Piper, Peter W.

Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin.

Roe, S. M., Prodromou, C., O'Brien, R., Ladbury, J. E., Piper, P. W., & Pearl, L. H. (1999) · Journal of Medicinal Chemistry

Heat shock proteins researchProtein Structure and Dynamics

Cited by 1,004

Crystal structure of an Hsp90–nucleotide–p23/Sba1 closed chaperone complex

Ali, M. M. U., Roe, S. M., Vaughan, C. K., Meyer, P., Panaretou, B., Piper, P. W., Prodromou, C., & Pearl, L. H. (2006) · Nature

Heat shock proteins researchProtein Structure and Dynamics

Cited by 962

ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo

Panaretou, B., Prodromou, C., Roe, S. M., O'Brien, R., Ladbury, J. E., Piper, P. W., & Pearl, L. H. (1998) · The EMBO Journal

Heat shock proteins researchProtein Structure and Dynamics

Cited by 735

The ATPase cycle of Hsp90 drives a molecular ‘clamp’ via transient dimerization of the N‐terminal domains

Prodromou, C., Panaretou, B., Chohan, S., Siligardi, G., O'Brien, R., Ladbury, J. E., Roe, S. M., Piper, P. W., & Pearl, L. H. (2000) · The EMBO Journal

Heat shock proteins researchProtein Structure and Dynamics

Cited by 492

Structural and Functional Analysis of the Middle Segment of Hsp90: Implications for ATP Hydrolysis and Client Protein and Cochaperone Interactions

Meyer, P., Prodromou, C., Hu, B., Vaughan, C., Roe, S. M., Panaretou, B., Piper, P. W., & Pearl, L. H. (2003) · Molecular Cell

Heat shock proteins researchProtein Structure and Dynamics

Cited by 491

A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone

Prodromou, C., Roe, S. M., Piper, P. W., & Pearl, L. H. (1997) · Nature Structural Biology

Heat shock proteins researchProtein Structure and Dynamics

Cited by 239

Co-chaperone regulation of conformational switching in the Hsp90 ATPase cycle

Siligardi, G., Hu, B., Panaretou, B., Piper, P. W., Pearl, L. H., & Prodromou, C. (2004) · Journal of Biological Chemistry

Heat shock proteins researchProtein Structure and Dynamics

Cited by 207

Swe1Wee1-Dependent Tyrosine Phosphorylation of Hsp90 Regulates Distinct Facets of Chaperone Function

Mollapour, M., Tsutsumi, S., Donnelly, A. C., Beebe, K., Tokita, M. J., Lee, M.-J., Lee, S., Morra, G., Bourboulia, D., Scroggins, B. T., et al. (2010) · Molecular Cell

Heat shock proteins researchUbiquitin and proteasome pathways

Cited by 196

A two-hybrid screen of the yeast proteome for Hsp90 interactors uncovers a novel Hsp90 chaperone requirement in the activity of a stress-activated mitogen-activated protein kinase, Slt2p (Mpk1p).

Millson, S. H., Truman, A. W., King, V., Prodromou, C., Pearl, L. H., & Piper, P. W. (2005) · Eukaryotic Cell

Heat shock proteins researchFungal and yeast genetics research

Cited by 172

Threonine 22 Phosphorylation Attenuates Hsp90 Interaction with Cochaperones and Affects Its Chaperone Activity

Mollapour, M., Tsutsumi, S., Truman, A. W., Xu, W., Vaughan, C. K., Beebe, K., Konstantinova, A., Vourganti, S., Panaretou, B., Piper, P. W., et al. (2011) · Molecular Cell

Heat shock proteins researchUbiquitin and proteasome pathways

Cited by 165

In the yeast heat shock response, Hsf1-directed induction of Hsp90 facilitates the activation of the Slt2 (Mpk1) mitogen-activated protein kinase required for cell integrity.

Truman, A. W., Millson, S. H., Nuttall, J. M., Mollapour, M., Prodromou, C., & Piper, P. W. (2007) · Eukaryotic Cell

Heat shock proteins researchFungal and yeast genetics research

Cited by 59