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Article

Actin-inhibition and folding of vertebrate deoxyribonuclease I are affected by mutations at residues 67 and 114.

Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology - 1 Jan 2006

Fujihara Junko, Hieda Yoko, Xue Yuying, Nakagami Norihito, Imamura Shinji, Takayama Koji, Kataoka Kaori, Takeshita Haruo

Abstract excerpt

Amino acid (aa) residues (Val-67 and Ala-114) have been suggested as being mainly responsible for actin-binding in human and bovine deoxyribonucleases I (DNase I). This study presents evidence of these two aa mutational mechanisms, not only for actin-binding but also for folding of DNase I in mammals, reptiles and amphibians. Human and viper snake (Agkistrodon blomhoffii) enzymes are inhibited by actin, whereas...

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PMID: 16311052
DOI: 10.1016/j.cbpb.2005.10.004

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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