Consulta: creatorFacets:"Wang,Lin"
Registros recuperados: 2
Data/hora: 10/06/2024 04:38:53

Impact of simulated acid rain on soil microbial community function in Masson pine seedlings
Provedor de dados: 69
Autores: Wang,Lin; Chen,Zhan; Shang,He; Wang,Jing; Zhang,Peng-yan.
Background Accompanying its rapid economic development and population growth, China is the world's third largest acid rain region, following Europe and North America. The effects of acid rain on forest ecosystem were widely researched, including the growth, the nutrient of the leaf and soil, and so on. However, there are few reports about the effects of acid rain on the soil microbial diversity. This study investigated the effects of acid rain on soil microbial community function under potted Masson pine seedlings (Pinus massoniana Lamb). Results After 7 months of treatment with simulated acid rain, the low acid load treatment (pH 5.5) stimulated soil microbial activity, and increased soil microbial diversity and richness, while the higher levels of acid...
Tipo: Journal article
Palavras-chave: Biolog; Metabolic capability; Soil microbial activity; Soil microbial diversity and richness.
Ano: 2014
URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582014000500002

TNNI3K is a novel mediator of myofilament function and phosphorylates cardiac troponin I
Provedor de dados: 56
Autores: Wang,Hui; Wang,Lin; Song,Li; Zhang,Yan-Wan; Ye,Jue; Xu,Rui-Xia; Shi,Na; Meng,Xian-Min.
The phosphorylation of cardiac troponin I (cTnI) plays an important role in the contractile dysfunction associated with heart failure. Human cardiac troponin I-interacting kinase (TNNI3K) is a novel cardiac-specific functional kinase that can bind to cTnI in a yeast two-hybrid screen. The purpose of this study was to investigate whether TNNI3K can phosphorylate cTnI at specific sites and to examine whether the phosphorylation of cTnI caused by TNNI3K can regulate cardiac myofilament contractile function. Co-immunoprecipitation was performed to confirm that TNNI3K could interact with cTnI. Kinase assays further indicated that TNNI3K did not phosphorylate cTnI at Ser23/24 and Ser44, but directly phosphorylated Ser43 and Thr143 in vitro. The results obtained...
Tipo: Info:eu-repo/semantics/article
Palavras-chave: TNNI3K; CTnI; Phosphorylation; Contraction function.
Ano: 2013
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2013000200128