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Analysis of long-range structural effects induced by DNase-I interaction with actin monomeric form or complexed to CapZ.

Author: AstierC, BenyaminY, BoyerM, KwiatekO, LebartM C, PapaI, RoustanC, UsmanovaA

Journal ArticleAn article published in an academic or professional journal that reports original research or scholarly analysis.
Research Support, Non-U.S. Gov'tResearch funding provided by government agencies outside the United States.

Overview

DNase-I binding to actin induced structural changes that decreased CapZ binding and abolished DNase-I inhibition activity.
Paper Details　
Original Abstract of the Article :
Two fundamental properties of monomeric actin were examined in this study, ie its interaction with DNase-I, and the inhibition of endonuclease activity consecutive to the association of the two molecules. In particular, the topological independence between catalytic site of DNase-I and interface wit...See full text at original site
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引用元：
https://doi.org/10.1016/s0300-9084(97)82740-x

データ提供：米国国立医学図書館（NLM）

DNase-I and Actin: A Delicate Dance of Molecular Interactions

This research delves into the intricate world of [molecular biology] and [protein interactions], exploring the interactions between DNase-I, a [deoxyribonuclease], and actin, a key protein in cell structure and movement. This study found that the binding of DNase-I to actin monomer induces significant conformational changes in actin, affecting its flexibility and the exposure of certain regions.

DNase-I: A Molecular Choreographer of Actin Conformational Changes

This research illuminates the complex interactions between DNase-I and actin. Just as a skilled dancer uses their body to express intricate movements, DNase-I subtly alters the shape of actin, influencing its function.

Implications for Cellular Processes

These findings have important implications for understanding the dynamics of actin and its role in cellular processes. A deeper understanding of these interactions could lead to new insights into various cellular functions, including cell motility and cytoskeletal organization.

Dr. Camel's Conclusion

This study reveals the fascinating interplay between DNase-I and actin, showcasing the delicate balance of molecular interactions. Just as the desert winds sculpt sand dunes, DNase-I subtly shapes the structure of actin, impacting its crucial role in cellular function.

Date :
  1. Date Completed 1998-02-05
  2. Date Revised 2019-08-22
Further Info :

Pubmed ID

9451449

DOI: Digital Object Identifier

10.1016/s0300-9084(97)82740-x

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Languages

English

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