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Wyszukujesz frazę "Li, Min" wg kryterium: Autor


Wyświetlanie 1-4 z 4
Tytuł:
High-grade mutant OmpF induces decreased bacterial survival rate
Autorzy:
Zhao, Zhi-ping
Liu, Ting-ting
Zhang, Li
Luo, Min
Nie, Xin
Li, Zai-xin
Pan, Yu
Powiązania:
https://bibliotekanauki.pl/articles/1039304.pdf
Data publikacji:
2014
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
antibiotic resistance
mOmpF
OmpF
outer membrane protein
bacterial survival rate
Opis:
OmpF plays very important roles in the influx of antibiotics and bacterial survival in the presence of antibiotics. However, high-grade mutant OmpF and its function in decreasing bacterial survival rate have not been reported to date. In the present study, we cloned a high-grade mutant OmpF (mOmpF) and sequence analysis suggested that over 45 percent of the DNA sequence was significantly mutated, leading to dramatic changes in over 55 percent of the amino acid sequence. mOmpF protein was successfully expressed. When grown in the presence of antibiotic, the bacterial survival rate decreased and the antibiotic inhibition zone became larger with the increase of the mOmpF. It was concluded that concentration of high-grade mutant mOmpF dramatically influenced the bacterial survival rate. The study presented here may provide insights into better understanding of the relationships between structure and function of OmpF.
Źródło:
Acta Biochimica Polonica; 2014, 61, 2; 369-373
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Amino acid substitutions of His296 alter the catalytic properties of Zymomonas mobilis 10232 levansucrase
Autorzy:
Li, Shu
Chen, Ming
Li, Gang
Yan, Yong
Yu, Hai
Zhan, Yu
Peng, Zi
Wang, Jin
Lin, Min
Powiązania:
https://bibliotekanauki.pl/articles/1040841.pdf
Data publikacji:
2008
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
Zymomonas mobilis
His296
levansucrase
levan
transfructosylation activity
hydrolysis activity
Opis:
His296 of Zymomonas mobilis levansucrase (EC 2.4.1.10) is crucial for the catalysis of the transfructosylation reaction. The three-dimensional structures of levansucrases revealed the His296 is involved in the substrate recognition and binding. In this study, nine mutants were created by site-directed mutagenesis, in which His296 was substituted with amino acids of different polarity, charge and length. The substitutions of His296 with Arg or Trp retained partial hydrolysis and transfructosylation activities. The positively charged Lys substitution resulted in a 2.5-fold increase of sucrose hydrolysis. Substitutions with short (Cys or Ser), negatively charged (Glu) or polar (Tyr) amino acids virtually abolished both the activities. Analysis of transfructosylation products indicated that the mutants synthesized different oligosaccharides, suggesting that amino acid substitutions of His296 strongly affected both the enzyme activity and transfructosylation products.
Źródło:
Acta Biochimica Polonica; 2008, 55, 1; 201-206
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Two Gln187 mutants of human soluble APRIL inhibit proliferation of lung carcinoma A549 cells
Autorzy:
Dai, Shuangshuang
Zheng, Yingru
Chen, Bin
Gao, Min
Zhang, Yan
Zhang, Li
Gong, Wei
He, Fengtain
Powiązania:
https://bibliotekanauki.pl/articles/1040492.pdf
Data publikacji:
2009
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
APRIL
Gln187 mutant of sAPRIL
anti-tumor activity
Opis:
Soluble APRIL (sAPRIL), the active form of a proliferation-inducing ligand (APRIL), is implicated in the proliferation of tumor cells. Suppressing APRIL function has been considered as a potential strategy for the therapy of APRIL-associated tumors. In the present study, we generated human sAPRIL and its two mutants, Gln187-D-sAPRIL (Gln187 deleted) and Gly187-sAPRIL (Gln187 replaced by Gly). In vitro experiments showed that the two mutants had similar specific binding capacity to lung carcinoma A549 cells compared to the wild-type sAPRIL, and both, especially Gly187-sAPRIL, exhibited significant antagonistic effect on sAPRIL-induced tumor cell proliferation in a dose-dependent manner, which might be predominantly mediated by blocking sAPRIL-induced MEK and ERK phosphorylation but not p38MAPK or JNK signaling. In vivo experiments with nude mice bearing A549 cell-derived xenograft tumor showed that only the Gly187-sAPRIL mutant could significantly suppress the tumor growth. These results suggest that Gln187 may be a crucial amino acid in APRIL-mediated tumor cell proliferation via the MEK-ERK signaling pathway and that the sAPRIL mutants may serve as novel potential antagonists of APRIL for the therapy of APRIL-associated cancers.
Źródło:
Acta Biochimica Polonica; 2009, 56, 4; 703-710
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Genomics and the evolution of aminoacyl-tRNA synthesis.
Autorzy:
Ruan, Benfang
Ahel, Ivan
Ambrogelly, Alex
Becker, Hubert
Bunjun, Shipra
Feng, Liang
Tumbula-Hansen, Debra
Ibba, Michael
Korencic, Dragana
Kobayashi, Hiroyuki
Jacquin-Becker, Clarisse
Mejlhede, Nina
Min, Bokkee
Raczniak, Gregory
Rinehart, Jesse
Stathopoulos, Constantinos
Li, Tong
Söll, Dieter
Powiązania:
https://bibliotekanauki.pl/articles/1044116.pdf
Data publikacji:
2001
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
evolution
tRNA
aminoacyl-tRNA
translation
protein synthesis
Opis:
Translation is the process by which ribosomes direct protein synthesis using the genetic information contained in messenger RNA (mRNA). Transfer RNAs (tRNAs) are charged with an amino acid and brought to the ribosome, where they are paired with the corresponding trinucleotide codon in mRNA. The amino acid is attached to the nascent polypeptide and the ribosome moves on to the next codon. Thus, the sequential pairing of codons in mRNA with tRNA anticodons determines the order of amino acids in a protein. It is therefore imperative for accurate translation that tRNAs are only coupled to amino acids corresponding to the RNA anticodon. This is mostly, but not exclusively, achieved by the direct attachment of the appropriate amino acid to the 3'-end of the corresponding tRNA by the aminoacyl-tRNA synthetases. To ensure the accurate translation of genetic information, the aminoacyl-tRNA synthetases must display an extremely high level of substrate specificity. Despite this highly conserved function, recent studies arising from the analysis of whole genomes have shown a significant degree of evolutionary diversity in aminoacyl-tRNA synthesis. For example, non-canonical routes have been identified for the synthesis of Asn-tRNA, Cys-tRNA, Gln-tRNA and Lys-tRNA. Characterization of non-canonical aminoacyl-tRNA synthesis has revealed an unexpected level of evolutionary divergence and has also provided new insights into the possible precursors of contemporary aminoacyl-tRNA synthetases.
Źródło:
Acta Biochimica Polonica; 2001, 48, 2; 313-321
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-4 z 4

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