2007
DOI: 10.1016/j.ijbiomac.2007.06.003
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Towards creatine kinase aggregation due to the cysteine modification at the flexible active site and refolding pathway

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Cited by 4 publications
(2 citation statements)
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“…This difference may arise due to the separate inactivation mechanisms. The parameters summarized in Table were consistent with those of CK from other studies [25]. CK possesses four cysteine residues and only one of them is believed to be essential for catalytic activity, where the other three are thought to be involved in CK folding [25][26][27].…”
Section: Resultssupporting
confidence: 86%
See 1 more Smart Citation
“…This difference may arise due to the separate inactivation mechanisms. The parameters summarized in Table were consistent with those of CK from other studies [25]. CK possesses four cysteine residues and only one of them is believed to be essential for catalytic activity, where the other three are thought to be involved in CK folding [25][26][27].…”
Section: Resultssupporting
confidence: 86%
“…The parameters summarized in Table were consistent with those of CK from other studies [25]. CK possesses four cysteine residues and only one of them is believed to be essential for catalytic activity, where the other three are thought to be involved in CK folding [25][26][27]. According to [2] muscle isoform of CK could retain its activity at temperatures below 50 °C and being completely in-activated after heat treatment at temperatures above 62 °C [28,29].…”
Section: Resultssupporting
confidence: 84%