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Journal articles on the topic 'HspSO'

Author: Grafiati

Published: 10 March 2023

Last updated: 19 July 2025

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1

Bala, Nurudeen Muhammad, and Suhailan Bin Safei. "A Hybrid Harmony Search and Particle Swarm Optimization Algorithm (HSPSO) for Testing Non-functional Properties in Software System." Statistics, Optimization & Information Computing 10, no. 3 (2021): 968–82. http://dx.doi.org/10.19139/soic-2310-5070-1039.

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An important aspect of improving software system is testing. However, it is time demanding and sometimeslabour intensive if done manually. In this paper, we developed an automatic search-based approach for testing the nonfunctional properties of a software system using hybrid harmony search and particle swarm optimization algorithms. The approach birthed a new algorithm named HSPSO, which is proposed based on the strength of HS over Genetic algorithm (GA) in terms of less adjustable parameters, quick convergence and smooth implementation. On the other hand, we propose the PSO to complement the

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Xu, Ji, Hong Zhou, Yanjun Fang, and Lan Liu. "Data-Driven Approach for the Short-Term Business Climate Forecasting Based on Power Consumption." Wireless Communications and Mobile Computing 2022 (April 27, 2022): 1–11. http://dx.doi.org/10.1155/2022/4037053.

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With the fast development of intelligent data-mining technologies, some advanced artificial intelligence approaches are widely developed and employed to help the decision-making of enterprises and government. The application of advanced and intelligent approaches successfully helps the enterprises and government find out the valuable information hidden in the massive economic data. This study presents a novel data-driven approach to forecast the short-term business climate using the electric power consumption data of large enterprises. In addition, the climate conditions, interactions between

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Banu, P. K. Nizar, and S. Andrews. "Harmony Search PSO Clustering for Tumor and Cancer Gene Expression Dataset." International Journal of Swarm Intelligence Research 5, no. 3 (2014): 1–21. http://dx.doi.org/10.4018/ijsir.2014070101.

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Enormous quantity of gene expression data from diverse data sources are accumulated due to the modern advancement in microarray technology that leads to major computational challenges. The foremost step towards addressing this challenge is to cluster genes which reveal hidden gene expression patterns and natural structures to find the interesting patterns from the underlying data that in turn helps in disease diagnosis and drug development. Particle Swarm Optimization (PSO) technique is extensively used for many practical applications but fails in finding the initial seeds to generate clusters

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Huirimilla Casanova, Leyla, Jonathan Henrriquez Luhr, Matías Castillo-Aguilar, et al. "La Alta Sensibilidad del Procesamiento Sensorial y su relación con el equilibrio postural en personas mayores. (The High Sensitivity of Sensory Processing and its relationship with postural balance in older people.)." Retos 58 (July 1, 2024): 308–14. http://dx.doi.org/10.47197/retos.v58.106788.

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El rasgo de alta sensibilidad al procesamiento sensorial (HSPST) es una característica neurológica específica que afecta al 20% de la población mundial. Se caracteriza porque la Persona Altamente Sensible (PAS) tiene altos niveles de capacidad empática, relatividad emocional y sensibilidad ante estímulos sutiles imperceptibles para los demás. Objetivo: Relacionar el rasgo del HSPST y el equilibrio postural en personas mayores. Métodos: El estudio fue de tipo correlacional. Se realizó en una única etapa mediante cuestionario presencial y evaluación del equilibrio postural. Los participantes en

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Kaneda, F., and P. G. Kwiat. "High-efficiency single-photon generation via large-scale active time multiplexing." Science Advances 5, no. 10 (2019): eaaw8586. http://dx.doi.org/10.1126/sciadv.aaw8586.

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Deterministic generation of single- and multiphoton states is a key requirement for large-scale optical quantum information and communication applications. While heralded single-photon sources (HSPSs) using nonlinear optical processes have enabled proof-of-principle demonstrations in this area of research, they are not scalable as their probabilistic nature severely limits their generation efficiency. We overcome this limitation by demonstrating a substantial improvement in HSPS efficiency via large-scale time multiplexing. Using an ultra-low loss, adjustable optical delay to multiplex 40 conv

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Tower, John. "Hsps and aging." Trends in Endocrinology & Metabolism 20, no. 5 (2009): 216–22. http://dx.doi.org/10.1016/j.tem.2008.12.005.

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Chen, Wei, Pengmian Feng, Tao Liu, and Dianchuan Jin. "Recent Advances in Machine Learning Methods for Predicting Heat Shock Proteins." Current Drug Metabolism 20, no. 3 (2019): 224–28. http://dx.doi.org/10.2174/1389200219666181031105916.

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Background:As molecular chaperones, Heat Shock Proteins (HSPs) not only play key roles in protein folding and maintaining protein stabilities, but are also linked with multiple kinds of diseases. Therefore, HSPs have been regarded as the focus of drug design. Since HSPs from different families play distinct functions, accurately classifying the families of HSPs is the key step to clearly understand their biological functions. In contrast to laborintensive and cost-ineffective experimental methods, computational classification of HSP families has emerged to be an alternative approach.Methods:We

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8

Baszczynski, Chris L. "Immunochemical analysis of heat-shock protein synthesis in maize (Zea mays L.)." Canadian Journal of Genetics and Cytology 28, no. 6 (1986): 1076–87. http://dx.doi.org/10.1139/g86-151.

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Polyclonal antibodies to 18-kilodalton (kDa) heat-shock proteins (HSPs) and to the high molecular weight (73 000 – 89 000) HSPs from 5- day-old maize plumules have been produced in rabbits. The antisera to high molecular weight HSPs show minor cross-reactivity to proteins of similar molecular mass in not heat-shocked tissues, while antisera to 18-kDa HSPs react only with this 18-kDa HSP class. HSPs of similar molecular mass and isoelectric points in maize plumules, mesocotyls, radicles, and young leaves also have similar antigenic determinants based on positive reactions with antisera to plumu

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Song, Xueming, Zhiqiang Chen, Chunbo Wu, and Shiguang Zhao. "Abrogating HSP Response Augments Cell Death Induced by As2O3 in Glioma Cell Lines." Canadian Journal of Neurological Sciences / Journal Canadien des Sciences Neurologiques 37, no. 4 (2010): 504–11. http://dx.doi.org/10.1017/s0317167100010544.

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Objectives:We previously reported that Arsenic trioxide (ATO) can inhibit glioma growth both in vitro and in vivo. While the use of ATO alone for solid tumor treatment sometimes was found to be ineffective which may be due to the protective pathways including heat shock proteins (HSPs) response induced by ATO. In this study, we modified HSPs expression to investigate whether HSPs had some effect on ATO induced glioma cell death.Methods:Trypan bule exclusion assay, mitochondrial membrane potential (MMP) Assay, and SubG1 detection were used to evaluate cell viability and western-blot was employe

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Liu, Sirui, Yinkun Liu, Endong Bao, and Shu Tang. "The Protective Role of Heat Shock Proteins against Stresses in Animal Breeding." International Journal of Molecular Sciences 25, no. 15 (2024): 8208. http://dx.doi.org/10.3390/ijms25158208.

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Heat shock proteins (HSPs) play an important role in all living organisms under stress conditions by acting as molecular chaperones. The expression of different HSPs during stress varies depending on their protective functions and anti-apoptotic activities. The application of HSPs improves the efficiency and decreases the economic cost of animal breeding. By upregulating the expression of HSPs, feed supplements can improve stress tolerance in farm animals. In addition, high expression of HSPs is often a feature of tumor cells, and inhibiting the expression of HSPs is a promising novel method f

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11

Vierling, Elizabeth. "MOLECULAR ANALYSIS OF HEAT STRESS PROTEINS IN HIGHER PLANTS." HortScience 25, no. 9 (1990): 1175e—1175. http://dx.doi.org/10.21273/hortsci.25.9.1175e.

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When plants experience high temperature stress, they respond by synthesizing a discrete set of proteins called heat shock proteins (HSPs). This response is not unique to plants, but is observed in all other eukaryotes. It is now known that the HSPs are evolutionarily conserved proteins, and furthermore, that HSPs function not only during stress, but also during normal growth and development. My laboratory has characterized several of the major groups of HSPs in higher plants. We have cloned genes encoding plant HSP70 proteins and low molecular weight (LMW) HSPs (17-23 kDa). Using this informat

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Rodríguez-Iturbe, B., and RJ Johnson. "Heat shock proteins and cardiovascular disease." Physiology International 105, no. 1 (2018): 19–37. http://dx.doi.org/10.1556/2060.105.2018.1.4.

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The development of stress drives a host of biological responses that include the overproduction of a family of proteins named heat shock proteins (HSPs), because they were initially studied after heat exposure. HSPs are evolutionarily preserved proteins with a high degree of interspecies homology. HSPs are intracellular proteins that also have extracellular expression. The primary role of HSPs is to protect cell function by preventing irreversible protein damage and facilitating molecular traffic through intracellular pathways. However, in addition to their chaperone role, HSPs are immunodomin

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Zhang, Miao, and Xiaowen Bi. "Heat Shock Proteins and Breast Cancer." International Journal of Molecular Sciences 25, no. 2 (2024): 876. http://dx.doi.org/10.3390/ijms25020876.

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Heat shock proteins (Hsps) are a group of stress-induced proteins involved in protein folding and maturation. Based on their molecular weight, Hsps can be divided into six families: small Hsps, Hsp40, Hsp60, Hsp70, Hsp90, and large Hsps. In the process of breast cancer tumorigenesis, Hsps play a central role in regulating cell reactions and functions including proliferation, metastasis, and apoptosis. Moreover, some of the critical Hsps also regulate the fine balance between the protective and destructive immunological responses within the tumor microenvironment. In this review, we systematica

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Xu, Qingbo, Bernhard Metzler, Marjan Jahangiri, and Kaushik Mandal. "Molecular chaperones and heat shock proteins in atherosclerosis." American Journal of Physiology-Heart and Circulatory Physiology 302, no. 3 (2012): H506—H514. http://dx.doi.org/10.1152/ajpheart.00646.2011.

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In response to stress stimuli, mammalian cells activate an ancient signaling pathway leading to the transient expression of heat shock proteins (HSPs). HSPs are a family of proteins serving as molecular chaperones that prevent the formation of nonspecific protein aggregates and assist proteins in the acquisition of their native structures. Physiologically, HSPs play a protective role in the homeostasis of the vessel wall but have an impact on immunoinflammatory processes in pathological conditions involved in the development of atherosclerosis. For instance, some members of HSPs have been show

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Das, Jugal Kishore, Xiaofang Xiong, Xingcong Ren, Jin-Ming Yang, and Jianxun Song. "Heat Shock Proteins in Cancer Immunotherapy." Journal of Oncology 2019 (December 11, 2019): 1–9. http://dx.doi.org/10.1155/2019/3267207.

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Heat shock proteins (HSPs) are highly conserved molecular chaperones with divergent roles in various cellular processes. The HSPs are classified according to their molecular size as HSP27, HSP40, HSP60, HSP70, and HSP90. The HSPs prevent nonspecific cellular aggregation of proteins by maintaining their native folding energetics. The disruption of this vital cellular process, driven by the aberrant expression of HSPs, is implicated in the progression of several different carcinomas. Many HSPs are also actively involved in promoting the proliferation and differentiation of tumor cells, contribut

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Sadura, Iwona, and Anna Janeczko. "Are Heat Shock Proteins Important in Low-Temperature-Stressed Plants? A Minireview." Agronomy 14, no. 6 (2024): 1296. http://dx.doi.org/10.3390/agronomy14061296.

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Heat shock proteins (HSPs) are mainly known to play important roles in plants against high-temperature (HT) stress. Their main function is to act as molecular chaperones for other proteins. It has also been proven that HSPs have a protective effect during other environmental stresses including low temperature (LT). To the best of our knowledge, the expression and role of HSPs in plants that have been exposed to LT have not yet been sufficiently reviewed. The aims of this minireview were (1) to briefly describe the origin, classification, structure, localisation and functions of HSPs, (2) to pr

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Wu, Shuang, Yongtian Zhao, Delu Wang, and Zhuo Chen. "Mode of Action of Heat Shock Protein (HSP) Inhibitors against Viruses through Host HSP and Virus Interactions." Genes 14, no. 4 (2023): 792. http://dx.doi.org/10.3390/genes14040792.

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Misfolded proteins after stress-induced denaturation can regain their functions through correct re-folding with the aid of molecular chaperones. As a molecular chaperone, heat shock proteins (HSPs) can help client proteins fold correctly. During viral infection, HSPs are involved with replication, movement, assembly, disassembly, subcellular localization, and transport of the virus via the formation of macromolecular protein complexes, such as the viral replicase complex. Recent studies have indicated that HSP inhibitors can inhibit viral replication by interfering with the interaction of the

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Paul, Catherine, Florence Manero, Sandrine Gonin, et al. "Small Hsps as regulators of apoptosis." Biology of the Cell 91, no. 7 (1999): 545. http://dx.doi.org/10.1016/s0248-4900(99)90250-2.

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Fang, Bingliang, and Wei Guo. "Enhancing antitumor immune response by HSPs." Cancer Biology & Therapy 7, no. 2 (2008): 196–97. http://dx.doi.org/10.4161/cbt.7.2.5578.

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Kilic, Arman, and Kaushik Mandal. "Heat Shock Proteins: Pathogenic Role in Atherosclerosis and Potential Therapeutic Implications." Autoimmune Diseases 2012 (2012): 1–9. http://dx.doi.org/10.1155/2012/502813.

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Heat shock proteins (HSPs) are a highly conserved group of proteins that are constitutively expressed and function as molecular chaperones, aiding in protein folding and preventing the accumulation of misfolded proteins. In the arterial wall, HSPs have a protective role under normal physiologic conditions. In disease states, however, HSPs expressed on the vascular endothelial cell surface can act as targets for detrimental autoimmunity due to their highly conserved sequences. Developing therapeutic strategies for atherosclerosis based on HSPs is challenged by the need to balance such physiolog

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Yun, Chul Won, Hyung Joo Kim, Ji Ho Lim, and Sang Hun Lee. "Heat Shock Proteins: Agents of Cancer Development and Therapeutic Targets in Anti-Cancer Therapy." Cells 9, no. 1 (2019): 60. http://dx.doi.org/10.3390/cells9010060.

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Heat shock proteins (HSPs) constitute a large family of molecular chaperones classified by their molecular weights, and they include HSP27, HSP40, HSP60, HSP70, and HSP90. HSPs function in diverse physiological and protective processes to assist in maintaining cellular homeostasis. In particular, HSPs participate in protein folding and maturation processes under diverse stressors such as heat shock, hypoxia, and degradation. Notably, HSPs also play essential roles across cancers as they are implicated in a variety of cancer-related activities such as cell proliferation, metastasis, and anti-ca

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Zininga, Tawanda, Lebogang Ramatsui, and Addmore Shonhai. "Heat Shock Proteins as Immunomodulants." Molecules 23, no. 11 (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 conditio

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Abi Zamer, Batoul, Waseem El-Huneidi, Mohamed Ahmed Eladl, and Jibran Sualeh Muhammad. "Ins and Outs of Heat Shock Proteins in Colorectal Carcinoma: Its Role in Carcinogenesis and Therapeutic Perspectives." Cells 10, no. 11 (2021): 2862. http://dx.doi.org/10.3390/cells10112862.

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Cancer cells can reprogram their metabolic activities and undergo uncontrolled proliferation by utilizing the power of heat shock proteins (HSPs). HSPs are highly conserved chaperones that facilitate the folding of intracellular proteins under stress. Constitutively, HSPs are expressed at low levels, but their expression upregulates in response to a wide variety of insults, including anticancer drugs, allowing cancer cells to develop chemoresistance. In recent years, several researchers have reported that HSPs could be an important therapeutic target in difficult-to-treat cancers such as color

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Liu, Daiqi, Xuyao Han, Zhiwei Zhang, Gary Tse, Qingmiao Shao, and Tong Liu. "Role of Heat Shock Proteins in Atrial Fibrillation: From Molecular Mechanisms to Diagnostic and Therapeutic Opportunities." Cells 12, no. 1 (2022): 151. http://dx.doi.org/10.3390/cells12010151.

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Heat shock proteins (HSPs) are endogenous protective proteins and biomarkers of cell stress response, of which examples are HSP70, HSP60, HSP90, and small HSPs (HSPB). HSPs protect cells and organs, especially the cardiovascular system, against harmful and cytotoxic conditions. More recent attention has focused on the roles of HSPs in the irreversible remodeling of atrial fibrillation (AF), which is the most common arrhythmia in clinical practice and a significant contributor to mortality. In this review, we investigated the relationship between HSPs and atrial remodeling mechanisms in AF. Pub

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Chiba, Tsuyoshi, Nanae Tanemura, and Chiharu Nishijima. "Determination of the Awareness about and Need for Health Support Pharmacies as the Provider of Consultation Service about Nutrition Education and Diet-Related Health Promotion by Health Professionals in Japan." Nutrients 14, no. 1 (2021): 165. http://dx.doi.org/10.3390/nu14010165.

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Health support pharmacies (HSPs) have been established as a new category of pharmacies in Japan. In addition to prescriptions, HSPs provide several health services, including consultations on diet/nutrition, health foods, and nursing care. Therefore, not only individuals receiving medications but also community residents should have access to HSPs. However, it is unclear whether people are aware of HSPs. Thus, the purpose of this study was to assess the awareness about HSPs and determine the need for their services. To this end, we conducted an online cross-sectional questionnaire survey in 10

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Goulhen, Florence, Daniel Grenier, and Denis Mayrand. "Oral Microbial Heat-shock Proteins and Their Potential Contributions to Infections." Critical Reviews in Oral Biology & Medicine 14, no. 6 (2003): 399–412. http://dx.doi.org/10.1177/154411130301400603.

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The oral cavity is a complex ecosystem in which several hundred microbial species normally cohabit harmoniously. However, under certain special conditions, the growth of some micro-organisms with a pathogenic potential is promoted, leading to infections such as dental caries, periodontal disease, and stomatitis. The physiology and pathogenic properties of micro-organisms are influenced by modifications in environmental conditions that lead to the synthesis of specific proteins known as the heat-shock proteins (HSPs). HSPs are families of highly conserved proteins whose main role is to allow mi

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Edmison, Daisy, Luyu Wang, and Swetha Gowrishankar. "Lysosome Function and Dysfunction in Hereditary Spastic Paraplegias." Brain Sciences 11, no. 2 (2021): 152. http://dx.doi.org/10.3390/brainsci11020152.

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Hereditary Spastic Paraplegias (HSPs) are a genetically diverse group of inherited neurological diseases with over 80 associated gene loci. Over the last decade, research into mechanisms underlying HSPs has led to an emerging interest in lysosome dysfunction. In this review, we highlight the different classes of HSPs that have been linked to lysosome defects: (1) a subset of complex HSPs where mutations in lysosomal genes are causally linked to the diseases, (2) other complex HSPs where mutation in genes encoding membrane trafficking adaptors lead to lysosomal defects, and (3) a subset of HSPs

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Voegeli, Tracy S., Amanda J. Wintink, Yu Chen та R. William Currie. "Heat shock proteins 27 and 70 regulating angiotensin II-induced NF-κB: a possible connection to blood pressure control?" Applied Physiology, Nutrition, and Metabolism 33, № 5 (2008): 1042–49. http://dx.doi.org/10.1139/h08-068.

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Heat shock proteins (HSPs) are critical for cell survival and have several mechanisms of action. HSPs regulate protein folding, suppress apoptosis, and regulate anti-oxidative activity. In addition, HSPs are involved in the regulation of the pro-inflammatory transcription factor nuclear factor (NF)-κB. When angiotensin (Ang) II is infused into rats, there is a significant increase in systolic blood pressure, and NF-κB is activated in the heart. If rats are heat shocked to induce the heat shock response and HSPs before Ang II infusion, there is a significant suppression of both the Ang II-induc

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Zhou, Qin, Xin-Yuan Guan, and Yan Li. "Roles of heat shock proteins in tumor immune microenvironment." Visualized Cancer Medicine 5 (2024): 3. http://dx.doi.org/10.1051/vcm/2024002.

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Heat shock proteins (HSPs) are the most abundant molecular chaperones in cells, categorized based on function and molecular weight into HSP families, namely, HSP40, HSP70, HSP90, HSP110, and HSPB (heat shock protein B), et al. HSPs are involved in protein homeostasis by assisting in the correct folding of proteins or incorrectly folded proteins, refolding partially denatured proteins, and degrading damaged proteins. High levels of HSPs have been shown to participate in oncogenesis, progression, and chemotherapy resistance in many cancers. Recently a new range of functions besides chaperons, mo

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Arnold-Schild, Danièle, Daniel Hanau, Danièle Spehner, et al. "Cutting Edge: Receptor-Mediated Endocytosis of Heat Shock Proteins by Professional Antigen-Presenting Cells." Journal of Immunology 162, no. 7 (1999): 3757–60. http://dx.doi.org/10.4049/jimmunol.162.7.3757.

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Abstract Immunization with heat shock proteins (HSPs) induces Ag-specific CTL responses. The specificity of the immune response is based on peptides associated with HSPs. To investigate how exogenous HSP/peptide complexes gain access to the MHC class I-restricted Ag presentation pathway, we incubated the monocytic cell line P388D1 and the dendritic cell line D2SC/1 with gold-labeled HSPs gp96 and HSC70. We show that HSPs bind specifically to the surface of these APCs and are internalized spontaneously by receptor-mediated endocytosis, demonstrating the existence of specific receptors for HSPs

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Yakovenko, L. F., O. V. Romashchenko, and I. V. Kroupskaya. "Heat shock proteins in the diagnosis and prognosis of reproductive disorders in women." HEALTH OF WOMAN, no. 7(133) (September 30, 2018): 77–83. http://dx.doi.org/10.15574/hw.2018.133.77.

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Heat shock proteins are structurally highly conserved and abundantly expressed by prokaryotic and eukaryotic cells under stressful conditions. HSPs are immunodominant antigens for many microbes. They are overexpressed at sites of acute and chronic inflammation and involved in the patogenesis of various diseases. Clinical studies and results of own investigations provided evidence that HSPs and anti-HSPs antibodies can be biomarkers for the diagnosis and prognosis of reproductive disorders in women. The involvement of HSPs and anti-HSPs antibodies in pathogenesis of tubal infertility, ovarian f

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Sghaier, Haïtham, Thuy Le Huyen Ai, Tokumasa Horiike, and Takao Shinozawa. "Molecular Chaperones: Proposal of a Systematic Computer-Oriented Nomenclature and Construction of a Centralized Database." In Silico Biology: Journal of Biological Systems Modeling and Multi-Scale Simulation 4, no. 3 (2004): 311–22. https://doi.org/10.3233/isb-00135.

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Molecular chaperones are a wide group of unrelated protein families whose role is to assist others proteins. Comparably, under environmental stress, stress proteins behave as biocatalysts of protein stabilization. Stress proteins include a large class of proteins that were originally termed heat shock proteins (HSPs) due to their initial discovery in tissues exposed to elevated temperatures. Many, but not all, stress proteins and HSPs are molecular chaperones. Moreover, not all HSPs are derivable from stress. HSPs are structurally diversified by the contribution of various domains having speci

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Sediqi, Khwaja Zubair, Lars Prehn, and Oliver Gasser. "Hyper-specific prefixes." ACM SIGCOMM Computer Communication Review 52, no. 2 (2022): 20–34. http://dx.doi.org/10.1145/3544912.3544916.

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Autonomous Systems (ASes) exchange reachability information between each other using BGP---the de-facto standard inter-AS routing protocol. While IPv4 (IPv6) routes more specific than /24 (/48) are commonly filtered (and hence not propagated), route collectors still observe many of them. In this work, we take a closer look at those "hyper-specific" prefixes (HSPs). In particular, we analyze their prevalence, use cases, and whether operators use them intentionally or accidentally. While their total number increases over time, most HSPs can only be seen by route collector peers. Nonetheless, som

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Brenu, E. W., D. R. Staines, L. Tajouri, T. Huth, K. J. Ashton, and S. M. Marshall-Gradisnik. "Heat Shock Proteins and Regulatory T Cells." Autoimmune Diseases 2013 (2013): 1–8. http://dx.doi.org/10.1155/2013/813256.

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Heat shock proteins (HSPs) are important molecules required for ideal protein function. Extensive research on the functional properties of HSPs indicates that HSPs may be implicated in a wide range of physiological functions including immune function. In the immune system, HSPs are involved in cell proliferation, differentiation, cytokine release, and apoptosis. Therefore, the ability of the immune system, in particular immune cells, to function optimally and in unison with other physiological systems is in part dependent on signaling transduction processes, including bidirectional communicati

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Larson, Brent K., Julie M. Hess, and Jeffrey M. Williams. "PROCEDURE FOR ESTIMATING OIL THREE-DIMENSIONAL SOLUBILITY PARAMETERS." Rubber Chemistry and Technology 90, no. 4 (2017): 621–32. http://dx.doi.org/10.5254/rct.82.83733.

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ABSTRACT Process oils make important contributions to nearly every compound in a tire, and oil–polymer interactions have effects on compound processing and performance. One way to predict oil–polymer interactions is to determine the three-dimensional (3-D) Hansen solubility parameters (HSPs) for both oil and polymer, and the polymer solubility sphere (PSS) radius. Favorable oil–polymer interactions occur when an oil's HSPs are located within a PSS. Interactions are stronger when an oil's HSPs are located closer to the center of the PSS. If an oil's HSPs are located outside a polymer's solubili

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Noble, Earl G., Kevin J. Milne, and C. W. James Melling. "Heat shock proteins and exercise: a primer." Applied Physiology, Nutrition, and Metabolism 33, no. 5 (2008): 1050–75. http://dx.doi.org/10.1139/h08-069.

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Heat shock proteins (HSPs) are, in general, prosurvival molecules within the cellular environment, and the overexpression of even just 1 family of HSPs can lead to protection against and improvements after a variety of stressors. Not surprisingly, a fertile area of study has grown out of effors to exploit the innate biologic behaviour of HSPs. Exercise, because of the inherent physiologic stresses associated with it, is but 1 stimulus that can result in a robust increase in various HSPs in several tissues, not the least of which happen to be the heart and skeletal muscle. The purpose of this r

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Nandan, Monica, Archana Singh, and Gokul Mandayam. "Social Value Creation and Social Innovation by Human Service Professionals: Evidence from Missouri, USA." Administrative Sciences 9, no. 4 (2019): 86. http://dx.doi.org/10.3390/admsci9040086.

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Owing to the contextual challenges, human service professionals (HSP) are creating social value (SV) for diverse vulnerable population groups through social innovation. This qualitative exploratory study investigates the nature of SV created by 14 HSPs, representing a diverse range of human service organizations (HSOs), and examines ‘why’ and ‘how’ they innovate. In addition, the study examines HSPs’ current understanding and practices related to social entrepreneurship (SE). The study findings highlight that increased accountability and new funding opportunities challenged HSPs to innovate. H

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Somu, Prathap, Sonali Mohanty, Nagaraj Basavegowda, Akhilesh Kumar Yadav, Subhankar Paul, and Kwang-Hyun Baek. "The Interplay between Heat Shock Proteins and Cancer Pathogenesis: A Novel Strategy for Cancer Therapeutics." Cancers 16, no. 3 (2024): 638. http://dx.doi.org/10.3390/cancers16030638.

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Heat shock proteins (HSPs) are developmentally conserved families of protein found in both prokaryotic and eukaryotic organisms. HSPs are engaged in a diverse range of physiological processes, including molecular chaperone activity to assist the initial protein folding or promote the unfolding and refolding of misfolded intermediates to acquire the normal or native conformation and its translocation and prevent protein aggregation as well as in immunity, apoptosis, and autophagy. These molecular chaperonins are classified into various families according to their molecular size or weight, encom

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Tytell, M. "Release of heat shock proteins (Hsps) and the effects of extracellular Hsps on neural cells and tissues." International Journal of Hyperthermia 21, no. 5 (2005): 445–55. http://dx.doi.org/10.1080/02656730500041921.

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Claesen, Marlies, Evelyne Punnewaert, Simon Malfait, Kristof Eeckloo, Ann Van Hecke, and Ward Schrooten. "Comparative study between the Patient Participation Culture Tool and the Hospital Survey on Patient Safety Culture using retrospective data from 2014 to 2021." BMJ Open Quality 14, no. 2 (2025): e003200. https://doi.org/10.1136/bmjoq-2024-003200.

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IntroductionPatient participation and safety are pivotal in healthcare quality, internationally acknowledged for enhancing health services. This study examines the correlation between two assessment tools, the Patient Participation Culture Tool (PACT) and the Hospital Survey on Patient Safety Culture (HSPSC), using retrospective data from 2014 to 2021.MethodFor the main analysis, dimensional scores of the HSPSC and domain scores of the PACT were aggregated according to hospital and specific wards. In a second step, we used aggregated scores by hospital and profession. Descriptive statistics ou

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EINSLA, BRIAN, ETHAN GLOR, JOHN ROPER, JEFF LEITINGER, NICK NICHOLAS, and SAMANTHA WOODFIN. "The use of hollow sphere pigments as strength additives in paper and paperboard coatings—Part 2: Optimization in paperboard formulations for opacity and strength." November 2020 19, no. 11 (2020): 597–604. http://dx.doi.org/10.32964/tj19.11.597.

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This report aims to summarize the efforts in testing the properties of coatings for paperboard utilizing hollow sphere pigments (HSPs). HSPs are known to effectively scatter light and replace titanium dioxide (TiO2) in architectural coating formulations. The effect of the particle size and void fraction was evaluated, along with many coating parameters, including level of addition, binder chemistry, and blends of two HSPs. The small HSPs that have optimized voids for scattering light showed equivalent strength to the TiO2-containing control. The strength data was surprising, particularly the i

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Buttacavoli, Miriam, Gianluca Di Cara, Cesare D’Amico, et al. "Prognostic and Functional Significant of Heat Shock Proteins (HSPs) in Breast Cancer Unveiled by Multi-Omics Approaches." Biology 10, no. 3 (2021): 247. http://dx.doi.org/10.3390/biology10030247.

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Heat shock proteins (HSPs) are a well-characterized molecular chaperones protein family, classified into six major families, according to their molecular size. A wide range of tumors have been shown to express atypical levels of one or more HSPs, suggesting that they could be used as biomarkers. However, the collective role and the possible coordination of HSP members, as well as the prognostic significance and the functional implications of their deregulated expression in breast cancer (BC) are poorly investigated. Here, we used a systematic multi-omics approach to assess the HSPs expression,

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Dahl, Heather, Tina Vo, and Margarita Huerta. " Using a Science Literary Lens to Conceptualize Anxiety Around COVID-19: Strategies for Human Services Professionals." Journal of Human Services 40, no. 1 (2021): 48–63. http://dx.doi.org/10.52678/2021.4.

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Amid the COVID-19 global pandemic, Human Services Professionals (HSPs) are faced with clients experiencing increased anxiety. HSPs again must broaden their scope of competency to approach this novel, natural phenomenon. Science literacy is the understanding and application of scientific knowledge toward decisions and sensemaking. Although science literacy has many facets, one area, Crosscutting Concepts (CCCs), prioritizes individuals’ funds of knowledge to engage with new phenomena such as COVID-19. This paper describes the role of HSPs responding to COVID-19; provides a conceptual framework

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Stephanou, Anastasis, and David S. Latchman. "Transcriptional Modulation of Heat-Shock Protein Gene Expression." Biochemistry Research International 2011 (2011): 1–8. http://dx.doi.org/10.1155/2011/238601.

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Heat-shock proteins (Hsps) are molecular chaperones that are ubiquitously expressed but are also induced in cells exposed to stressful stimuli. Hsps have been implicated in the induction and propagation of several diseases. This paper focuses on regulatory factors that control the transcription of the genes encoding Hsps. We also highlight how distinct transcription factors are able to interact and modulate Hsps in different pathological states. Thus, a better understanding of the complex signaling pathways regulating Hsp expression may lead to novel therapeutic targets.

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Zheng, Hao-Yuan, Peng-Hao Qin, Kun Yang, Tong-Xian Liu, You-Jun Zhang, and Dong Chu. "Genome-Wide Identification and Analysis of the Heat-Shock Protein Gene Superfamily in Bemisia tabaci and Expression Pattern Analysis under Heat Shock." Insects 13, no. 7 (2022): 570. http://dx.doi.org/10.3390/insects13070570.

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The thermal tolerance of Bemisia tabaci MED, an invasive whitefly species with worldwide distribution, plays an important role in its ecological adaptation during the invasion process. Heat-shock proteins (HSPs) are closely related to heat resistance. In this study, 33 Hsps (BtaHsps) were identified based on sequenced genome of B. tabaci MED belonging to six HSP families, among which 22 Hsps were newly identified. The secondary structures of a further 22 BtaHsps were also predicted. The results of RT-qPCR showed that heat shock could affect the expression of 14 of the 22 Hsps newly identified

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Yurina, N. P. "The Role of Heat Shock Proteins in Plant Protection from Oxidative Stress." Молекулярная биология 57, no. 6 (2023): 949–64. http://dx.doi.org/10.31857/s0026898423060228.

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The review considers the recent progress on the role of heat shock proteins (HSPs), as well as transcription factors of heat shock proteins (HSFs) in protecting plants from oxidative stress induced by various types of abiotic and biotic stresses. HSPs are pleiotropic proteins involved in various intracellular processes and performing many important functions. In particular, HSPs increase plant resistance to stress by protecting the structure and activity of proteins of the antioxidant system. Overexpression of Hsps genes under stressful conditions, leading to an increased content of HSP, can b

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Rees, C. A. B., N. C. Hogan, D. B. Walden, and B. G. Atkinson. "Identification of mRNAs encoding low molecular mass heat-shock proteins in maize (Zea mays L.)." Canadian Journal of Genetics and Cytology 28, no. 6 (1986): 1106–14. http://dx.doi.org/10.1139/g86-154.

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Subjecting 5-day-old maize seedlings to a rapid elevation in growth temperature (heat shock; 25–42 °C) results in a shift in the pattern of protein synthesis in maize plumules from the production of a broad spectrum of proteins to the new and (or) enhanced synthesis of a small number of heat-shock proteins (HSPs). The low relative molecular mass (Mr) HSPs, and more specifically an 18-kDa HSP with four major isoelectric variants, represent the majority of HSP synthesis following cell-free translation of total cellular poly (A)+ RNAs and polyribosomal RNAs extracted from heat-shocked plumules. I

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Moseley, Pope L. "Heat shock proteins and heat adaptation of the whole organism." Journal of Applied Physiology 83, no. 5 (1997): 1413–17. http://dx.doi.org/10.1152/jappl.1997.83.5.1413.

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Moseley, Pope L. Heat shock proteins and heat adaptation of the whole organism. J. Appl. Physiol. 83(5): 1413–1417, 1997.—Adaptation to heat may occur through acclimatization or thermotolerance; however, the linkage of these phenomena is poorly understood. The importance of heat shock proteins (HSPs) in thermotolerance and differences in their accumulation in organisms adapted to the heat suggest a role for HSPs in acclimatization as well. The role of HSPs in heat adaptation of the whole organism and the interrelationships among heat adaptation, endotoxin tolerance, and cytokine resistance thr

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Jeyachandran, Sivakamavalli, Hethesh Chellapandian, Kiyun Park, and Ihn-Sil Kwak. "A Review on the Involvement of Heat Shock Proteins (Extrinsic Chaperones) in Response to Stress Conditions in Aquatic Organisms." Antioxidants 12, no. 7 (2023): 1444. http://dx.doi.org/10.3390/antiox12071444.

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Heat shock proteins (HSPs) encompass both extrinsic chaperones and stress proteins. These proteins, with molecular weights ranging from 14 to 120 kDa, are conserved across all living organisms and are expressed in response to stress. The upregulation of specific genes triggers the synthesis of HSPs, facilitated by the interaction between heat shock factors and gene promoter regions. Notably, HSPs function as chaperones or helper molecules in various cellular processes involving lipids and proteins, and their upregulation is not limited to heat-induced stress but also occurs in response to anox

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Zhang, Haifeng, Jiubo Cui, Weiwei Pei, and Dongfang Wang. "A CASSCF/CSAPT2 Study on the Reaction Pathways From HOSS to HSSO Radicals." E3S Web of Conferences 165 (2020): 05025. http://dx.doi.org/10.1051/e3sconf/202016505025.

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In this paper, we used the CASSCF/CASPT2 method to study the low-lying electronic states of the HOSS and HSSO radicals. Based on the Cs and C1 symmetries, the geometrical parameters, total energies, configurations, oscillator strengths, excitation energies, oscillator strengths and harmonic vibrational frequencies of the HOSS and HSSO radicals were calculated. We found that the ground state of HSSO radical with C1 symmetry has multi-configurational character, which leads to a significant difference of dihedral angles of HSSO radical among at our work and at References. Moreover, a transition s

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