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Front Cover: Characterizations of HSP90‐Interacting Complex in Renal Cells Using Tandem Affinity Purification and Its Potential Role in Kidney Stone Formation
Author(s) -
Manissorn Juthatip,
Singhto Nilubon,
Thongboonkerd Visith
Publication year - 2018
Publication title -
proteomics
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.201870211
Subject(s) - hsp90 , chemistry , heat shock protein , tandem , chaperone (clinical) , gene knockdown , intracellular , tandem mass spectrometry , proteomics , microbiology and biotechnology , computational biology , biochemistry , biology , mass spectrometry , chromatography , materials science , medicine , apoptosis , pathology , composite material , gene
DOI: 10.1002/pmic.201800004 Heat shock protein 90 (HSP90) is a highly abundant molecular chaperone that interacts with many other intracellular proteins to regulate various cellular functions. In article number 1800004 , Manissorn et al. characterize HSP90‐interacting complex in human renal cells under normal physiologic state using tandem affinity purification (TAP) followed by protein identification with an ultrahigh‐resolution tandem mass spectrometer (Qq‐TOF MS/MS). In addition, its role in kidney stone formation has been demonstrated by HSP90 knockdown using small‐interfering RNA. Art designer: Supatcha Sassanarakkit.