Zobrazeno 1 - 10
of 35
pro vyhledávání: '"Xinzhi Lu"'
Autor:
Cuifang Han, Yuchao Gu, Hui Shan, Wenyi Mi, Jiahui Sun, Minghui Shi, Xinling Zhang, Xinzhi Lu, Feng Han, Qianhong Gong, Wengong Yu
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-12 (2017)
SIRT1 is a stress sensor whose deacetylase activity is increased during cellular stress, but the molecular mechanism is unclear. Here, the authors show that O-GlcNAcylation of SIRT1 is elevated upon different stress stimuli and increases SIRT1 deacet
Externí odkaz:
https://doaj.org/article/e0611664b7764e24b6f08b4487935b48
Publikováno v:
PLoS ONE, Vol 6, Iss 4, p e18514 (2011)
Bacterial exopolysaccharides have always been suggested to play crucial roles in the bacterial initial adhesion and the development of complex architecture in the later stages of bacterial biofilm formation. However, Escherichia coli group II capsula
Externí odkaz:
https://doaj.org/article/1d70866a74d946209d5e2c2258abd7b1
Autor:
Wengong Yu, Xinzhi Lu, Feng Han, Jing Yang, Cuifang Han, Qiong Fan, Haiyan Liu, Yuqing Ge, Wenyi Mi, Yuchao Gu
GlcNAcylation, a dynamic posttranslational modification, is involved in a wide range of biological processes and some human diseases. Although there is emerging evidence that some tumor-associated proteins are modified by GlcNAcylation, the role of G
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bea6d2050c4892653f0adae7045ee509
https://doi.org/10.1158/0008-5472.c.6500336
https://doi.org/10.1158/0008-5472.c.6500336
Autor:
Wengong Yu, Xinzhi Lu, Feng Han, Jing Yang, Cuifang Han, Qiong Fan, Haiyan Liu, Yuqing Ge, Wenyi Mi, Yuchao Gu
Supplementary Methods, Figures 1-10 from GlcNAcylation Plays an Essential Role in Breast Cancer Metastasis
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::65e3b1ecb88c86bc2e8fbb53363c29f4
https://doi.org/10.1158/0008-5472.22382852.v1
https://doi.org/10.1158/0008-5472.22382852.v1
Publikováno v:
International journal of biological macromolecules. 194
A new α-agarase AgaE belonging to glycoside hydrolase (GH) family 96 was identified and cloned from marine bacterium Thalassomonas sp. LD5. AgaE consists of 926 amino acids with a theoretical molecular mass of 97 kDa. The optimum temperature and pH
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aae3fa046b2157f0a7fc06fed6247850
https://pubmed.ncbi.nlm.nih.gov/34863832
https://pubmed.ncbi.nlm.nih.gov/34863832
Publikováno v:
International Journal of Biological Macromolecules. 109:880-887
CsnA, a chitosanase from Renibacterium sp. QD1, has great potential for industrial applications due to its high yield and broad pH stability. In this study, a specific Glu160 in CsnA was identified by sequence alignment, and structural analysis and M
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e84a531dd3fb0d8f991e2b10f2aeed8b
https://doi.org/10.1016/j.ijbiomac.2017.11.071
https://doi.org/10.1016/j.ijbiomac.2017.11.071
Publikováno v:
Applied Microbiology and Biotechnology. 102:2203-2212
It has been a long time since the first α-agarase was discovered. However, only two α-agarases have been cloned and partially characterized so far and the study of α-agarases has lagged far behind that of β-agarases. Here, we report an α-agarase
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ed372f985b631c2bc9b8d7ba043a8c58
https://doi.org/10.1007/s00253-018-8762-6
https://doi.org/10.1007/s00253-018-8762-6
Publikováno v:
Biotechnology Letters. 40:75-82
To determine the effects of the extra N-terminal seven-amino-acid sequence on the function of chitosanase CsnA.Sequence and structure analysis indicated that the mature CsnA contains a seven-amino-acid extension in a disordered form at the N-terminus
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2038828a17ff3949ddbae6cb72ee409a
https://doi.org/10.1007/s10529-017-2436-9
https://doi.org/10.1007/s10529-017-2436-9
Publikováno v:
Biotechnology letters. 42(10)
To characterize the hydrolysis product and the substrate binding in the catalytic cavity of α-agarase AgaD. The time course curve showed that AgaD degraded agarose by the endo-type cleavage. AgaD did not degrade agarobiose (A2) and agarotetraose (A4
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7e2929924ae92cad6d4da0c353cd527b
https://pubmed.ncbi.nlm.nih.gov/32399660
https://pubmed.ncbi.nlm.nih.gov/32399660
Publikováno v:
Biotechnology letters. 40(1)
In Table 1 as published, some of the data were wrong. The corrected Table 1 is shown here. In addition, according to the corrected Table 1, the sentence “the k cat /K m of CsnA-CBM5 was higher than that of WT by 143%” in the part of “The kineti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b2c335e4904207c2e96083a3bf0302dc
https://pubmed.ncbi.nlm.nih.gov/28748352
https://pubmed.ncbi.nlm.nih.gov/28748352