Pearl, Laurence H.

Structure and mechanism of the Hsp90 molecular chaperone machinery

Pearl, L. H., & Prodromou, C. (2006) · Annual Review of Biochemistry

Heat shock proteins researchProtein Structure and Dynamics

Cited by 1,103

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

Therapeutic opportunities within the DNA damage response

Pearl, L. H., Schierz, A. C., Ward, S. E., Al-Lazikani, B., & Pearl, F. M. G. (2015) · Nature Reviews Cancer

DNA Repair MechanismsCancer-related Molecular Pathways

Cited by 587

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

The Hsp90 molecular chaperone: an open and shut case for treatment

Pearl, L. H., Prodromou, C., & Workman, P. (2008) · Biochemical Journal

Heat shock proteins researchUbiquitin and proteasome pathways

Cited by 447

Structure and in vivo function of Hsp90

Pearl, L. H., & Prodromou, C. (2000) · Current Opinion in Structural Biology

Heat shock proteins researchProtein Structure and Dynamics

Cited by 317

Structural basis for recruitment of glycogen synthase kinase 3β to the axin—APC scaffold complex

Dajani, R., Fraser, E., Roe, S. M., Yeo, M., Good, V. M., Thompson, V., Dale, T. C., & Pearl, L. H. (2003) · The EMBO Journal

Wnt/β-catenin signaling in development and cancerSignaling Pathways in Disease

Cited by 315

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

Structural Insights into Formation of an Active Signaling Complex between Rac and Phospholipase C Gamma 2

Bunney, T. D., Opaleye, O., Roe, S. M., Vatter, P., Baxendale, R. W., Walliser, C., Everett, K. L., Josephs, M. B., Christow, C., Rodrigues-Lima, F., et al. (2009) · Molecular Cell

Protein Kinase Regulation and GTPase SignalingReceptor Mechanisms and Signaling

Cited by 72

Macrophage migration inhibitory factor of the parasitic nematode Trichinella spiralis

TAN, T. H. P., EDGERTON, S. A. V., KUMARI, R., McALISTER, M. S. B., ROWE, S. M., NAGL, S., PEARL, L. H., SELKIRK, M. E., BIANCO, A. E., TOTTY, N. F., et al. (2001) · Biochemical Journal

Macrophage Migration Inhibitory FactorParasitic Diseases Research and Treatment

Cited by 50

Uncovering an allosteric mode of action for a selective inhibitor of human Bloom syndrome protein

Chen, X., Ali, Y. I., Fisher, C. E., Arribas-Bosacoma, R., Rajasekaran, M. B., Williams, G., Walker, S., Booth, J. R., Hudson, J. J., Roe, S. M., et al. (2021) · eLife

DNA Repair MechanismsEnzyme Structure and Function

Cited by 34

Solution structure of the Hop TPR2A domain and investigation of target druggability by NMR, biochemical and in silico approaches

Darby, J. F., Vidler, L. R., Simpson, P. J., Al-Lazikani, B., Matthews, S. J., Sharp, S. Y., Pearl, L. H., Hoelder, S., & Workman, P. (2020) · Scientific Reports

Heat shock proteins researchProtein Structure and Dynamics

Cited by 17

TopBP1 utilises a bipartite GINS binding mode to support genome replication

Day, M., Tetik, B., Parlak, M., Almeida-Hernández, Y., Räschle, M., Kaschani, F., Siegert, H., Marko, A., Sanchez-Garcia, E., Kaiser, M., et al. (2024) · Nature Communications

DNA Repair MechanismsGenomics and Chromatin Dynamics

Cited by 14

The human RIF1-Long isoform interacts with BRCA1 to promote recombinational fork repair under DNA replication stress

Dong, Q., Day, M., Saito, Y., Parker, E., Watts, L. P., Kanemaki, M. T., Oliver, A. W., Pearl, L. H., Hiraga, S.-I., & Donaldson, A. D. (2025) · Nature Communications

DNA Repair MechanismsBRCA gene mutations in cancer

Cited by 4