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Article ; Online: Expanding our understanding of the role polyprotein conformation plays in the coronavirus life cycle.

Gildenhuys, Samantha

2020 Volume 477, Issue 8, Page(s) 1479–1482

Abstract: Coronavirus are the causative agents in many globally concerning respiratory disease outbreaks such as severe acute respiratory syndrome (SARS), Middle East respiratory syndrome (MERS) and coronavirus disease-2019 (COVID-19). It is therefore important ... ...

Abstract	Coronavirus are the causative agents in many globally concerning respiratory disease outbreaks such as severe acute respiratory syndrome (SARS), Middle East respiratory syndrome (MERS) and coronavirus disease-2019 (COVID-19). It is therefore important that we improve our understanding of how the molecular components of the virus facilitate the viral life cycle. These details will allow for the design of effective interventions. Krichel and coauthors in their article in the Biochemical Journal provide molecular details of how the viral polyprotein (nsp7-10) produced from the positive single stranded RNA genome, is cleaved to form proteins that are part of the replication/transcription complex. The authors highlight the impact the polyprotein conformation has on the cleavage efficiency of the main protease (Mpro) and hence the order of release of non-structural proteins 7-10 (nsp7-10) of the SARS-CoV. Cleavage order is important in controlling viral processes and seems to have relevance in terms of the protein-protein complexes formed. The authors made use of mass spectrometry to advance our understanding of the mechanism by which coronaviruses control nsp 7, 8, 9 and 10 production in the virus life cycle.
MeSH term(s)	Betacoronavirus ; COVID-19 ; Coronavirus ; Coronavirus Infections ; Humans ; Pandemics ; Pneumonia, Viral ; Polyproteins ; SARS Virus ; SARS-CoV-2 ; Virus Replication
Chemical Substances	Polyproteins
Keywords	covid19
Language	English
Publishing date	2020-04-27
Publishing country	England
Document type	Journal Article ; Comment
ZDB-ID	2969-5
ISSN	1470-8728 ; 0006-2936 ; 0306-3275 ; 0264-6021
ISSN (online)	1470-8728
ISSN	0006-2936 ; 0306-3275 ; 0264-6021
DOI	10.1042/BCJ20200223
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Article ; Online: Spectroscopic Analysis of the Bacterially Expressed Head Domain of Rotavirus VP6.

Strachan, Milaan Simone / Mashapa, Tshepo / Gildenhuys, Samantha

Bioscience reports

2024

Abstract: The rotavirus capsid protein VP6 forms the middle of three protein layers and is responsible for many critical steps in the viral life cycle. VP6 as a structural protein can be used in various applications including as a subunit vaccine component. The ... ...

Abstract	The rotavirus capsid protein VP6 forms the middle of three protein layers and is responsible for many critical steps in the viral life cycle. VP6 as a structural protein can be used in various applications including as a subunit vaccine component. The head domain of VP6 (VP6H) contains key sequences that allow the protein to trimerize and that represent epitopes that are recognized by human antibodies in the viral particle. The domain is rich in beta-sheet secondary structures. Here VP6H was solubilised from bacterial inclusion bodies and purified using a single affinity chromatography step. Spectral (far-UV circular dichroism and intrinsic tryptophan fluorescence) analysis revealed that the purified domain had native-like secondary and tertiary structures. The domain could maintain structure up to 44°C during thermal denaturation following which structural changes result in an intermediate forming and finally irreversible aggregation and denaturation. The chemical denaturation with urea and guanidinium chloride produces intermediates that represent a loss in the cooperativity. The VP6H domainis stable and can fold to produce its native structure in the absence of the VP6 base domain but cannot be defined as an independent folding unit.
Language	English
Publishing date	2024-04-09
Publishing country	England
Document type	Journal Article
ZDB-ID	764946-0
ISSN	1573-4935 ; 0144-8463
ISSN (online)	1573-4935
ISSN	0144-8463
DOI	10.1042/BSR20232178
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Article: Expanding our understanding of the role polyprotein conformation plays in the coronavirus life cycle

Gildenhuys, Samantha

Biochem J

Abstract	Coronavirus are the causative agents in many globally concerning respiratory disease outbreaks such as severe acute respiratory syndrome (SARS), Middle East respiratory syndrome (MERS) and coronavirus disease-2019 (COVID-19). It is therefore important that we improve our understanding of how the molecular components of the virus facilitate the viral life cycle. These details will allow for the design of effective interventions. Krichel and coauthors in their article in the Biochemical Journal provide molecular details of how the viral polyprotein (nsp7-10) produced from the positive single stranded RNA genome, is cleaved to form proteins that are part of the replication/transcription complex. The authors highlight the impact the polyprotein conformation has on the cleavage efficiency of the main protease (Mpro) and hence the order of release of non-structural proteins 7-10 (nsp7-10) of the SARS-CoV. Cleavage order is important in controlling viral processes and seems to have relevance in terms of the protein-protein complexes formed. The authors made use of mass spectrometry to advance our understanding of the mechanism by which coronaviruses control nsp 7, 8, 9 and 10 production in the virus life cycle.
Keywords	covid19
Publisher	WHO
Document type	Article
Note	WHO #Covidence: #143859
Database	COVID19

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Article ; Online: Expanding our understanding of the role polyprotein conformation plays in the coronavirus life cycle

Gildenhuys, Samantha

Biochemical Journal

2020 Volume 477, Issue 8, Page(s) 1479–1482

Abstract	Coronavirus are the causative agents in many globally concerning respiratory disease outbreaks such as severe acute respiratory syndrome (SARS), Middle East respiratory syndrome (MERS) and coronavirus disease-2019 (COVID-19). It is therefore important that we improve our understanding of how the molecular components of the virus facilitate the viral life cycle. These details will allow for the design of effective interventions. Krichel and coauthors in their article in the Biochemical Journal provide molecular details of how the viral polyprotein (nsp7–10) produced from the positive single stranded RNA genome, is cleaved to form proteins that are part of the replication/transcription complex. The authors highlight the impact the polyprotein conformation has on the cleavage efficiency of the main protease (Mpro) and hence the order of release of non-structural proteins 7–10 (nsp7–10) of the SARS-CoV. Cleavage order is important in controlling viral processes and seems to have relevance in terms of the protein–protein complexes formed. The authors made use of mass spectrometry to advance our understanding of the mechanism by which coronaviruses control nsp 7, 8, 9 and 10 production in the virus life cycle.
Keywords	Cell Biology ; Biochemistry ; Molecular Biology ; covid19
Language	English
Publisher	Portland Press Ltd.
Publishing country	uk
Document type	Article ; Online
ZDB-ID	2969-5
ISSN	1470-8728 ; 0006-2936 ; 0306-3275 ; 0264-6021
ISSN (online)	1470-8728
ISSN	0006-2936 ; 0306-3275 ; 0264-6021
DOI	10.1042/bcj20200223
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Expanding our understanding of the role polyprotein conformation plays in the coronavirus life cycle

Gildenhuys, Samantha

2020

Abstract: Connected Content This is a commentary on: Processing of the SARS-CoV pp1a/ab nsp7–10 region ... Coronavirus are the causative agents in many globally concerning respiratory disease outbreaks such as severe acute respiratory syndrome (SARS), Middle East ... ...

Abstract	Connected Content This is a commentary on: Processing of the SARS-CoV pp1a/ab nsp7–10 region Coronavirus are the causative agents in many globally concerning respiratory disease outbreaks such as severe acute respiratory syndrome (SARS), Middle East respiratory syndrome (MERS) and coronavirus disease-2019 (COVID-19). It is therefore important that we improve our understanding of how the molecular components of the virus facilitate the viral life cycle. These details will allow for the design of effective interventions. Krichel and coauthors in their article in the Biochemical Journal provide molecular details of how the viral polyprotein (nsp7–10) produced from the positive single stranded RNA genome, is cleaved to form proteins that are part of the replication/transcription complex. The authors highlight the impact the polyprotein conformation has on the cleavage efficiency of the main protease (Mpro) and hence the order of release of non-structural proteins 7–10 (nsp7–10) of the SARS-CoV. Cleavage order is important in controlling viral processes and seems to have relevance in terms of the protein–protein complexes formed. The authors made use of mass spectrometry to advance our understanding of the mechanism by which coronaviruses control nsp 7, 8, 9 and 10 production in the virus life cycle. Life and Consumer Sciences
Keywords	Covid-19 ; Coronavirus ; nsp7–10 ; polyprotein ; 1a/ab ; polyprotein conformation ; posttranslational control ; SARS-CoV ; covid19
Subject code	572
Language	English
Publisher	Portland Press
Publishing country	za
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article: In Vitro α-Glucosidase and α-Amylase Inhibition, Cytotoxicity and Free Radical Scavenging Profiling of the 6-Halogeno and Mixed 6,8-Dihalogenated 2-Aryl-4-methyl-1,2-dihydroquinazoline 3-Oxides.

Magwaza, Nontokozo M / More, Garland K / Gildenhuys, Samantha / Mphahlele, Malose J

Antioxidants (Basel, Switzerland)

2023 Volume 12, Issue 11

Abstract: Series of the 6-bromo/iodo substituted 2-aryl-4-methyl-1,2-dihydroquinazoline-3-oxides and their mixed 6,8-dihalogenated (Br/I and I/Br) derivatives were evaluated for inhibitory properties against α-glucosidase and/or α-amylase activities and for ... ...

Abstract	Series of the 6-bromo/iodo substituted 2-aryl-4-methyl-1,2-dihydroquinazoline-3-oxides and their mixed 6,8-dihalogenated (Br/I and I/Br) derivatives were evaluated for inhibitory properties against α-glucosidase and/or α-amylase activities and for cytotoxicity against breast (MCF-7) and lung (A549) cancer cell lines. The 6-bromo-2-phenyl substituted
Language	English
Publishing date	2023-11-06
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2704216-9
ISSN	2076-3921
ISSN	2076-3921
DOI	10.3390/antiox12111971
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Article: Bluetongue virus viral protein 7 stability in the presence of glycerol and sodium chloride.

Russell, Bonnie Leigh / Gildenhuys, Samantha

Clinical and experimental vaccine research

2020 Volume 9, Issue 2, Page(s) 108–118

Abstract: Purpose: The : Materials and methods: Recombinant BTV VP7 was expressed in a bacterial cell system and purified before being analysed using spectroscopic techniques including far-ultraviolet (UV) circular dichroism and intrinsic tryptophan ... ...

Abstract	Purpose: The Materials and methods: Recombinant BTV VP7 was expressed in a bacterial cell system and purified before being analysed using spectroscopic techniques including far-ultraviolet (UV) circular dichroism and intrinsic tryptophan fluorescence. BTV was analysed in a number of different buffer conditions. Results: We report here that BTV VP7 maintains its native secondary structure until at least 52℃ and native-like tertiary structure to at least 80℃. Far-UV circular dichroism and intrinsic tryptophan fluorescence emission spectra indicate significant secondary and tertiary structure remaining even at 90℃, respectively. Six M guanidinium chloride is able to unfold BTV VP7 while 8 M urea could not. Conclusion: Twenty percent glycerol and 300 mM sodium chloride appear to have a protective effect on BTV VP7's structure, as significantly more structure is seen at 90℃ when compared to BTV VP7 without the addition of these chemicals. Both glycerol and sodium chloride are common vaccine additives.
Language	English
Publishing date	2020-07-31
Publishing country	Korea (South)
Document type	Journal Article
ZDB-ID	2684652-4
ISSN	2287-366X ; 2287-3651
ISSN (online)	2287-366X
ISSN	2287-3651
DOI	10.7774/cevr.2020.9.2.108
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Article: In Vitro Enzymatic and Kinetic Studies, and In Silico Drug-Receptor Interactions, and Drug-Like Profiling of the 5-Styrylbenzamide Derivatives as Potential Cholinesterase and β-Secretase Inhibitors with Antioxidant Properties.

Mphahlele, Malose J / Agbo, Emmanuel N / More, Garland K / Gildenhuys, Samantha

Antioxidants (Basel, Switzerland)

2021 Volume 10, Issue 5

Abstract: The 5-(styryl)anthranilamides were transformed into the corresponding 5-styryl-2-( ...

Abstract	The 5-(styryl)anthranilamides were transformed into the corresponding 5-styryl-2-(
Language	English
Publishing date	2021-04-22
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2704216-9
ISSN	2076-3921
ISSN	2076-3921
DOI	10.3390/antiox10050647
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Article ; Online: Solubilisation and purification of recombinant bluetongue virus VP7 expressed in a bacterial system.

Russell, Bonnie L / Gildenhuys, Samantha

Protein expression and purification

2018 Volume 147, Page(s) 85–93

Abstract: Bluetongue virus (BTV) is an Orbivirus that has a profound economic impact due to direct loss of livestock as well as movement bans in an attempt to prevent the spread of the disease to susceptible areas. BTV VP7, along with VP3, forms the inner capsid ... ...

Abstract	Bluetongue virus (BTV) is an Orbivirus that has a profound economic impact due to direct loss of livestock as well as movement bans in an attempt to prevent the spread of the disease to susceptible areas. BTV VP7, along with VP3, forms the inner capsid core of the virus where it acts as the barrier between the outer layer and the inner core housing the genetic material. Purification of BTV VP7 has proven to be problematic and expensive mainly due to its insolubility is several expression systems. To overcome this, in this paper we present a protocol for the solubilisation of BTV VP7 from inclusion bodies expressed in E.coli, and subsequent purification using nickel affinity chromatography. The purified protein was then characterised using native PAGE, far ultraviolet circular dichroism (far-UV CD) and intrinsic fluorescence and found to have both secondary and tertiary structure even in the presence of 5 M urea. Both tertiary and secondary structure was further shown to be to be maintained at least to 42 °C in 5 M urea.
MeSH term(s)	Bluetongue virus/genetics ; Bluetongue virus/metabolism ; Circular Dichroism ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Inclusion Bodies, Viral/metabolism ; Protein Unfolding ; Recombinant Proteins/chemistry ; Recombinant Proteins/isolation & purification ; Recombinant Proteins/metabolism ; Solubility ; Spectrometry, Fluorescence ; Temperature ; Viral Core Proteins/chemistry ; Viral Core Proteins/genetics ; Viral Core Proteins/metabolism
Chemical Substances	Recombinant Proteins ; Viral Core Proteins ; VP7 protein, orbivirus (137764-11-5)
Language	English
Publishing date	2018-03-15
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1055455-5
ISSN	1096-0279 ; 1046-5928
ISSN (online)	1096-0279
ISSN	1046-5928
DOI	10.1016/j.pep.2018.03.006
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Article ; Online: Benzofuran-selenadiazole hybrids as novel α-glucosidase and cyclooxygenase-2 inhibitors with antioxidant and cytotoxic properties.

Olomola, Temitope O / Mphahlele, Malose J / Gildenhuys, Samantha

Bioorganic chemistry

2020 Volume 100, Page(s) 103945

Abstract: Series of 2-arylbenzofuran-1,2,3-selenodiazole hybrids were prepared via multiple reactions and then evaluated in vitro through enzymatic assay for inhibitory effect against α-glucosidase and cyclooxygenase-2 (COX-2) activities including antioxidant ... ...

Abstract	Series of 2-arylbenzofuran-1,2,3-selenodiazole hybrids were prepared via multiple reactions and then evaluated in vitro through enzymatic assay for inhibitory effect against α-glucosidase and cyclooxygenase-2 (COX-2) activities including antioxidant activity. The presence of 1,2,3-selenodiazole moiety resulted in increased inhibitory effect for compounds 4a-f against α-glucosidase and COX-2 activities, and increased free radical scavenging activity. 6-Acetoxy-2-phenyl-5-(1,2,3-selenadiazol-4-yl)benzofuran (4a) and its 2-(4-methoxyphenyl) substituted derivative (4f) were, in turn, screened for antiproliferation against the breast MCF-7 cancer cell line and for cytotoxicity on the human embryonic kidney derived Hek293-T cells. A cell-based antioxidant activity assay involving lipopolysaccharide induced reactive oxygen species production in these cells was performed. Molecular docking has also been performed on these two compounds to predict protein-ligand interactions against α-glucosidase and COX-2.
MeSH term(s)	Antioxidants/chemistry ; Azoles/chemistry ; Benzofurans/chemistry ; Binding Sites ; Catalytic Domain ; Cell Line ; Cell Survival/drug effects ; Cyclooxygenase 2/chemistry ; Cyclooxygenase 2/metabolism ; Cyclooxygenase 2 Inhibitors/chemistry ; Cyclooxygenase 2 Inhibitors/metabolism ; Cyclooxygenase 2 Inhibitors/pharmacology ; Glycoside Hydrolase Inhibitors/chemistry ; Glycoside Hydrolase Inhibitors/metabolism ; Glycoside Hydrolase Inhibitors/pharmacology ; Humans ; Kinetics ; Lipopolysaccharides/pharmacology ; MCF-7 Cells ; Molecular Conformation ; Molecular Docking Simulation ; Reactive Oxygen Species/metabolism ; Structure-Activity Relationship ; alpha-Glucosidases/chemistry ; alpha-Glucosidases/metabolism
Chemical Substances	Antioxidants ; Azoles ; Benzofurans ; Cyclooxygenase 2 Inhibitors ; Glycoside Hydrolase Inhibitors ; Lipopolysaccharides ; Reactive Oxygen Species ; Cyclooxygenase 2 (EC 1.14.99.1) ; alpha-Glucosidases (EC 3.2.1.20) ; benzofuran (LK6946W774)
Language	English
Publishing date	2020-05-18
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	120080-x
ISSN	1090-2120 ; 0045-2068
ISSN (online)	1090-2120
ISSN	0045-2068
DOI	10.1016/j.bioorg.2020.103945
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