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Literature DB >> 23075983

Molecular biology: Choose your protein partners.

Rahul S Samant, Paul Workman.

Abstract

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Year: 2012 PMID： 23075983 DOI： 10.1038/490351a

Source DB: PubMed Journal: Nature ISSN： 0028-0836 Impact factor: 49.962

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12 in total

1. Structure of an Hsp90-Cdc37-Cdk4 complex.

Authors: Cara K Vaughan; Ulrich Gohlke; Frank Sobott; Valerie M Good; Maruf M U Ali; Chrisostomos Prodromou; Carol V Robinson; Helen R Saibil; Laurence H Pearl
Journal: Mol Cell Date: 2006-09-01 Impact factor: 17.970

2. Activated B-RAF is an Hsp90 client protein that is targeted by the anticancer drug 17-allylamino-17-demethoxygeldanamycin.

Authors: Silvy da Rocha Dias; Frank Friedlos; Yvonne Light; Caroline Springer; Paul Workman; Richard Marais
Journal: Cancer Res Date: 2005-12-01 Impact factor: 12.701

3. Hsp90 as a capacitor for morphological evolution.

Authors: S L Rutherford; S Lindquist
Journal: Nature Date: 1998-11-26 Impact factor: 49.962

4. High-throughput mapping of a dynamic signaling network in mammalian cells.

Authors: Miriam Barrios-Rodiles; Kevin R Brown; Barish Ozdamar; Rohit Bose; Zhong Liu; Robert S Donovan; Fukiko Shinjo; Yongmei Liu; Joanna Dembowy; Ian W Taylor; Valbona Luga; Natasa Przulj; Mark Robinson; Harukazu Suzuki; Yoshihide Hayashizaki; Igor Jurisica; Jeffrey L Wrana
Journal: Science Date: 2005-03-11 Impact factor: 47.728

10. Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation.

Authors: L Whitesell; E G Mimnaugh; B De Costa; C E Myers; L M Neckers
Journal: Proc Natl Acad Sci U S A Date: 1994-08-30 Impact factor: 11.205

Molecular biology: Choose your protein partners.

1. Structure of an Hsp90-Cdc37-Cdk4 complex.

2. Activated B-RAF is an Hsp90 client protein that is targeted by the anticancer drug 17-allylamino-17-demethoxygeldanamycin.

3. Hsp90 as a capacitor for morphological evolution.

4. High-throughput mapping of a dynamic signaling network in mammalian cells.

5. Quantitative analysis of HSP90-client interactions reveals principles of substrate recognition.

Review 6. Approaches for defining the Hsp90-dependent proteome.

Review 7. Altered Hsp90 function in cancer: a unique therapeutic opportunity.

8. A systematic interaction map of validated kinase inhibitors with Ser/Thr kinases.

9. Hsp90 recognizes a common surface on client kinases.

10. Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation.