized as intracellular proteins, which function to limit protein aggregation, facilitate protein refolding, and chaperone proteins. During times of cellular stress, intracellular Hsp levels increase to provide cellular protection. Recently, it has been recognized that Hsp, particularly Hsp72, are also found extracellularly (eHsp72), where they exhibit potent immunomodulatory effects on innate and acquired immunity. Circulating eHsp72 levels also greatly increase during times of stress (i.e., when an organism is exposed to a physical/psychological stressor or suffers from various pathological conditions). It has been proposed that elevated eHsp72 serves a protective role by facilitating immunological responses during times of increased risk of pathogenic challenge and/or tissue damage. This review focuses on the in vivo releasing signals and immunomodulatory function(s) of endogenous eHsp72. In addition, we present data that emphasize the importance of caution when conducting in vitro immunological tests of Hsp72 function.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“the release of Hsp72 (a possible DAMP) after tailshock is dependent on α-adrenergic, but not βor glucocorticoid, receptor signaling (Johnson et al, 2005;Johnson and Fleshner, 2006).”
From Danger Signals and Inflammasomes: Stress-Evoked Sterile Inflammation in Mood Disorders (2017) · cites this paper as Johnson and Fleshner, 2006
Citations
Cites
Goodman & Gilman's The Pharmacological Basis of Therapeutics
Brunton, L. L. (1985) · Cited by 7,321
Goodman and Gilman's the Pharmacological Basis of Therapeutics
Stigelman, W. H., & Pharm, D. (1986) · Military Medicine · doi:10.1093/milmed/151.1.386 · Cited by 6,796
Lindquist, S., & Craig, E. A. (1988) · Annual Review of Genetics · doi:10.1146/annurev.ge.22.120188.003215 · Cited by 5,304
Toll-like receptors: critical proteins linking innate and acquired immunity
Akira, S., Takeda, K., & Kaisho, T. (2001) · Nature Immunology · doi:10.1038/90609 · Cited by 4,777
Molecular chaperones in cellular protein folding
Hartl, F. U. (1996) · Nature · doi:10.1038/381571a0 · Cited by 3,584
Zitvogel, L., Régnault, A., Lozier, A., Wolfers, J., Flament, C., Tenza, D., Ricciardi‐Castagnoli, P., Raposo, G., & Amigorena, S. (1998) · Nature Medicine · doi:10.1038/nm0598-594 · Cited by 2,266
A new puffing pattern induced by temperature shock and DNP in drosophila
Ritossa, F. (1962) · Cellular and Molecular Life Sciences · doi:10.1007/bf02172188 · Cited by 2,146
Asea, A. A. A., Kraeft, S., Kurt‐Jones, E. A., Stevenson, M. A., Chen, L. B., Finberg, R. W., Koo, G. C., & Calderwood, S. K. (2000) · Nature Medicine · doi:10.1038/74697 · Cited by 1,642
Natural adjuvants: Endogenous activators of dendritic cells
Gallucci, S., Lolkema, M. P., & Matzinger, P. (1999) · Nature Medicine · doi:10.1038/15200 · Cited by 1,601
Novel Signal Transduction Pathway Utilized by Extracellular HSP70
Asea, A., Rehli, M., Kabingu, E., Boch, J. A., Baré, O., Auron, P. E., Stevenson, M. A., & Calderwood, S. K. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200497200 · Cited by 1,510
Flagged first, then by citations
3 of the 148 references couldn’t be matched to a known paper.
Research works printed but not linked: 1
- Gao, 2003, Endotoxin contamination in recombinant human heat shock protein 70 (Hsp70) preparation is responsible for the induction of tumor necrosis factor α release by murine macrophages, J. Biol. Chem., 278, 174, 10.1074/jbc.M208742200 · DOI · Paper page
Cited by
Sorted by citations
Depression as a Microglial Disease
Yirmiya, R., Rimmerman, N., & Reshef, R. (2015) · Trends in Neurosciences · doi:10.1016/j.tins.2015.08.001 · Cited by 944
Lee, J.-W., Choi, H., Hwang, U.-K., Kang, J., Kang, Y. J., Kim, K. I., & Kim, J. (2019) · Environmental Toxicology and Pharmacology · doi:10.1016/j.etap.2019.03.010 · Cited by 527
Parainflammation, Chronic Inflammation and Age-Related Macular Degeneration
Chen, M., & Xu, H. (2015) · Journal of Leukocyte Biology · doi:10.1189/jlb.3ri0615-239r · Cited by 381
Chen, T., Guo, J., Han, C., Yang, M., & Cao, X. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.182.3.1449 · Cited by 242
Non-targeted bystander effects induced by ionizing radiation
Morgan, W. F., & Sowa, M. B. (2006) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2006.11.009 · Cited by 219
Danger Signals and Inflammasomes: Stress-Evoked Sterile Inflammation in Mood Disorders
Fleshner, M., Frank, M., & Maier, S. F. (2017) · Neuropsychopharmacology · doi:10.1038/npp.2016.125 · Cited by 216
Self-citationMolecular mechanisms of natural killer cell activation in response to cellular stress
Chan, C. J., Smyth, M. J., & Martinet, L. (2013) · Cell Death and Differentiation · doi:10.1038/cdd.2013.26 · Cited by 222
Exosomes, DAMPs and miRNA: Features of Stress Physiology and Immune Homeostasis
Fleshner, M., & Crane, C. R. (2017) · Trends in Immunology · doi:10.1016/j.it.2017.08.002 · Cited by 212
Self-citationKrause, M. D. S., Heck, T. G., Bittencourt, A., Scomazzon, S. P., Newsholme, P., Curi, R., & de Bittencourt, P. I. H. (2015) · Mediators of Inflammation · doi:10.1155/2015/249205 · Cited by 178
Heat shock proteins and exercise: a primer
Noble, E. G., Milne, K. J., & Melling, C. W. J. (2008) · Applied Physiology Nutrition and Metabolism · doi:10.1139/h08-069 · Cited by 165
Maslanik, T., Mahaffey, L., Tannura, K., Beninson, L., Greenwood, B. N., & Fleshner, M. (2013) · Brain, Behavior, and Immunity · doi:10.1016/j.bbi.2012.10.014 · Cited by 156
Self-citationThe surface‐exposed chaperone, Hsp60, is an agonist of the microglial TREM2 receptor
Stefano, L., Racchetti, G., Bianco, F., Passini, N., Gupta, R. S., Panina‐Bordignon, P., & Meldolesi, J. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06130.x · Cited by 150
Therapeutic effect of exogenous hsp70 in mouse models of Alzheimer’s disease
Bobkova, N. V., Garbuz, D. G., Nesterova, I., Medvinskaya, N., Samokhin, A., Alexandrova, I., Yashin, V., Karpov, V., Kukharsky, M. S., Ninkina, N. N., et al. (2013) · Journal of Alzheimer's Disease · doi:10.3233/jad-130779 · Cited by 138
Neuroendocrine Regulation of Brain Cytokines After Psychological Stress
Johnson, J. D., Barnard, D. F., Kulp, A. C., & Mehta, D. M. (2019) · Journal of the Endocrine Society · doi:10.1210/js.2019-00053 · Cited by 135
Self-citationHorowitz, M., & Robinson, S. D. M. (2007) · Progress in brain research · doi:10.1016/s0079-6123(06)62021-9 · Cited by 128
Fleshner, M. (2013) · Brain, Behavior, and Immunity · doi:10.1016/j.bbi.2012.08.012 · Cited by 126
Self-citationExosomal Hsp70 Induces a Pro-Inflammatory Response to Foreign Particles Including Mycobacteria
Anand, P., Anand, E., Bleck, C., Anes, E., & Griffiths, G. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010136 · Cited by 131
Yin, Y., Zhang, P., Yue, X., Du, X., Li, W., Yin, Y., Yi, C., & Li, Y. (2018) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2018.06.056 · Cited by 120
Unfolding the Role of Large Heat Shock Proteins: New Insights and Therapeutic Implications
Zuo, D., Subjeck, J. R., & Wang, X. (2016) · Frontiers in Immunology · doi:10.3389/fimmu.2016.00075 · Cited by 122
Hoekstra, S. P., BISHOP, N. C., Faulkner, S. H., Bailey, S. J., & Leicht, C. A. (2018) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00407.2018 · Cited by 123
Stacchiotti, A., Morandini, F., Bettoni, F., Schena, I., Lavazza, A., Grigolato, P. G., Apostoli, P., Rezzani, R., & Aleo, M. F. (2009) · Toxicology · doi:10.1016/j.tox.2009.08.014 · Cited by 108
Divergence of intracellular and extracellular HSP72 in type 2 diabetes: does fat matter?
Rodrigues-Krause, J. D. C., Krause, M. D. S., O’Hagan, C., VITO, G. D., Boreham, C. A., Murphy, C., Newsholme, P., & Colleran, G. (2012) · Cell Stress and Chaperones · doi:10.1007/s12192-011-0319-x · Cited by 107
Chaiworapongsa, T., Erez, O., Kusanovic, J. P., Vaisbuch, E., Mazaki‐Tovi, S., Gotsch, F., Than, N. G., Mittal, P., Kim, Y. M., Camacho, N., et al. (2008) · The Journal of Maternal-Fetal & Neonatal Medicine · doi:10.1080/14767050802054550 · Cited by 108
The Pathogenesis of Glaucoma in the Interplay with the Immune System
Rieck, J. (2013) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.12-9781 · Cited by 104
Fong, J. J., Sreedhara, K., Deng, L., Varki, N. M., Angata, T., Liu, Q., Nizet, V., & Varki, A. P. (2015) · The EMBO Journal · doi:10.15252/embj.201591407 · Cited by 104
Deak, T., Quinn, M., Cidlowski, J. A., Victoria, N. C., Murphy, A. Z., & Sheridan, J. F. (2015) · Stress · doi:10.3109/10253890.2015.1053451 · Cited by 108
HSP70 expression: does it a novel fatigue signalling factor from immune system to the brain?
Heck, T. G., Schöler, C. M., & de Bittencourt, P. I. H. (2011) · Cell Biochemistry and Function · doi:10.1002/cbf.1739 · Cited by 101
Heat Shock Protein 70 in Alzheimer’s Disease
Lu, R.-C., Tan, M., Wang, H., Xie, A., Yu, J., & Tan, L. (2014) · BioMed Research International · doi:10.1155/2014/435203 · Cited by 103
Effect of heat acclimation on heat shock protein 72 and interleukin-10 in humans
Yamada, P. M., Amorim, F. T., Moseley, P. L., Robergs, R. A., & Schneider, S. M. (2007) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00242.2007 · Cited by 101
Stress response for disease control in aquaculture
Sung, Y. Y., MacRae, T. H., Sorgeloos, P., & Bossier, P. (2011) · Reviews in Aquaculture · doi:10.1111/j.1753-5131.2011.01049.x · Cited by 99
Ferat-Osorio, E. A., Sánchez-Anaya, A., Gutiérrez-Mendoza, M., Boscó-Gárate, I., Wong‐Baeza, I., Pastelin‐Palacios, R., Pedraza‐Alva, G., Bonifaz, L. C., Cortés‐Reynosa, P., Perez‐Salazar, E., et al. (2014) · Journal of Inflammation · doi:10.1186/1476-9255-11-19 · Cited by 100
Engler, H., Bailey, M. T., Engler, A., Stiner-Jones, L. M., Quan, N., & Sheridan, J. F. (2008) · Psychoneuroendocrinology · doi:10.1016/j.psyneuen.2007.10.007 · Cited by 97
Zhang, T., Lu, Q., Su, C., Yang, Y., Hu, D., & Xu, Q. (2017) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2017.04.058 · Cited by 94
Hulina, A., Grdić Rajković, M., Jakšić Despot, D., Jelić, D., Dojder, A., Čepelak, I., & Rumora, L. (2018) · Cell Stress and Chaperones · doi:10.1007/s12192-017-0847-0 · Cited by 92
Welc, S. S., & Clanton, T. L. (2012) · Experimental Physiology · doi:10.1113/expphysiol.2012.068189 · Cited by 95
Luo, X., Zuo, X., Zhou, Y., Zhang, B., Shi, Y., Liu, M., Wang, K., McMillian, D., & Xiao, X. (2008) · Arthritis Research & Therapy · doi:10.1186/ar2399 · Cited by 96
Sevin, M., Girodon, F., Garrido, C., & de Thonel, A. (2015) · Mediators of Inflammation · doi:10.1155/2015/970242 · Cited by 91
Hyperthermia increases interleukin-6 in mouse skeletal muscle
Welc, S. S., Phillips, N. A., Oca‐Cossio, J., Wallet, S. M., Chen, D. L., & Clanton, T. L. (2012) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00028.2012 · Cited by 88
Thermoregulation as a disease tolerance defense strategy
Schieber, A. M. P., & Ayres, J. S. (2016) · Pathogens and Disease · doi:10.1093/femspd/ftw106 · Cited by 89
Yao, Y., Watson, A. D., Ji, S., & Boström, K. I. (2009) · Circulation Research · doi:10.1161/circresaha.109.202333 · Cited by 87
Heat Shock Proteins and Disease Control in Aquatic Organisms
Sung, Y. Y., & MacRae, T. H. (2013) · Journal of Aquaculture Research & Development · doi:10.4172/2155-9546.s2-006 · Cited by 85
A central role for inducible heat‐shock protein 70 in autoimmune vitiligo
Mosenson, J. A., Eby, J. M., Hernandez, C., & Poole, I. C. L. (2013) · Experimental Dermatology · doi:10.1111/exd.12183 · Cited by 83
Sung, Y. Y., Pineda, C., MacRae, T. H., Sorgeloos, P., & Bossier, P. (2008) · Cell Stress and Chaperones · doi:10.1007/s12192-008-0011-y · Cited by 80
Heat-shock proteins: new keys to the development of cytoprotective therapies
Kim, H. P., Morse, D., & Choi, A. M. K. (2006) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.10.5.759 · Cited by 79
Maslanik, T., Tannura, K., Mahaffey, L., Loughridge, A. B., Benninson, L., Ursell, L., Greenwood, B. N., Knight, R., & Fleshner, M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0050636 · Cited by 77
Self-citationHeat shock protein 72 : release and biological significance during exercise
Whitham, M. (2007) · Frontiers in bioscience · doi:10.2741/2765 · Cited by 78
Extracellular heat shock protein 72 is a marker of the stress protein response in acute lung injury
Ganter, M. T., Ware, L. B., Howard, M., Roux, J., Gartland, B., Matthay, M. A., Fleshner, M., & Pittet, J. (2006) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00405.2005 · Cited by 78
Self-citationStress for maintaining memory: HSP70 as a mobile messenger for innate and adaptive immunity
Chen, T., & Cao, X. (2010) · European Journal of Immunology · doi:10.1002/eji.201040616 · Cited by 76
Magalhães, F. D. C., Amorim, F. T., Passos, R. L. F., da Fonseca, M. A., Oliveira, K. P. M., Lima, M. R. M., Guimarães, J. B., Ferreira‐Júnior, J. B., Martini, A. R. P., Lima, N. R. V., et al. (2010) · Cell Stress and Chaperones · doi:10.1007/s12192-010-0197-7 · Cited by 75
Pig Longissimus lumborum proteome: Part II: Relationships between protein content and meat quality
Kwasiborski, A., Sayd, T., Chambon, C., Santé-Lhoutellier, V., Rocha, D., & Terlouw, C. E. M. (2008) · Meat Science · doi:10.1016/j.meatsci.2008.04.032 · Cited by 75
Krause, M. D. S., Keane, K. N., Rodrigues-Krause, J. D. C., Crognale, D., Egan, B., VITO, G. D., Murphy, C., & Newsholme, P. (2013) · Clinical Science · doi:10.1042/cs20130678 · Cited by 75
Yang, Y., Yu, H., Li, H., Wang, A., & Yu, H. (2016) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2016.09.014 · Cited by 75
Baruah, K., Huy, T. T., Norouzitallab, P., Niu, Y., Gupta, S. K., Schryver, P. D., & Bossier, P. (2015) · Scientific Reports · doi:10.1038/srep09427 · Cited by 72
Old Friends, immunoregulation, and stress resilience
Langgartner, D., Lowry, C. A., & Reber, S. O. (2018) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-018-2228-7 · Cited by 76
Gibson, O. R., Alex, D., Parfitt, T., Taylor, L. K., Watt, P., & Maxwell, N. (2013) · Cell Stress and Chaperones · doi:10.1007/s12192-013-0468-1 · Cited by 70
Baruah, K., Norouzitallab, P., Linayati, L., Sorgeloos, P., & Bossier, P. (2014) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2014.06.004 · Cited by 67
Lemal, P., May, K., König, S., Schroyen, M., & Gengler, N. (2023) · Journal of Dairy Science · doi:10.3168/jds.2022-22727 · Cited by 75
Rozhkova, E., Yurinskaya, M. M., Zatsepina, O. G., Garbuz, D. G., Карпов, В. Л., Surkov, S. A., Murashev, A. N., Ostrov, V. F., Margulis, B. A., Евгеньев, М. Б., et al. (2010) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2009.05375.x · Cited by 66
Zhou, Y., Mao, H., Li, S., Cao, S., Li, Z., Zhuang, S., Fan, J., Dong, X., Borkan, S. C., Wang, Y., et al. (2010) · Journal of the American Society of Nephrology · doi:10.1681/asn.2009050552 · Cited by 67
Beninson, L. A., Brown, P. N., Loughridge, A. B., Saludes, J. P., Maslanik, T., Hills, A., Woodworth, T. T., Craig, W. C., Yin, H. H., & Fleshner, M. (2014) · PLoS ONE · doi:10.1371/journal.pone.0108748 · Cited by 65
Self-citationExtracellular Heat Shock Proteins: Alarmins for the Host Immune System
Wheeler, D. S. (2011) · The Open Inflammation Journal · doi:10.2174/1875041901104010049 · Cited by 65
Heck, T. G., Scomazzon, S. P., Nunes, P. R., Schöler, C. M., da Silva, G. S., Bittencourt, A., Faccioni‐Heuser, M. C., Krause, M. D. S., Bazotte, R. B., Curi, R., et al. (2017) · Cell Stress and Chaperones · doi:10.1007/s12192-017-0771-3 · Cited by 63
Calvani, R., Picca, A., Marini, F., Biancolillo, A., Gervasoni, J., Persichilli, S., Primiano, A., Coelho‐Júnior, H. J., Cesari, M., Bossola, M., et al. (2020) · GeroScience · doi:10.1007/s11357-020-00197-x · Cited by 66
Salah, A. S., Nahas, A. F. E., & Mahmoud, S. (2017) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2017.09.008 · Cited by 61
Kamanga‐Sollo, E., Pampusch, M. S., White, M. E., Hathaway, M. R., & Dayton, W. R. (2011) · Journal of Animal Science · doi:10.2527/jas.2011-4123 · Cited by 60
Hsp-72, a candidate prognostic indicator of heatstroke
Dehbi, M., Baturcam, E., Eldali, A., Ahmed, M., Kwaasi, A. A. A., Chishti, M. A., & Bouchama, A. (2010) · Cell Stress and Chaperones · doi:10.1007/s12192-010-0172-3 · Cited by 60
DNAJB3/HSP-40 Cochaperone Is Downregulated in Obese Humans and Is Restored by Physical Exercise
Abubaker, J. A., Tiss, A., Abu‐Farha, M., Al-Ghimlas, F., Al‐Khairi, I., Baturcam, E., Cherian, P., Elkum, N. B., Hammad, M. M., John, J., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0069217 · Cited by 59
Tang, D., Kang, R., Cao, L., Zhang, G., Yu, Y., Xiao, W., Wang, H., & Xiao, X. (2008) · Critical Care Medicine · doi:10.1097/01.ccm.0000295316.86942.ce · Cited by 58
Afiqah‐Aleng, N., Sung, Y. Y., MacRae, T. H., & Wahid, M. E. A. (2015) · PLoS ONE · doi:10.1371/journal.pone.0135603 · Cited by 57
Wu, F., Yuan, Y., Li, D., Liao, S., Yan, B., Wei, J., Zhou, Y., Zhu, J., Zhang, G., & Feng, Z. (2011) · Cancer Letters · doi:10.1016/j.canlet.2011.11.020 · Cited by 56
Activation of hepatocytes by extracellular heat shock protein 72
Galloway, E., Shin, T., Huber, N., Eismann, T., Kuboki, S., Schuster, R. M., Blanchard, J. A., Wong, H. R., & Lentsch, A. B. (2008) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00032.2008 · Cited by 56
Baruah, K., Ranjan, J., Sorgeloos, P., & Bossier, P. (2010) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2010.07.011 · Cited by 55
Extracellular Vesicles and the Stress System
Makrygianni, E. A., & Chrousos, G. P. (2022) · Neuroendocrinology · doi:10.1159/000527182 · Cited by 59
Винокуров, М. Г., Ostrov, V. F., Yurinskaya, M. M., Garbuz, D. G., Murashev, A. N., Antonova, O. Y., & Евгеньев, М. Б. (2011) · Cell Stress and Chaperones · doi:10.1007/s12192-011-0288-0 · Cited by 53
Zhang, A., Zhou, X., Wang, X., & Zhou, H. (2011) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2011.02.009 · Cited by 54
Fitrolaki, M.-D., Dimitriou, H., Venihaki, M., Katrinaki, M., Ilia, S., & Briassoulis, G. C. (2016) · Medicine · doi:10.1097/md.0000000000004651 · Cited by 52
Kustanova, G. A., Murashev, A. N., Карпов, В. Л., Margulis, B. A., Guzhova, I. V., Прохоренко, И. Р., Grachev, S. V., & Evgen’ev, M. B. (2006) · Cell Stress and Chaperones · doi:10.1379/csc-195r.1 · Cited by 52
Lee, C.-T., & Repasky, E. A. (2012) · Frontiers in Immunology · doi:10.3389/fimmu.2012.00140 · Cited by 51
Matrix metalloproteinase processing of signaling molecules to regulate inflammation
Butler, G. S., & Overall, C. M. (2013) · Periodontology 2000 · doi:10.1111/prd.12035 · Cited by 51
Boyko, A., Troyanova, N. I., Kovalenko, E. I., & Sapozhnikov, A. M. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18122633 · Cited by 54
Krause, M. D. S., Crognale, D., Cogan, K. E., Contarelli, S., Egan, B., Newsholme, P., & VITO, G. D. (2018) · Experimental Gerontology · doi:10.1016/j.exger.2018.12.004 · Cited by 59
Shanely, R. A., Nieman, D. C., Zwetsloot, K. A., Knab, A. M., Imagita, H., Luo, B., Davis, B. A., & Zubeldia, J. M. (2013) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2013.09.005 · Cited by 49
Tiss, A., Khadir, A., Abubaker, J. A., Abu‐Farha, M., Al‐Khairi, I., Cherian, P., John, J., Kavalakatt, S., Warsame, S., Al-Ghimlas, F., et al. (2014) · Lipids in Health and Disease · doi:10.1186/1476-511x-13-106 · Cited by 50
Exogenous heat shock protein 27 uniquely blocks differentiation of monocytes to dendritic cells
Laudański, K., De, A. K., & Miller‐Graziano, C. L. (2007) · European Journal of Immunology · doi:10.1002/eji.200636993 · Cited by 51
Wang, S., Xie, S., Zhang, C., Pan, Z., Sun, D., Zhou, A., Xu, G., & Zou, J. (2022) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2022.03.045 · Cited by 48
Sakharov, D. A., Maltseva, D. V., Riabenko, E., Shkurnikov, M. Y., Northoff, H., Tonevitsky, A., & Grigoriev, A. I. (2011) · European Journal of Applied Physiology · doi:10.1007/s00421-011-2048-3 · Cited by 47
Heat shock proteins (HSPs) in the homeostasis of regulatory T cells (Tregs)
Koliński, T., Marek-Trzonkowska, N. M., Trzonkowski, P., & Siebert, J. (2016) · Central European Journal of Immunology · doi:10.5114/ceji.2016.63133 · Cited by 46
Wang, S., Xie, S., Wang, Z., Zhang, C., Pan, Z., Sun, D., Xu, G., & Zou, J. (2021) · Biological Trace Element Research · doi:10.1007/s12011-021-02917-6 · Cited by 45
Krause, M. D. S., & Rodrigues-Krause, J. D. C. (2010) · Medical Hypotheses · doi:10.1016/j.mehy.2010.10.025 · Cited by 45
Khadir, A., Kavalakatt, S., Cherian, P., Warsame, S., Abubaker, J. A., Dehbi, M., & Tiss, A. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00016 · Cited by 57
Giraldo, E., Martín-Cordero, L., García, J. J., Gerhmann, M., Multhoff, G., & Ortega, E. (2009) · European Journal of Applied Physiology · doi:10.1007/s00421-009-1201-8 · Cited by 43
Detection of Highly Curved Membrane Surfaces Using a Cyclic Peptide Derived from Synaptotagmin-I
Saludes, J. P., Morton, L. A., Ghosh, N., Beninson, L. A., Chapman, E. R., Fleshner, M., & Yin, H. H. (2012) · ACS Chemical Biology · doi:10.1021/cb3002705 · Cited by 41
Self-citationChen, X., Lu, H.-M., Niu, X., Wang, G., & Zhang, D. (2015) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2015.02.019 · Cited by 41
Patterns of gene expression associated with recovery and injury in heat-stressed rats
Stallings, J. D., Ippolito, D. L., Rakesh, V., Baer, C. E., Dennis, W. E., Helwig, B. G., Jackson, D. A., Leon, L. R., Lewis, J. A., & Jaques Reifman, A. (2014) · BMC Genomics · doi:10.1186/1471-2164-15-1058 · Cited by 42
Leite, J. S. M., Cruzat, V. F., Krause, M. D. S., & de Bittencourt, P. I. H. (2016) · Nutrire · doi:10.1186/s41110-016-0021-y · Cited by 41
Fan, Y., Cheng, Q., Liu, B., Wang, C., Liu, H., Pan, X.-X., Teng, P., Hu, L., Zhang, G., Han, Y., et al. (2017) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2017.10.006 · Cited by 40
Saludes, J. P., Morton, L. A., Coulup, S. K., Fiorini, Z., Cook, B. M., Beninson, L. A., Chapman, E. R., Fleshner, M., & Yin, H. H. (2013) · Molecular BioSystems · doi:10.1039/c3mb70109c · Cited by 39
Self-citationMiragem, A. A., & de Bittencourt, P. I. H. (2017) · Human Reproduction Update · doi:10.1093/humupd/dmx020 · Cited by 39
Tsuji, T., Kato, A., Yasuda, H., Miyaji, T., Luo, J., Sakao, Y., Ito, H., Fujigaki, Y., & Hishida, A. (2008) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2008.09.031 · Cited by 39
Effect of caffeine supplementation on the extracellular heat shock protein 72 response to exercise
Whitham, M., Walker, G. J., & BISHOP, N. C. (2006) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00409.2006 · Cited by 39
Metadata
- Authors
- Johnson, J. D., & Fleshner, M.
- Affiliations
- University of Colorado Boulder (US)
- Corresponding author
- Fleshner, Monika
- ORCID
- Fleshner, Monika
- Venue
- Journal of Leukocyte Biology
- Publisher
- Oxford University Press (OUP)
- Published
- 2005-12-30
- Volume
- 79
- Issue
- 3
- Pages
- 425-434
- ISSN
- 0741-5400 (ISSN-L)
- 1938-3673
- OpenAlex
- W2165218249
- Cited by
- 251
- References
- 148
- Citations by year
- 2026: 5 · 2025: 2 · 2024: 2 · 2023: 8 · 2022: 7 · 2021: 6 · 2020: 8 · 2019: 8 · 2018: 12 · 2017: 13 · 2016: 12 · 2015: 21 · 2014: 18 · 2013: 18 · 2012: 20
- FWCI
- 1.02
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Leukocyte Biology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › S100 Proteins and Annexins
- Keywords
- HSP72, secretory pathway, immunomodulation, innate immunity, adaptive immunity, stress response, molecular chaperones
- MeSH terms
- Animals, Cell Membrane, Humans, Immunity, Cellular, Immunity, Innate, Immunologic Factors, Receptors, Adrenergic, alpha, Stress, Physiological, Signal Transduction, Up-Regulation, Extracellular Fluid, HSP72 Heat-Shock Proteins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review