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Title:           Hsp90 S-nitrosylation at Cys521, as a conformational switch, modulates cycling of Hsp90-AHA1-CDC37 chaperone machine to aggravate atherosclerosis
Subject:         Redox Biology, 52 (2022) 102290. doi:10.1016/j.redox.2022.102290
Keywords:        Heat shock protein 90,S-nitrosylation,Atherosclerosis,Oxidative stress,Endothelial dysfunction
Author:          Shuang Zhao
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      Title: Hsp90 ​S-nitrosylation at Cys521, as a conformational switch, modulates cycling of Hsp90-AHA1-CDC37 chaperone machine to ag ...
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        Title: 1 Introduction
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        Title: 2 Materials and methods
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          Title: 2.1 Experimental animals
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          Title: 2.2 Human artery specimens
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          Title: 2.3 Cell culture and treatment
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          Title: 2.4 Plasmid transfection
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          Title: 2.5 Biotin switch assay
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          Title: 2.6 Mass spectrometry for S-nitrosylated proteins identification
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          Title: 2.7 RNA-sequence analysis
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          Title: 2.8 Proximity Ligation Assay (PLA)
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          Title: 2.9 En face analysis of atherosclerosis and plaque histology
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          Title: 2.10 Assessment of endothelium-dependent relaxation
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          Title: 2.11 Monocyte adhesion assay
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          Title: 2.12 Monocyte transmigration assay
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          Title: 2.13 Measurement of cyclic GMP (cGMP) level
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          Title: 2.17 Detection of malondialdehyde (MDA) level
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          Title: 2.18 Western blotting
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          Title: 2.19 Coimmunoprecipitation
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          Title: 2.20 Real-time quantitative PCR (qPCR) analysis
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        Title: 3 Results
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          Title: 3.1 SNO-Hsp90 is elevated in atherosclerotic aortas and oxLDL-treated ECs
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          Title: 3.2 iNOS contributes to the S-nitrosylation of Hsp90 at Cys521
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          Title: 3.3 SNO-Hsp90 at Cys521 reduces endothelial NO bioavailability via Hsp90/AHA1/eNOS pathway
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          Title: 3.4 SNO-Hsp90 at Cys521 induces endothelial adhesion, inflammation and oxidative stress via Hsp90/CDC37/NF-κB signaling
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          Title: 3.5 Inhibition of SNO-Hsp90 by Cys521 mutation alleviates atherosclerosis in ApoE-/- mice
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        Title: Author contributions
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        Title: Declaration of competing interest
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        Title: Acknowledgements
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        Title: Appendix A Supplementary data
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    Title: Hsp90 S-nitrosylation at Cys521, as a conformational switch, modulates cycling of Hsp90-AHA1-CDC37 chaperone machine to aggravate atherosclerosis
    Author: Shuang Zhao
    Subject: Redox Biology, 52 (2022) 102290. doi:10.1016/j.redox.2022.102290
    Keywords: Heat shock protein 90,S-nitrosylation,Atherosclerosis,Oxidative stress,Endothelial dysfunction
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       Subtype: Link
       Rect: 323, 254, 555, 260
       Flags: Print
      Annotation: 
       Subtype: Link
       Rect: 323, 246, 396, 252
       Flags: Print
      Annotation: 
       Subtype: Link
       Rect: 323, 238, 545, 244
       Flags: Print
      Annotation: 
       Subtype: Link
       Rect: 323, 230, 552, 236
       Flags: Print
      Annotation: 
       Subtype: Link
       Rect: 323, 222, 347, 228
       Flags: Print
  Checksum: c5706855
   Type: CRC32
  Checksum: 97e5c4b2c604a3ef010ba59092a24668
   Type: MD5
  Checksum: 025efaf345d2fe56fd41fec49f5acaa7c9da0a44
   Type: SHA-1
  Checksum: f4939c6b6368209115c0acd2d9d41ad3dfef70d4304cacd070e3b62e95ea9841
   Type: SHA-256