(Q28290854)

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Hsp90 as a capacitor for morphological evolution

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Hsp90 as a capacitor for morphological evolution (English)

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author name string

S L Rutherford

1

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S Lindquist

2

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publication date

26 November 1998

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396

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336-42

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6709

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In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone

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Protein folding and the regulation of signaling pathways

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Mutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase

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Transient interaction of Hsp90 with early unfolding intermediates of citrate synthase. Implications for heat shock in vivo

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The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding

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Reduced levels of hsp90 compromise steroid receptor action in vivo

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A role for Hsp90 in retinoid receptor signal transduction

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Mammalian p50Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4

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Heat-shock protein hsp90 governs the activity of pp60v-src kinase

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HSP90 interacts with and regulates the activity of heat shock factor 1 in Xenopus oocytes

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Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1

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Mutations in Hsp83 and cdc37 impair signaling by the sevenless receptor tyrosine kinase in Drosophila.

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The heat shock protein 83 (Hsp83) is required for Raf-mediated signalling in Drosophila

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

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CANALIZATION OF DEVELOPMENT AND THE INHERITANCE OF ACQUIRED CHARACTERS

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Coevolution of functionally constrained characters: prerequisites for adaptive versatility

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Naturally occurring genetic variation affects Drosophila photoreceptor determination.

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Effect of polymorphism in the Drosophila regulatory gene Ultrabithorax on homeotic stability.

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Ras1 and a putative guanine nucleotide exchange factor perform crucial steps in signaling by the sevenless protein tyrosine kinase.

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A role for Hsp90 in cell cycle control: Wee1 tyrosine kinase activity requires interaction with Hsp90.

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Consolidated OpenCitations Corpus – April 2017

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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Consolidated OpenCitations Corpus – April 2017

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