Identification and characterization of the Hfq bacterial amyloid region DNA interactions-Reference-Cited by-同舟云学术

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Identification and characterization of the Hfq bacterial amyloid region DNA interactions

Published:2021 Issue: Volume:1 Page:100029
ISSN:2667-1603
Container-title:BBA Advances
language:en
Short-container-title:BBA Advances

Author:

Turbant Florian,Hamoui Omar El,Partouche David,Sandt Christophe,Busi Florent,Wien Frank,Arluison Véronique

Funder

Centre National de la Recherche Scientifique

Commissariat à l'Énergie Atomique et aux Énergies Alternatives

Agence Nationale de la Recherche

Publisher

Elsevier BV

Reference75 articles.

1. DNA-induced partial unfolding of prion protein leads to its polymerisation to amyloid;Nandi;J. Mol. Biol.,2002

2. Amyloid plaques beyond Abeta: a survey of the diverse modulators of amyloid aggregation;Stewart;Biophys. Rev.,2017

3. Pathological implications of nucleic acid interactions with proteins associated with neurodegenerative diseases;Cordeiro;Biophys. Rev.,2014

4. Nuclear translocation uncovers the amyloid peptide Abeta42 as a regulator of gene transcription;Barucker;J. Biol. Chem.,2014

5. Alzheimer amyloid peptide abeta42 regulates gene expression of transcription and growth factors;Barucker;J. Alzheimers Dis.,2015

Cited by 2 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Dynamic action of an intrinsically disordered protein in DNA compaction that induces mycobacterial dormancy;Nucleic Acids Research;2023-12-04

2. Hfq C-terminal region forms a β-rich amyloid-like motif without perturbing the N-terminal Sm-like structure;Communications Biology;2023-10-21

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