Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Chiao-I Kuo"'
Autor:
Shanshan Li, Kan-Yen Hsieh, Chiao-I Kuo, Tzu-Chi Lin, Szu-Hui Lee, Yi-Ru Chen, Chun-Hsiung Wang, Meng-Ru Ho, See-Yeun Ting, Kaiming Zhang, Chung-I Chang
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-13 (2023)
Abstract Many AAA+ (ATPases associated with diverse cellular activities) proteins function as protein or DNA remodelers by threading the substrate through the central pore of their hexameric assemblies. In this ATP-dependent translocating state, the
Externí odkaz:
https://doaj.org/article/9bf22aa7817641b7b47e58b76cb20d3a
Autor:
Hsiu-Jung Wang, Víctor M. Hernández-Rocamora, Chiao-I Kuo, Kan-Yen Hsieh, Szu-Hui Lee, Meng-Ru Ho, Zhijay Tu, Waldemar Vollmer, Chung-I Chang
Publikováno v:
mBio, Vol 14, Iss 5 (2023)
ABSTRACT The peptidoglycan layer is a defining characteristic of bacterial cells, providing them with structural support and osmotic protection. In Escherichia coli, this layer is linked to the outer membrane via the abundant membrane-anchored protei
Externí odkaz:
https://doaj.org/article/df3b6d1848904fbabacc81e1cbda67b5
Autor:
Meng-Sheng Lee, Kan-Yen Hsieh, Chiao-I Kuo, Szu-Hui Lee, Shambhavi Garde, Manjula Reddy, Chung-I Chang
Publikováno v:
mBio, Vol 13, Iss 1 (2022)
ABSTRACT Bacterial cells are encased in peptidoglycan (PG), a polymer of disaccharide N-acetylglucosamine (GlcNAc) and N-acetyl-muramic acid (MurNAc) cross-linked by peptide stems. PG is synthesized in the cytoplasm as UDP-MurNAc-peptide precursors,
Externí odkaz:
https://doaj.org/article/8d883f309da74cdebb1340beb11cca16
Publikováno v:
PLoS ONE, Vol 8, Iss 7, p e67843 (2013)
NLRPs (Nucleotide-binding domain, leucine-rich repeat and pyrin domain containing proteins) are a family of pattern-recognition receptors (PRRs) that sense intracellular microbial components and endogenous stress signals. NLRP10 (also known as PYNOD)
Externí odkaz:
https://doaj.org/article/a92e303225c14c8d8c1fcbdb3e3dca20
Autor:
Jiahn-Haur Liao, Chiao-I Kuo, Ya-Yi Huang, Yu-Ching Lin, Yen-Chen Lin, Chen-Yui Yang, Wan-Ling Wu, Wei-Hau Chang, Yen-Chywan Liaw, Li-Hua Lin, Chung-I Chang, Shih-Hsiung Wu
Publikováno v:
PLoS ONE, Vol 7, Iss 7, p e40226 (2012)
Lon proteases are a family of ATP-dependent proteases involved in protein quality control, with a unique proteolytic domain and an AAA(+) (ATPases associated with various cellular activities) module accommodated within a single polypeptide chain. The
Externí odkaz:
https://doaj.org/article/c97fd7ebd4824fb5b03f9a06883e0c86
Bacterial cells are encased in peptidoglycan (PG), a polymer of disaccharide N-acetyl-glucosamine (GlcNAc) and N-acetyl-muramic acid (MurNAc) cross-linked by peptide stems. PG is synthesized in the cytoplasm as UDP-MurNAc-peptide precursors, of which
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1e6caedc8002d9da0a4f949d79aecbb3
https://doi.org/10.1101/2021.12.07.471703
https://doi.org/10.1101/2021.12.07.471703
Autor:
Kai-Fa Huang, Shih-Chieh Su, Shanshan Li, Chung-I Chang, Chiao-I Kuo, Kaiming Zhang, Kan-Yen Hsieh
Publikováno v:
Science Advances
Description
One-way translocation and processive cleavage of substrate polypeptide occur in each of the Lon proteolytic active sites.
The Lon protease is the prototype of a family of proteolytic machines with adenosine triphosphatase module
One-way translocation and processive cleavage of substrate polypeptide occur in each of the Lon proteolytic active sites.
The Lon protease is the prototype of a family of proteolytic machines with adenosine triphosphatase module
Autor:
Shanshan Li, Chung-I Chang, Grigore D. Pintilie, Kan-Yen Hsieh, Chiao-I Kuo, Kaiming Zhang, Szu-Hui Lee
Publikováno v:
Science Advances
Description
Full-length structures of the Lon protease complex reveal a tensegrity helix triangle for substrate selection and unfolding.
Lon is an evolutionarily conserved proteolytic machine carrying out a wide spectrum of biological activ
Full-length structures of the Lon protease complex reveal a tensegrity helix triangle for substrate selection and unfolding.
Lon is an evolutionarily conserved proteolytic machine carrying out a wide spectrum of biological activ
Autor:
Kentaro Ihara, Soichi Wakatsuki, Shih-Hsiung Wu, Kai-Fa Huang, Chung-I Chang, Jiahn-Haur Liao, Chiao-I Kuo
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 69:1395-1402
The Lon proteases are a unique family of chambered proteases with a built-in AAA+ (ATPases associated with diverse cellular activities) module. Here, crystal structures of a unique member of the Lon family with no intrinsic ATPase activity in the pro
Publikováno v:
PLoS ONE
PLoS ONE, Vol 8, Iss 7, p e67843 (2013)
PLoS ONE, Vol 8, Iss 7, p e67843 (2013)
NLRPs (Nucleotide-binding domain, leucine-rich repeat and pyrin domain containing proteins) are a family of pattern-recognition receptors (PRRs) that sense intracellular microbial components and endogenous stress signals. NLRP10 (also known as PYNOD)