Structural insights into a secretory abundant heat-soluble protein from an anhydrobiotic tardigrade, Ramazzottius varieornatus-Reference-Cited by-同舟云学术

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Structural insights into a secretory abundant heat-soluble protein from an anhydrobiotic tardigrade, Ramazzottius varieornatus

Published:2017-08 Issue:16 Volume:591 Page:2458-2469
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:FEBS Lett

Author:

Fukuda Yohta¹,Miura Yoshimasa¹,Mizohata Eiichi¹,Inoue Tsuyoshi¹

Affiliation:

1. Department of Applied Chemistry; Graduate School of Engineering; Osaka University; Suita Osaka Japan

Funder

Japan Society for the Promotion of Science

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Reference67 articles.

1. The problem of anabiosis or latent life: history and current concept;Keilin;Proc R Soc Lon B,1959

2. Survival in extreme environments - on the current knowledge of adaptations in tardigrades;Mobjerg;Acta Physiol (Oxf),2011

3. On dormancy strategies in tardigrades;Guidetti;J Insect Physiol,2011

4. Establishment of a rearing system of the extremotolerant tardigrade Ramazzottius varieornatus: a new model animal for astrobiology;Horikawa;Astrobiology,2008

5. The physiology of cryptobiosis in tardigrades;Crowe;Mem 1st Ital Idrobiol,1975

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1. Structural adaptability and surface activity of peptides derived from tardigrade proteins;Protein Science;2024-08-16

2. Tardigrade secretory proteins protect biological structures from desiccation;Communications Biology;2024-05-25

3. The tardigrade-derived mitochondrial abundant heat soluble protein improves adipose-derived stem cell survival against representative stressors;Scientific Reports;2024-05-23

4. The major inducible small heat shock protein HSP20-3 in the tardigrade Ramazzottius varieornatus forms filament-like structures and is an active chaperone;Cell Stress and Chaperones;2024-02

5. Helicity of a tardigrade disordered protein contributes to its protective function during desiccation;Protein Science;2024-01-23

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