Results 11 to 20 of about 170,313 (323)

Transfection of Heat Shock Protein 70kDa (HSP70)

International Journal of Peptide Research and Therapeutics, 2022
Abstract Heat shock protein 70kDa (HSP70) is a major protein family in the cell protections against stress-induced denaturation and aggregation and in the folding of nascent proteins. It is a highly conserved protein that can be found in most organisms and is strongly connected to several intracellular pathways such as protein folding and ...
Maxime Gestin, Luca Falato, Michela Ciccarelli, Carmine Pasquale Cerrato, Claes Andréasson, Ülo Langel   +5 more
openaire   +1 more source

STRUCTURAL AND BIOCHEMICAL ELUCIDATION OF MOSQUITO HEAT SHOCK PROTEIN 70

International Journal of Infectious Diseases, 2023
Intro: Heat Shock Proteins function as molecular chaperones and found present in almost all living organism. Furthermore, HSPs are divided into many different classes based on their molecular mass, amino acid composition, and physiological function ...
S. Chakraborti
doaj   +1 more source

The membrane-associated transient receptor potential vanilloid channel is the central heat shock receptor controlling the cellular heat shock response in epithelial cells. [PDF]

PLoS ONE, 2013
The heat shock response (HSR) is a highly conserved molecular response to various types of stresses, including heat shock, during which heat-shock proteins (Hsps) are produced to prevent and repair damages in labile proteins and membranes.
Zohar Bromberg, Pierre Goloubinoff, Younousse Saidi, Yoram George Weiss   +3 more
doaj   +1 more source

HSP70 Gene Family in Brassica rapa: Genome-Wide Identification, Characterization, and Expression Patterns in Response to Heat and Cold Stress

Cells, 2022
Heat shock proteins protect plants from abiotic stress, such as salt, drought, heat, and cold stress. HSP70 is one of the major members of the heat shock protein family.
Javaria Tabusam, Qiling Shi, Daling Feng, Sumer Zulfiqar, Shuxing Shen, Wei Ma, Jianjun Zhao   +6 more
doaj   +1 more source

Heat shock proteins: Biological functions, pathological roles, and therapeutic opportunities

MedComm, 2022
The heat shock proteins (HSPs) are ubiquitous and conserved protein families in both prokaryotic and eukaryotic organisms, and they maintain cellular proteostasis and protect cells from stresses.
Chen Hu, Jing Yang, Z. Qi, Hong Wu, Bei-lei Wang, F. Zou, Husheng Mei, Jing Liu, Wen-chao Wang, Qingsong Liu   +9 more
semanticscholar   +1 more source

Identification of a testis-enriched heat shock protein and fourteen members of Hsp70 family in the swamp eel. [PDF]

PLoS ONE, 2013
BACKGROUND: Gonad differentiation is one of the most important developmental events in vertebrates. Some heat shock proteins are associated with gonad development. Heat shock protein 70 (Hsp70) in the teleost fish and its roles in sex differentiation are
Yan He, Majing Luo, Minhan Yi, Yue Sheng, Yibin Cheng, Rongjia Zhou, Hanhua Cheng   +6 more
doaj   +1 more source

Eukaryotic DNAJ/K Database: A Comprehensive Phylogenomic Analysis Platform for the DNAJ/K Family [PDF]

Genomics & Informatics, 2013
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).
Kyeongchae Cheong, Jaehyuk Choi, Jaeyoung Choi, Jongsun Park, Suwang Jang, Yong-Hwan Lee   +5 more
doaj   +1 more source

Hsp70/J-protein machinery from Glossina morsitans morsitans, vector of African trypanosomiasis. [PDF]

PLoS ONE, 2017
Tsetse flies (Glossina spp.) are the sole vectors of the protozoan parasites of the genus Trypanosoma, the causative agents of African Trypanosomiasis.
Stephen J Bentley, Aileen Boshoff
doaj   +1 more source

Hsp70 in mitochondrial biogenesis [PDF]

, 1994
The family of hsp70 (70 kilodalton heat shock protein) molecular chaperones plays an essential and diverse role in cellular physiology, Hsp70 proteins appear to elicit their effects by interacting with polypeptides that present domains which exhibit non ...
A. Tzagoloff, A. Tzagoloff, A.J. Caplan, A.J. Caplan, B.D. Gambill, B.S. Glick, C.K. Suzuki, D. Ang, D. M. Cyr, D.M. Cyr, D.M. Cyr, D.M. Cyr, D.M. Cyr, D.P. Atencio, E. Ikeda, E. Kutejová, E.A. Craig, E.A. Craig, F.-U. Hartl, G.S.P. Groot, H.R.B. Pelham, J. Ostermann, J. Rassow, J.F. Dice, J.P. Hendrick, K. Liberek, L. Dyck van, M. Eilers, M. Kiebler, M. Schleyer, M.-J. Gething, M.Y. Cheng, N. Rowley, N. Wang, P. Borst, P. Terpstra, P.-J. Kang, R. A. Stuart, R.A. Stuart, R.A. Stuart, R.B. Deshaies, R.G. Hadikusumo, R.J. Nelson, R.P. Beckman, S. Lindquist, S. Rospert, S.T. Hwang, T. Langer, U.C. Manning-Krieg, W. Neupert, W. Neupert, W. Voos, W.J. Chirico, Z. Xia   +53 more
core   +1 more source

Heat-shock pretreatment inhibits sorbitol-induced apoptosis in K562, U937 and HeLa cells. [PDF]

, 2009
The aim of this study was to determine whether heat-shock pretreatment exerted a protective effect against sorbitol-induced apoptotic cell death in K562, U937 and HeLa cell lines and whether such protection was associated with a decreased cytochrome c
Aventaggiato, Michele, De Martino, Luisa, Di Stefano, Carla, Fiorito, Filomena, Indelicato, Manuela, Marfe, Gabriella, Pucci, Bruna, Russo, Matteo A., Tafani, Marco   +8 more
core   +1 more source