Results 81 to 90 of about 109,885 (301)
Macrocyclic Inhibitors of Hsp90 [PDF]
Current Topics in Medicinal Chemistry, 2010 Heat shock proteins (HSP) are a family of highly conserved proteins, whose expression increases in response to stresses that may threaten cell survival. Over the past decade, heat shock protein 90 (Hsp90) has emerged as a potential therapeutic target for cancer as it plays a vital role in normal cell maturation and acts as a molecular chaperone for ...
Johnson, V +4 more
openaire +3 more sources
Advanced Science, EarlyView.Molecular, genetic, virological, and biochemical analysis in combination with global proteome and phosphoproteome profiling and functional assays were applied to study the role of PR130 in the context of HSV‐1 replication. The observations reveal that host‐intrinsic mechanisms regulate HSV‐1 replication and highlight PR130 as a susceptibility factor of
Johannes Jungwirth +10 more
wiley +1 more source
Expression of HSP90 Gene in the Cryopreserved Bovine Spermatozoa
Scientific Papers Animal Science and Biotechnologies, 2023 Cryopreservation is a technique, commonly used for a long-term storage of male gametes as an effective way to preserve their longevity and vitality. During cryopreservation and following the thawing process, sperm cells are exposed to thermal stress ...
Filip Benko +4 more
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Virulence of HtpG+ and HtpG− strains of Yersinia pestis for Mice and Guinea Pigs
Проблемы особо опасных инфекций, 2020 HtpG (high-temperature protein G) is a bacterial homologue of the highly conserved molecular chaperone Hsp90 of eukaryotes, which plays an important role in protection against stress in many bacterial species.
E. A. Krasil’nikova +7 more
doaj +1 more source
HSP90 and the chaperoning of cancer
Nature Reviews Cancer, 2005 Standing watch over the proteome, molecular chaperones are an ancient and evolutionarily conserved class of proteins that guide the normal folding, intracellular disposition and proteolytic turnover of many of the key regulators of cell growth, differentiation and survival.
Luke, Whitesell, Susan L, Lindquist
openaire +2 more sources
Pyroptosis‐Inducing Engineered Microparticles for Cancer Immunotherapy
Advanced Science, EarlyView.Engineered microparticles co‐delivering geldanamycin and dual nanobodies induce targeted pyroptosis and block PD‐L1 and CD47 pathways, reprogramming the tumor microenvironment and achieving potent antitumor immunity in lung cancer models with minimal toxicity.
Tianli Hao +12 more
wiley +1 more source
Drug Design, Development and Therapy, 2020 Liang-Jian Hong, Ai-Jun Chen, Feng-Zeng Li, Ke-Jun Chen, Sheng Fang Department of Dermatology, The First Affiliated Hospital of Chongqing Medical University, Chongqing 400016, People’s Republic of ChinaCorrespondence: Sheng FangDepartment of ...
Hong LJ, Chen AJ, Li FZ, Chen KJ, Fang S
doaj
Covalent Reprogramming of Kinase Binders to Modulate Protein Abundance
Advanced Science, EarlyView.Electrophilic remodeling of a broad‐spectrum kinase binder reveals how subtle chemical changes reprogram protein fate. An acrylamide analog of a multi‐kinase binder selectively stabilizes Aurora kinase A (AURKA) by suppressing its ubiquitination, while a short‐linker variant converts this stabilizer into a degrader.
Chen Mozes +4 more
wiley +1 more source
The clickable activity-based probe of anti-apoptotic calenduloside E
Pharmaceutical Biology, 2019 Context: Calenduloside E (CE), one of the primary natural products found in Aralia elata (Miq.) Seem. (Araliaceae), possesses prominent anti-apoptotic potential.
Yu Tian +8 more
doaj +1 more source
Calcyclin Binding Protein/Siah-1 Interacting Protein Is a Hsp90 Binding Chaperone. [PDF]
PLoS ONE, 2016 The Hsp90 chaperone activity is tightly regulated by interaction with many co-chaperones. Since CacyBP/SIP shares some sequence homology with a known Hsp90 co-chaperone, Sgt1, in this work we performed a set of experiments in order to verify whether ...
Agnieszka Góral +6 more
doaj +1 more source