Structural and functional coupling of Hsp90- and Sgt1-centred multi-protein complexes

Por Zhang, Minghao, Botër, Marta, Li, Kuoyu, Kadota, Yasuhiro, Panaretou, Barry, Prodromou, Chrisostomos, Shirasu, Ken, Pearl, Laurence H
Publicado em 2008

Charged linker sequence modulates eukaryotic heat shock protein 90 (Hsp90) chaperone activity

Por Tsutsumi, Shinji, Mollapour, Mehdi, Prodromou, Chrisostomos, Lee, Chung-Tien, Panaretou, Barry, Yoshida, Soichiro, Mayer, Matthias P., Neckers, Leonard M.
Publicado em 2012

Investigating the protein-protein interactions of the yeast Hsp90 chaperone system by two-hybrid analysis: potential uses and limitations of this approach

Por Millson, Stefan H., Truman, Andrew W., Wolfram, Francis, King, Victoria, Panaretou, Barry, Prodromou, Chrisostomos, Pearl, Laurence H., Piper, Peter W.
Publicado em 2004

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

Por Ali, Maruf M. U., Roe, S. Mark, Vaughan, Cara, Meyer, Phillipe, Panaretou, Barry, Piper, Peter W., Prodromou, Chrisostomos, Pearl, Laurence H.
Publicado no Nature (2006)

Chaperone ligand-discrimination by the TPR-domain protein Tah1

Por Millson, Stefan H., Vaughan, Cara K., Zhai, Chao, Ali, Maruf M. U., Panaretou, Barry, Piper, Peter W., Pearl, Laurence H., Prodromou, Chrisostomos
Publicado em 2008

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

Por Prodromou, Chrisostomos, Panaretou, Barry, Chohan, Shahzad, Siligardi, Giuliano, O’Brien, Ronan, Ladbury, John E., Roe, S.Mark, Piper, Peter W., Pearl, Laurence H.
Publicado em 2000

Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery

Por Meyer, Philippe, Prodromou, Chrisostomos, Liao, Chunyan, Hu, Bin, Mark Roe, S, Vaughan, Cara K, Vlasic, Ignacija, Panaretou, Barry, Piper, Peter W, Pearl, Laurence H
Publicado em 2004

Hsp90-Dependent Activation of Protein Kinases Is Regulated by Chaperone-Targeted Dephosphorylation of Cdc37

Por Vaughan, Cara K., Mollapour, Mehdi, Smith, Jennifer R., Truman, Andrew, Hu, Bin, Good, Valerie M., Panaretou, Barry, Neckers, Len, Clarke, Paul A., Workman, Paul, Piper, Peter W., Prodromou, Chrisostomos, Pearl, Laurence H.
Publicado em 2008

Threonine 22 phosphorylation attenuates Hsp90 interaction with co-chaperones and affects its chaperone activity

Por Mollapour, Mehdi, Tsutsumi, Shinji, Truman, Andrew W., Xu, Wanping, Vaughan, Cara K., Beebe, Kristin, Konstantinova, Anna, Vourganti, Srinivas, Panaretou, Barry, Piper, Peter W., Trepel, Jane B., Prodromou, Chrisostomos, Pearl, Laurence H., Neckers, Len
Publicado em 2011

Tumor suppressor Tsc1 is a new Hsp90 co‐chaperone that facilitates folding of kinase and non‐kinase clients

Por Woodford, Mark R, Sager, Rebecca A, Marris, Elijah, Dunn, Diana M, Blanden, Adam R, Murphy, Ryan L, Rensing, Nicholas, Shapiro, Oleg, Panaretou, Barry, Prodromou, Chrisostomos, Loh, Stewart N, Gutmann, David H, Bourboulia, Dimitra, Bratslavsky, Gennady, Wong, Michael, Mollapour, Mehdi
Publicado no EMBO J (2017)

The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug binding

Por Woodford, Mark R., Dunn, Diana M., Blanden, Adam R., Capriotti, Dante, Loiselle, David, Prodromou, Chrisostomos, Panaretou, Barry, Hughes, Philip F., Smith, Aaron, Ackerman, Wendi, Haystead, Timothy A., Loh, Stewart N., Bourboulia, Dimitra, Schmidt, Laura S., Marston Linehan, W., Bratslavsky, Gennady, Mollapour, Mehdi
Publicado no Nat Commun (2016)

Swe1(Wee1)-dependent tyrosine phosphorylation of Hsp90 regulates distinct facets of chaperone function

Por Mollapour, Mehdi, Tsutsumi, Shinji, Donnelly, Alison C., Beebe, Kristin, Tokita, Mari J., Lee, Min-Jung, Lee, Sunmin, Morra, Giulia, Bourboulia, Dimitra, Scroggins, Bradley T., Colombo, Giorgio, Blagg, Brian S., Panaretou, Barry, Stetler-Stevenson, William G., Trepel, Jane B., Piper, Peter W., Prodromou, Chrisostomos, Pearl, Laurence H., Neckers, Len
Publicado em 2010

Asymmetric Hsp90 N-domain SUMOylation recruits Aha1 and ATP-competitive inhibitors

Por Mollapour, Mehdi, Bourboulia, Dimitra, Beebe, Kristin, Woodford, Mark R., Polier, Sigrun, Hoang, Anthony, Chelluri, Raju, Li, Yu, Guo, Ailan, Lee, Min-Jung, Fotooh-Abadi, Elham, Khan, Sahar, Prince, Thomas, Miyajima, Naoto, Yoshida, Soichiro, Tsutsumi, Shinji, Xu, Wanping, Panaretou, Barry, Stetler-Stevenson, William G., Bratslavsky, Gennady, Trepel, Jane B., Prodromou, Chrisostomos, Neckers, Len
Publicado em 2014

Mps1 Mediated Phosphorylation of Hsp90 Confers Renal Cell Carcinoma Sensitivity and Selectivity to Hsp90 Inhibitors

Por Woodford, Mark R., Truman, Andrew W., Dunn, Diana M., Jensen, Sandra M., Cotran, Richard, Bullard, Renee, Abouelleil, Mourad, Beebe, Kristin, Wolfgeher, Donald, Wierzbicki, Sara, Post, Dawn E., Caza, Tiffany, Tsutsumi, Shinji, Panaretou, Barry, Kron, Stephen J., Trepel, Jane B., Landas, Steve, Prodromou, Chrisostomos, Shapiro, Oleg, Stetler-Stevenson, William G., Bourboulia, Dimitra, Neckers, Len, Bratslavsky, Gennady, Mollapour, Mehdi
Publicado no Cell Rep (2016)

c-Abl Mediated Tyrosine Phosphorylation of Aha1 Activates Its Co-chaperone Function in Cancer Cells

Por Dunn, Diana M., Woodford, Mark R., Truman, Andrew W., Jensen, Sandra M., Schulman, Jacqualyn, Caza, Tiffany, Remillard, Taylor C., Loiselle, David, Wolfgeher, Donald, Blagg, Brian S.J., Franco, Lucas, Haystead, Timothy A., Daturpalli, Soumya, Mayer, Matthias P., Trepel, Jane B., Morgan, Rhodri M.L., Prodromou, Chrisostomos, Kron, Stephen J., Panaretou, Barry, Stetler-Stevenson, William G., Landas, Steve K., Neckers, Len, Bratslavsky, Gennady, Bourboulia, Dimitra, Mollapour, Mehdi
Publicado no Cell Rep (2015)