Results 51 to 60 of about 3,381,955 (240)

Membrane composition and thermodynamic identity as boundaries of life for synthetic cell research

FEBS Letters, EarlyView.
What makes a cell a cell? The boundary of a living cell is not just a wall. Read as a Markov blanket, the membrane separates internal from external states, generating identity and non‐equilibrium order. Can this identity be rebuilt from scratch in a synthetic cell?
Caterina Presutti, Bert Poolman
wiley   +1 more source

Hsp90 governs dispersion and drug resistance of fungal biofilms [PDF]

, 2011
Fungal biofilms are a major cause of human mortality and are recalcitrant to most treatments due to intrinsic drug resistance. These complex communities of multiple cell types form on indwelling medical devices and their eradication often requires ...
Ramage Gordon, Lopez-Ribot, J.L., Rajendran Ranjith, Ramage, G., Leah E. Cowen, Uppuluri Priya, Robbins, N., Priya Uppuluri, Rajendran, R., Andes, D., Jose L Lopez-Ribot, David Andes, Leah E Cowen, Nicole Robbins, Uppuluri, P., Robbins Nicole, Nett Jeniel, Lopez-Ribot Jose L., Jose L. Lopez-Ribot, Cowen, L.E., Nett, J., Ranjith Rajendran, Gordon Ramage, Jeniel Nett, Andes David, Cowen Leah E.   +25 more
core   +2 more sources

Heat shock protein 90: biological functions, diseases, and therapeutic targets

MedComm
Heat shock protein 90 (Hsp90) is a predominant member among Heat shock proteins (HSPs), playing a central role in cellular protection and maintenance by aiding in the folding, stabilization, and modification of diverse protein substrates. It collaborates
Huiyun Wei, Yingying Zhang, Yilin Jia, Xunan Chen, Tengda Niu, Aniruddha Chatterjee, Pengxing He, Guiqin Hou   +7 more
doaj   +1 more source

Discovery and development of natural heat shock protein 90 inhibitors in cancer treatment

Acta Pharmaceutica Sinica B, 2012
Heat shock protein 90 (Hsp90) is a highly conserved molecular chaperone that plays a vital role in the signal transduction of cancers. Hsp90 inhibitors are able to inhibit Hsp90 or the complex of Hsp90 and co-chaperones resulting in the degradation of ...
Yong Li, Dongmei Zhang, Jun Xu, Junmin Shi, Lei Jiang, Nan Yao, Wencai Ye   +6 more
doaj   +1 more source

Chromatin Immunoprecipitation (ChIP) of Heat Shock Protein 90 (Hsp90)

, 2023
Chromatin immunoprecipitation followed by sequencing (ChIP-seq) is a widely used technique for genome-wide mapping of protein-DNA interactions and epigenetic marks in vivo. Recent studies have suggested an important role of heat shock protein 90 (Hsp90) in chromatin. This molecular chaperone assists other proteins to acquire their mature and functional
openaire   +2 more sources

The VHL tumor suppressor at the crossroad of protein folding, aggregation, and cancer

Molecular Oncology, EarlyView.
Mutations, environmental stress, and chaperone dysfunction can destabilize pVHL, promoting its conversion from the native folded state into amyloid‐like assemblies. This transition may contribute to protein storage, cell dormancy, survival, and drug resistance.
Lara Abad, Silvio Carlo Ermanno Tosatto, Emanuela Leonardi   +2 more
wiley   +1 more source

Characterization of a wheat HSP70 gene and its expression in response to stripe rust infection and abiotic stresses [PDF]

, 2011
Members of the family of 70-kD heat shock proteins (HSP70 s) play various stress-protective roles in plants. In this study, a wheat HSP70 gene was isolated from a suppression subtractive hybridization (SSH) cDNA library of wheat leaves infected by ...
Wang, S.J., Dai, X.W., Duan, Y.H., Kang, Z.S., Ding, K., Chen, Y.Y., Govers, F., Huang, L.L., Guo, J., Zhang, H.   +9 more
core   +1 more source

The evolution of heat shock protein 90 C-terminal inhibitors: From novobiocin to potential clinical candidates

Cell Stress & Chaperones
Heat shock protein 90 (Hsp90) is a highly conserved molecular chaperone that regulates the maturation of various client proteins. Most therapeutic studies have focused on N-terminal Hsp90 inhibitors, but these are limited by dose-escalating toxicities ...
Xiaosheng Jiang, Brian S.J. Blagg
doaj   +1 more source

In silico analysis of the HSP90 chaperone system from the African trypanosome, Trypanosoma brucei

Frontiers in Molecular Biosciences, 2022
African trypanosomiasis is a neglected tropical disease caused by Trypanosoma brucei (T. brucei) and spread by the tsetse fly in sub-Saharan Africa. The trypanosome relies on heat shock proteins for survival in the insect vector and mammalian host.
Miebaka Jamabo, Stephen John Bentley, Paula Macucule-Tinga, Praise Tembo, Adrienne Lesley Edkins, Aileen Boshoff   +5 more
doaj   +1 more source

RET Is a Heat Shock Protein 90 (HSP90) Client Protein and Is Knocked Down upon HSP90 Pharmacological Block [PDF]

The Journal of Clinical Endocrinology & Metabolism, 2010
Mutations of the RET receptor tyrosine kinase are associated to multiple endocrine neoplasia type 2 (MEN2) and sporadic medullary thyroid carcinoma (MTC). The heat shock protein (HSP) 90 chaperone is required for folding and stability of several kinases.
Alfano L., Guida T., Provitera L., VECCHIO, GIANCARLO, Billaud M., SANTORO, MASSIMO, CARLOMAGNO, Francesca   +6 more
openaire   +5 more sources