Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
Short sequence-paperHspB3, the most deviating of the six known human small heat shock proteins1
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Cited by (49)
The potential role of heat shock protein 27 in cardiovascular disease
2012, Clinica Chimica ActaCharacterization of O-phosphohydroxyproline in rat α-crystallin A
2010, Journal of Biological ChemistryCitation Excerpt :The αAins-crystallin is therefore 196 amino acids long (21). The sequence similarity of α-crystallins to small heat shock proteins has led to the establishment of the α-crystallin family of small heat shock proteins (sHsps), which share the α-crystallin domain (28–30). The α-crystallin domain is the primary sequence of the protein in the C-terminal half of the sHsps (31, 32).
The Small Heat-Shock Proteins HSPB2 and HSPB3 Form Well-defined Heterooligomers in a Unique 3 to 1 Subunit Ratio
2009, Journal of Molecular BiologyInteractions of HSP22 (HSPB8) with HSP20, αb-crystallin, and HSPB3
2005, Biochemical and Biophysical Research CommunicationsCitation Excerpt :There may be several possible explanations for the discrepancy between the YTH and FRET results. HSPB3 has been suggested to be the most deviating member of the mammalian sHSP superfamily [20], while HSP20 and αB-crystallin (and HSP27) are phylogenetically the closest to HSP22 [1]. Also, a conserved N-terminal motif (WD/EPF) of HSP27, that is not present in HSPB3, may mediate important intramolecular interactions with hydrophobic surfaces of the α-crystallin domain of the protein [3,21].
- 1
The nucleotide sequence data of HspB3 have been submitted to the EMBL/GenBank databases under accession No. Y17782.