To study the resistance mechanism of clinical isolates of Ureaplasma urealyticum resistant to fluoroquinolones Methods Thirteen isolates of Ureaplasma urealyticum resistant to six fluoroquinolones were selected out ...To study the resistance mechanism of clinical isolates of Ureaplasma urealyticum resistant to fluoroquinolones Methods Thirteen isolates of Ureaplasma urealyticum resistant to six fluoroquinolones were selected out of 184 clinical isolates and their QRDRs (quinolone resistance determining region) gyrA, gyrB, parC and parE were amplified by PCR Sequencing results were compared to those susceptible reference strains and a comparison of deduced amino acid sequences were performed Results Sequence comparison revealed a C to A change at 87nt of gyrA QRDR leading to the substitution of Asp95 with glutamic acid and a C to T change at 50nt of parC QRDR leading to the substitution of Ser80 with leucine Conclusion These results suggest that a C to A change at 87nt of gyrA QRDR and a C to T change at 50nt of parC QRDR are associated with fluoroquinolone resistance of Ureaplasma urealyticum展开更多
Severe acute respiratory syndrome coronavirus 2(SARS-CoV-2)has spread rapidly throughout the world.SARS-CoV-2 is an enveloped,plus-stranded RNA virus with a single-stranded RNA genome of approximately 30,000 nucleotid...Severe acute respiratory syndrome coronavirus 2(SARS-CoV-2)has spread rapidly throughout the world.SARS-CoV-2 is an enveloped,plus-stranded RNA virus with a single-stranded RNA genome of approximately 30,000 nucleotides.The SARS-CoV-2 genome encodes 29 proteins,including 16 nonstructural,4 structural and 9 accessory proteins.To date,over 1,228 experimental structures of SARS-CoV-2 proteins have been deposited in the Protein Data Bank(PDB),including 16 protein structures,two functional domain structures of nucleocapsid(N)protein,and scores of complexes.Overall,they exhibit high similarity to SARS-CoV proteins.Here,we summarize the progress of structural and functional research on SARS-CoV-2 proteins.These studies provide structural and functional insights into proteins of SARS-CoV-2,and further elucidate the daedal relationship between different components at the atomic level in the viral life cycle,including attachment to the host cell,viral genome replication and transcription,genome packaging and assembly,and virus release.It is important to understand the structural and functional properties of SARS-CoV-2 proteins as it will facilitate the development of anti-CoV drugs and vaccines to prevent and control the current SARS-CoV-2 pandemic.展开更多
Sirtuins(SIRTs) are nicotinamide adenine dinucleotide(NAD^+)-dependent protein deacetylases,which regulate important biological processes ranging from apoptosis,age-associated pathophysiologies,adipocyte and muscle di...Sirtuins(SIRTs) are nicotinamide adenine dinucleotide(NAD^+)-dependent protein deacetylases,which regulate important biological processes ranging from apoptosis,age-associated pathophysiologies,adipocyte and muscle differentiation,and energy expenditure to gluconeogenesis.Very recently,sirtuin 5(SIRT5) has received considerable attention due to that it was found to have weak deacetylase activity but strong desuccinylase,demalonylase and deglutarylase activities,and it was also found to be associated with several human diseases such as cancer,Alzheimer's disease,and Parkinson's disease.In this review,we for the first time summarized the structure characteristics,known peptide and small-molecule inhibitors of SIRT5,extracted some clues from current available information and introduced some feasible,practical in silico methods,which might be useful in further efforts to develop new SIRT5 inhibitors.展开更多
基金ThisstudywassupportedbyagrantfromtheEducationCommitteeofHunanProvince (No 0 0A0 0 9)
文摘To study the resistance mechanism of clinical isolates of Ureaplasma urealyticum resistant to fluoroquinolones Methods Thirteen isolates of Ureaplasma urealyticum resistant to six fluoroquinolones were selected out of 184 clinical isolates and their QRDRs (quinolone resistance determining region) gyrA, gyrB, parC and parE were amplified by PCR Sequencing results were compared to those susceptible reference strains and a comparison of deduced amino acid sequences were performed Results Sequence comparison revealed a C to A change at 87nt of gyrA QRDR leading to the substitution of Asp95 with glutamic acid and a C to T change at 50nt of parC QRDR leading to the substitution of Ser80 with leucine Conclusion These results suggest that a C to A change at 87nt of gyrA QRDR and a C to T change at 50nt of parC QRDR are associated with fluoroquinolone resistance of Ureaplasma urealyticum
文摘Severe acute respiratory syndrome coronavirus 2(SARS-CoV-2)has spread rapidly throughout the world.SARS-CoV-2 is an enveloped,plus-stranded RNA virus with a single-stranded RNA genome of approximately 30,000 nucleotides.The SARS-CoV-2 genome encodes 29 proteins,including 16 nonstructural,4 structural and 9 accessory proteins.To date,over 1,228 experimental structures of SARS-CoV-2 proteins have been deposited in the Protein Data Bank(PDB),including 16 protein structures,two functional domain structures of nucleocapsid(N)protein,and scores of complexes.Overall,they exhibit high similarity to SARS-CoV proteins.Here,we summarize the progress of structural and functional research on SARS-CoV-2 proteins.These studies provide structural and functional insights into proteins of SARS-CoV-2,and further elucidate the daedal relationship between different components at the atomic level in the viral life cycle,including attachment to the host cell,viral genome replication and transcription,genome packaging and assembly,and virus release.It is important to understand the structural and functional properties of SARS-CoV-2 proteins as it will facilitate the development of anti-CoV drugs and vaccines to prevent and control the current SARS-CoV-2 pandemic.
基金supported by the Chun hui of Ministry of Education Project(Z2015120)the National Natural Science Foundation of China(81502989)the China Postdoctoral Science Foundation Funded Project(2015M570789)
文摘Sirtuins(SIRTs) are nicotinamide adenine dinucleotide(NAD^+)-dependent protein deacetylases,which regulate important biological processes ranging from apoptosis,age-associated pathophysiologies,adipocyte and muscle differentiation,and energy expenditure to gluconeogenesis.Very recently,sirtuin 5(SIRT5) has received considerable attention due to that it was found to have weak deacetylase activity but strong desuccinylase,demalonylase and deglutarylase activities,and it was also found to be associated with several human diseases such as cancer,Alzheimer's disease,and Parkinson's disease.In this review,we for the first time summarized the structure characteristics,known peptide and small-molecule inhibitors of SIRT5,extracted some clues from current available information and introduced some feasible,practical in silico methods,which might be useful in further efforts to develop new SIRT5 inhibitors.