Robert Matts to Protein Folding
This is a "connection" page, showing publications Robert Matts has written about Protein Folding.
Connection Strength
0.905
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Modular folding and evidence for phosphorylation-induced stabilization of an hsp90-dependent kinase. J Biol Chem. 1998 Apr 03; 273(14):8475-82.
Score: 0.153
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Hsp90 is obligatory for the heme-regulated eIF-2alpha kinase to acquire and maintain an activable conformation. J Biol Chem. 1997 Apr 25; 272(17):11648-56.
Score: 0.143
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ATP-dependent chaperoning activity of reticulocyte lysate. J Biol Chem. 1994 Apr 01; 269(13):9493-9.
Score: 0.116
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High-throughput assay for the identification of Hsp90 inhibitors based on Hsp90-dependent refolding of firefly luciferase. Bioorg Med Chem. 2007 Mar 01; 15(5):1939-46.
Score: 0.070
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Novobiocin induces a distinct conformation of Hsp90 and alters Hsp90-cochaperone-client interactions. Biochemistry. 2004 Jun 29; 43(25):8217-29.
Score: 0.059
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Phosphorylation of serine 13 is required for the proper function of the Hsp90 co-chaperone, Cdc37. J Biol Chem. 2003 Oct 03; 278(40):38117-20.
Score: 0.055
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Differential inhibition of Hsc70 activities by two Hsc70-binding peptides. Biochemistry. 2002 Mar 19; 41(11):3742-53.
Score: 0.050
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p50(cdc37) is a nonexclusive Hsp90 cohort which participates intimately in Hsp90-mediated folding of immature kinase molecules. Biochemistry. 2000 Jun 27; 39(25):7631-44.
Score: 0.045
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Dual role for Hsc70 in the biogenesis and regulation of the heme-regulated kinase of the alpha subunit of eukaryotic translation initiation factor 2. Mol Cell Biol. 1999 Sep; 19(9):5861-71.
Score: 0.042
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Molybdate inhibits hsp90, induces structural changes in its C-terminal domain, and alters its interactions with substrates. Biochemistry. 1999 Mar 23; 38(12):3837-49.
Score: 0.041
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Luciferase renaturation assays of chaperones and chaperone antagonists. Methods Mol Biol. 1998; 102:129-41.
Score: 0.038
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Hsp90-mediated folding of the lymphoid cell kinase p56lck. Biochemistry. 1996 Oct 15; 35(41):13451-9.
Score: 0.035
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The anticancer drug AUY922 generates a proteomics fingerprint that is highly conserved among structurally diverse Hsp90 inhibitors. J Proteome Res. 2013 Aug 02; 12(8):3697-706.
Score: 0.027
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Derrubone, an inhibitor of the Hsp90 protein folding machinery. J Nat Prod. 2007 Dec; 70(12):2014-8.
Score: 0.019
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The molecular chaperone Hsp90 is required for signal transduction by wild-type Hck and maintenance of its constitutively active counterpart. Cell Growth Differ. 2001 Aug; 12(8):409-17.
Score: 0.012