Results 51 to 60 of about 477,265 (189)

Assembly and biochemical properties of a human chaperone/co-chaperone protein complex [PDF]

, 2010
The 70kDa members of the heat shock protein family (eg. Hsp70) function as molecular chaperones by binding to exposed hydrophobic patches on nascent polypeptides forming non-covalent interactions, thereby preventing their aggregation and facilitating ...
Vydyanath, A.
core   +1 more source

Targeting opioid receptors with pharmacological chaperones

Pharmacological Research, 2014
G protein-coupled receptors (GPCRs) are polytopic membrane proteins that have a pivotal role in cellular signaling. Like other membrane proteins, they fold in the endoplasmic reticulum (ER) before they are transported to the plasma membrane. The ER quality control monitors the folding process and misfolded proteins and slowly folding intermediates are ...
Ulla E, Petäjä-Repo, Jarkko J, Lackman
openaire   +2 more sources

Heat Shock Protein 70 (HSP70) Induction: Chaperonotherapy for Neuroprotection after Brain Injury

Cells, 2020
The 70 kDa heat shock protein (HSP70) is a stress-inducible protein that has been shown to protect the brain from various nervous system injuries. It allows cells to withstand potentially lethal insults through its chaperone functions.
Jong Youl Kim, Sumit Barua, Mei Ying Huang, Joohyun Park, Midori A. Yenari, Jong Eun Lee   +5 more
doaj   +1 more source

Identification of Cytoplasmic Chaperone Networks Relevant for Respiratory Syncytial Virus Replication

Frontiers in Microbiology, 2022
RNA viruses have limited coding capacity and must therefore successfully subvert cellular processes to facilitate their replication. A fundamental challenge faced by both viruses and their hosts is the ability to achieve the correct folding and assembly ...
Victor Latorre, Ron Geller
doaj   +1 more source

Pharmacologic chaperoning as a strategy to treat Gaucher disease [PDF]

The FEBS Journal, 2007
We briefly introduce the most common lysosomal storage disorder, Gaucher disease, concisely describe the Food and Drug Administration approved strategies to ameliorate Gaucher disease, and then outline the emerging pharmacologic chaperone strategy that offers the promise to remedy this malady.
Zhanqian, Yu, Anu R, Sawkar, Jeffery W, Kelly   +2 more
openaire   +2 more sources

The Human TPR Protein TTC4 Is a Putative Hsp90 Co-Chaperone Which Interacts with CDC6 and Shows Alterations in Transformed Cells. [PDF]

, 2008
BACKGROUND: The human TTC4 protein is a TPR (tetratricopeptide repeat) motif-containing protein. The gene was originally identified as being localized in a genomic region linked to breast cancer and subsequent studies on melanoma cell lines revealed ...
Bennett, D, Cotterill, S, Dorothy Bennett, Gilles Crevel, Bennett Dorothy, Cotterill Sue, Sue Cotterill, Crevel Gilles, Crevel, G   +8 more
core   +2 more sources

Pharmacological Chaperones Attenuate the Development of Opioid Tolerance [PDF]

International Journal of Molecular Sciences, 2020
Opioids are potent analgesics widely used to control acute and chronic pain, but long-term use induces tolerance that reduces their effectiveness. Opioids such as morphine bind to mu opioid receptors (MORs), and several downstream signaling pathways are capable of inducing tolerance. We previously reported that signaling from the endoplasmic reticulum (
Youta Okuyama, Hisayo Jin, Hiroshi Kokubun, Tomohiko Aoe   +3 more
openaire   +2 more sources

Structure of human lysosomal acid α-glucosidase–a guide for the treatment of Pompe disease

Nature Communications, 2017
Pompe disease is caused by mutations in lysosomal acid α-glucosidase (GAA) and patients are being treated with recombinant human α-glucosidase (rhGAA).
Véronique Roig-Zamboni, Beatrice Cobucci-Ponzano, Roberta Iacono, Maria Carmina Ferrara, Stanley Germany, Yves Bourne, Giancarlo Parenti, Marco Moracci, Gerlind Sulzenbacher   +8 more
doaj   +1 more source

Natural products triptolide, celastrol, and withaferin A inhibit the chaperone activity of peroxiredoxin I [PDF]

, 2015
Peroxiredoxin I (Prx I) plays an important role in cancer development and inflammation. It is a dual-functional protein which acts as both an antioxidant enzyme and a molecular chaperone. While there have been intensive studies on its peroxidase activity,
Heck, AJR, Yang, D, Tao, X, Kao, Richard, Lee, On Yi, Rose, RJ, Sub Biomol.Mass Spect. and Proteomics, Zhao, Q, Ding, Y, Chen, P, Zhang, ZF, Zhao, Qian, Lee, OY, Deng, ZS, Heck, Albert J R, Gao, Peng, Zhao, H, Zhang, Zhehao, Sub Biomol.Mass Spectrometry & Proteom., Biomolecular Mass Spectrometry and Proteomics, Zhao, Hong, Rose, Rebecca J., Yang, Dan, Gao, P, Kao, RYT, Chen, Pin, Tao, Xin Pei, Deng, Zhangshuang, Ding, Yu   +28 more
core   +1 more source

Pharmacological effectors of GRP78 chaperone in cancers

Biochemical Pharmacology, 2019
The protein chaperone GRP78 is a master regulator of endoplasmic reticulum (ER) functions and is frequently over-expressed at the surface of cancer cells where it contributes to chemo-resistance. It represents a well-studied ER stress marker but an under-explored target for new drug development.
Bailly, Christian, Waring, Michael J.
openaire   +3 more sources