The C-Terminal Half of Heat Shock Protein 90 Represents a Second Site for Pharmacologic Intervention in Chaperone Function

Publisher： Bentham Science Publishers

E-ISSN： 1873-5576|3|5|343-347

ISSN： 1568-0096

Source： Current Cancer Drug Targets, Vol.3, Iss.5, 2003-10, pp. : 343-347

Disclaimer: Any content in publications that violate the sovereignty, the constitution or regulations of the PRC is not accepted or approved by CNPIEC.

Previous Menu Next

Abstract

Related content

Post-translational modification of heat-shock protein 90: impact on chaperone function

By Scroggins Bradley T   Neckers Len  

Expert Opinion on Drug Discovery, Vol. 2, Iss. 10, 2007-10 ,pp. : 1403-1414

Informa Healthcare

Access to resources Recommend Favorite

The Heat Shock Protein 90 Chaperone Complex: An Evolving Therapeutic Target

By  

Current Cancer Drug Targets, Vol. 8, Iss. 6, 2008-09 ,pp. : 522-535

Bentham Science Publishers

Access to resources Recommend Favorite

Targeting Heat Shock Protein 90 for Malaria

By  

Mini Reviews in Medicinal Chemistry, Vol. 13, Iss. 13, 2013-11 ,pp. : 1903-1920

Bentham Science Publishers

Access to resources Recommend Favorite

Advances in the discovery and development of heat-shock protein 90 inhibitors for cancer treatment

By Patel Hardik J   Modi Shanu   Chiosis Gabriela   Taldone Tony  

Expert Opinion on Drug Discovery, Vol. 6, Iss. 5, 2011-05 ,pp. : 559-587

Informa Healthcare

Access to resources Recommend Favorite

Heat-shock protein 90 inhibitors as novel cancer chemotherapeutics – an update

By Neckers Len   Neckers Katharine  

Expert Opinion on Emerging Drugs, Vol. 10, Iss. 1, 2005-02 ,pp. : 137-149

Informa Healthcare

Access to resources Recommend Favorite