4.6 Article

Development of the first geldanamycin-based HSP90 degraders

相关参考文献

注意:仅列出部分参考文献,下载原文获取全部文献信息。
Article Chemistry, Medicinal

Discovery of BP3 as an efficacious proteolysis targeting chimera (PROTAC) degrader of HSP90 for treating breast cancer

Quanyu Liu et al.

Summary: This study systematically described the design, synthesis, and evaluation of HSP90 degraders based on the PROTAC strategy. The candidate compound 16b (BP3) was found to effectively degrade HSP90 and inhibit the growth of human breast cancer cells. The results suggest that the HSP90-targeting PROTAC strategy has potential novel applications in breast cancer therapy.

EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY (2022)

Article Chemistry, Multidisciplinary

Development of a First-in-Class Small-Molecule Inhibitor of the C-Terminal Hsp90 Dimerization

Sanil Bhatia et al.

Summary: Heat shock proteins 90 (Hsp90) are promising therapeutic targets for cancer treatment due to their involvement in stabilizing oncoproteins. Most Hsp90 inhibitors target the N-terminal domain, but modulators that interfere with the C-terminal domain have shown potential without inducing adverse effects. A first-in-class small-molecule inhibitor targeting Hsp90 C-terminal domain dimerization has been developed, which reduces leukemia cells and induces apoptosis without inducing protective resistance mechanisms.

ACS CENTRAL SCIENCE (2022)

Article Chemistry, Medicinal

Solid-Phase Synthesis of Cereblon-Recruiting Selective Histone Deacetylase 6 Degraders (HDAC6 PROTACs) with Antileukemic Activity

Laura Sinatra et al.

Summary: In this study, we achieved the chemical knockdown of histone deacetylase 6 (HDAC6) using proteolysis targeting chimera (PROTAC) technology. Two series of cereblon-recruiting PROTACs were synthesized, allowing the rapid preparation of HDAC6 degrader mini libraries. Both PROTAC series demonstrated selective degradation of HDAC6 in leukemia cell lines.

JOURNAL OF MEDICINAL CHEMISTRY (2022)

Review Biochemistry & Molecular Biology

Role of HSP90 in Cancer

Bereket Birbo et al.

Summary: HSP90 is a crucial chaperone protein with different isoforms present in various cell compartments. Elevated levels of HSP90 have been linked to cancer, making it a target for cancer drugs. Differences in conformation between normal HSP90 and tumor phenotype HSP90 have led to the development of HSP90 inhibitors as a potential cancer treatment.

INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES (2021)

Article Biochemistry & Molecular Biology

Unleashing the full potential of Hsp90 inhibitors as cancer therapeutics through simultaneous inactivation of Hsp90, Grp94, and TRAP1

Hye-Kyung Park et al.

EXPERIMENTAL AND MOLECULAR MEDICINE (2020)

Review Biochemistry & Molecular Biology

Spotlight on 17-AAG as an Hsp90 inhibitor for molecular targeted cancer treatment

Sona Talaei et al.

CHEMICAL BIOLOGY & DRUG DESIGN (2019)

Article Cell Biology

Structure, Function, and Regulation of the Hsp90 Machinery

Maximilian M. Biebl et al.

COLD SPRING HARBOR PERSPECTIVES IN BIOLOGY (2019)

Review Biochemistry & Molecular Biology

The HSP90 Family: Structure, Regulation, Function, and Implications in Health and Disease

Abdullah Hoter et al.

INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES (2018)

Review Cell Biology

The HSP90 chaperone machinery

Florian H. Schopf et al.

NATURE REVIEWS MOLECULAR CELL BIOLOGY (2017)

Review Pharmacology & Pharmacy

Heat shock protein 90 inhibitors in the treatment of cancer: current status and future directions

Komal Jhaveri et al.

EXPERT OPINION ON INVESTIGATIONAL DRUGS (2014)

Article Pharmacology & Pharmacy

The Therapeutic Target Hsp90 and Cancer Hallmarks

Yoshihiko Miyata et al.

CURRENT PHARMACEUTICAL DESIGN (2013)

Article Chemistry, Medicinal

Synthesis of novel fluorescent probes for the molecular chaperone Hsp90

L Llauger-Bufi et al.

BIOORGANIC & MEDICINAL CHEMISTRY LETTERS (2003)

Article Chemistry, Medicinal

Synthesis and evaluation of geldanamycin-testosterone hybrids

SD Kuduk et al.

BIOORGANIC & MEDICINAL CHEMISTRY LETTERS (2000)