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Article ; Online: How tetraspanin-mediated cell entry of SARS-CoV-2 can dysregulate the shedding of the ACE2 receptor by ADAM17.

Healy, Eamonn F

Biochemical and biophysical research communications

2022 Volume 593, Page(s) 52–56

Abstract: COVID-19, the respiratory infection caused by the novel coronavirus SARS-CoV-2, presents a clinical picture consistent with the dysregulation of many of the pathways mediated by the metalloprotease ADAM17. ADAM17 is a sheddase that plays a key role in ... ...

Abstract	COVID-19, the respiratory infection caused by the novel coronavirus SARS-CoV-2, presents a clinical picture consistent with the dysregulation of many of the pathways mediated by the metalloprotease ADAM17. ADAM17 is a sheddase that plays a key role in the modulation of ACE2, the receptor which also functions as the point of attachment leading to cell entry by the virus. This work investigates the possibility that ADAM17 dysregulation and attachment of the SARS-CoV-2 virion to the ACE2 receptor are linked events, with the latter causing the former. Tetraspanins, the transmembrane proteins that function as scaffolds for the construction of viral entry platforms, are mooted as key components in this connection.
MeSH term(s)	ADAM17 Protein/chemistry ; ADAM17 Protein/metabolism ; Angiotensin-Converting Enzyme 2/chemistry ; Angiotensin-Converting Enzyme 2/metabolism ; Binding Sites ; COVID-19/epidemiology ; COVID-19/transmission ; COVID-19/virology ; Humans ; Models, Biological ; Molecular Docking Simulation ; Multiprotein Complexes/chemistry ; Multiprotein Complexes/metabolism ; Pandemics ; Protein Binding ; Protein Domains ; Receptors, Virus/chemistry ; Receptors, Virus/metabolism ; SARS-CoV-2/metabolism ; SARS-CoV-2/physiology ; Tetraspanin 29/chemistry ; Tetraspanin 29/metabolism ; Virus Internalization
Chemical Substances	Multiprotein Complexes ; Receptors, Virus ; Tetraspanin 29 ; Angiotensin-Converting Enzyme 2 (EC 3.4.17.23) ; ADAM17 Protein (EC 3.4.24.86)
Language	English
Publishing date	2022-01-15
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	205723-2
ISSN	1090-2104 ; 0006-291X ; 0006-291X
ISSN (online)	1090-2104 ; 0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2022.01.038
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Article: How tetraspanin-mediated cell entry of SARS-CoV-2 can dysregulate the shedding of the ACE2 receptor by ADAM17

Healy, Eamonn F.

Biochemical and biophysical research communications. 2022 Feb. 19, v. 593

2022

Abstract	COVID-19, the respiratory infection caused by the novel coronavirus SARS-CoV-2, presents a clinical picture consistent with the dysregulation of many of the pathways mediated by the metalloprotease ADAM17. ADAM17 is a sheddase that plays a key role in the modulation of ACE2, the receptor which also functions as the point of attachment leading to cell entry by the virus. This work investigates the possibility that ADAM17 dysregulation and attachment of the SARS-CoV-2 virion to the ACE2 receptor are linked events, with the latter causing the former. Tetraspanins, the transmembrane proteins that function as scaffolds for the construction of viral entry platforms, are mooted as key components in this connection.
Keywords	COVID-19 infection ; Severe acute respiratory syndrome coronavirus 2 ; metalloproteinases ; research ; respiratory tract diseases ; virion ; viruses
Language	English
Dates of publication	2022-0219
Size	p. 52-56.
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	205723-2
ISSN	0006-291X ; 0006-291X
ISSN (online)	0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2022.01.038
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Article ; Online: Organic chemistry as representation.

Healy, Eamonn F

Foundations of chemistry

2020 Volume 23, Issue 1, Page(s) 59–68

Abstract: Electron redistribution is the cornerstone of our understanding of chemical reactivity. For the vast majority of organic reactions electrons are assumed to move in pairs providing explanatory mechanisms through the generation of intermediate structures. ... ...

Abstract	Electron redistribution is the cornerstone of our understanding of chemical reactivity. For the vast majority of organic reactions electrons are assumed to move in pairs providing explanatory mechanisms through the generation of intermediate structures. But for many transformations these discrete steps are idealized constructs, involving intermediates assumed but not empirically justified. This unitary perspective predicated on the curved arrow formalism has resulted in the scenario where for many organic transformations our supposed understanding far surpasses our growing knowledge. Reformulating organic mechanisms to include single electron transfer (SET) as a component of, or an alternative to, the prevailing iconic descriptions can provide for a more empirically adequate mechanistic description. In addition using the language of SET presents an opportunity to unify mechanistic concepts under a common donor/acceptor framework.
Language	English
Publishing date	2020-07-06
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	2015456-2
ISSN	1572-8463 ; 1386-4238
ISSN (online)	1572-8463
ISSN	1386-4238
DOI	10.1007/s10698-020-09379-z
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Article: Visualizing the molecular wave function in σ-coordinated complexes.

Healy, Eamonn F

Computational & theoretical chemistry

2018 Volume 1125, Page(s) 128–132

Abstract: The π-complex theory developed by Michael J. S. Dewar in 1949 has had its most profound impact as part of the Dewar-Chatt-Duncanson model, a seminal and foundational contribution to the field of organometallic chemistry. Over time it has demonstrated its ...

Abstract	The π-complex theory developed by Michael J. S. Dewar in 1949 has had its most profound impact as part of the Dewar-Chatt-Duncanson model, a seminal and foundational contribution to the field of organometallic chemistry. Over time it has demonstrated its utility in systems far from those originally envisaged, including σ-coordinated metal-complexes. This latter application is notable due to Dewar's original skepticism that his π-complex theory could be extended to σ-bonds. Separately it has previously been demonstrated that a one-electron wave function. can be shown to satisfy an exact one-electron Schrödinger equation describing the motion of the single electron in the average field of the remaining electrons. To celebrate the centenary of his birth this paper seeks to demonstrate that σ-coordinated metal-complexes present a perfect system to exemplify both the utility of the one-electron wave function and the power of the π-complex theory.
Language	English
Publishing date	2018-01-06
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	2587365-9
ISSN	2210-271X
ISSN	2210-271X
DOI	10.1016/j.comptc.2018.01.010
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Article ; Online: A model for COVID-19-induced dysregulation of ACE2 shedding by ADAM17.

Healy, Eamonn F / Lilic, Marko

Biochemical and biophysical research communications

2021 Volume 573, Page(s) 158–163

Abstract: The angiotensin Converting Enzyme 2 (ACE2) receptor is a key component of the renin-angiotensin-aldesterone system (RAAS) that mediates numerous effects in the cardiovascular system. It is also the cellular point of contact for the coronavirus spike ... ...

Abstract	The angiotensin Converting Enzyme 2 (ACE2) receptor is a key component of the renin-angiotensin-aldesterone system (RAAS) that mediates numerous effects in the cardiovascular system. It is also the cellular point of contact for the coronavirus spike protein. Cleavage of the receptor is both important to its physiological function as well as being necessary for cell entry by the virus. Shedding of ACE2 by the metalloprotease ADAM17 releases a catalytically active soluble form of ACE2, but cleavage by the serine protease TMPRSS2 is necessary for virion internalization. Complicating the issue is the observation that circulating ACE2 can also bind to the virus effectively blocking attachment to the membrane-bound receptor. This work investigates the possibility that the inflammatory response to coronavirus infection can abrogate shedding by ADAM17, thereby favoring cleavage by TMPRSS2 and thus cell entry by the virion.
MeSH term(s)	ADAM17 Protein/chemistry ; ADAM17 Protein/metabolism ; Angiotensin-Converting Enzyme 2/chemistry ; Angiotensin-Converting Enzyme 2/metabolism ; Binding Sites ; HSP20 Heat-Shock Proteins/chemistry ; HSP20 Heat-Shock Proteins/metabolism ; Heat-Shock Response/physiology ; Host-Pathogen Interactions/physiology ; Humans ; Protein Domains ; Protein Interaction Domains and Motifs ; SARS-CoV-2/pathogenicity ; Serine Endopeptidases/metabolism ; Virus Internalization
Chemical Substances	HSP20 Heat-Shock Proteins ; HSPB6 protein, human ; ACE2 protein, human (EC 3.4.17.23) ; Angiotensin-Converting Enzyme 2 (EC 3.4.17.23) ; Serine Endopeptidases (EC 3.4.21.-) ; TMPRSS2 protein, human (EC 3.4.21.-) ; ADAM17 Protein (EC 3.4.24.86) ; ADAM17 protein, human (EC 3.4.24.86)
Language	English
Publishing date	2021-08-15
Publishing country	United States
Document type	Journal Article
ZDB-ID	205723-2
ISSN	1090-2104 ; 0006-291X ; 0006-291X
ISSN (online)	1090-2104 ; 0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2021.08.040
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Article: A model for COVID-19-induced dysregulation of ACE2 shedding by ADAM17

Healy, Eamonn F. / Lilic, Marko

Biochemical and biophysical research communications. 2021 Oct. 08, v. 573

2021

Abstract	The angiotensin Converting Enzyme 2 (ACE2) receptor is a key component of the renin-angiotensin-aldesterone system (RAAS) that mediates numerous effects in the cardiovascular system. It is also the cellular point of contact for the coronavirus spike protein. Cleavage of the receptor is both important to its physiological function as well as being necessary for cell entry by the virus. Shedding of ACE2 by the metalloprotease ADAM17 releases a catalytically active soluble form of ACE2, but cleavage by the serine protease TMPRSS2 is necessary for virion internalization. Complicating the issue is the observation that circulating ACE2 can also bind to the virus effectively blocking attachment to the membrane-bound receptor. This work investigates the possibility that the inflammatory response to coronavirus infection can abrogate shedding by ADAM17, thereby favoring cleavage by TMPRSS2 and thus cell entry by the virion.
Keywords	Coronavirus infections ; cardiovascular system ; inflammation ; metalloproteinases ; models ; research ; serine proteinases ; virion ; viruses
Language	English
Dates of publication	2021-1008
Size	p. 158-163.
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	205723-2
ISSN	0006-291X ; 0006-291X
ISSN (online)	0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2021.08.040
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Article ; Online: A prion-like mechanism for the propagated misfolding of SOD1 from in silico modeling of solvated near-native conformers.

Healy, Eamonn F

PloS one

2017 Volume 12, Issue 5, Page(s) e0177284

Abstract: A prion-like mechanism has been developed to explain the observed promotion of amyloid aggregation caused by conversion of structurally intact SOD1 to a misfolded form. Superoxide dismutase [Cu-Zn], or SOD1, is a homo-dimeric protein that functions as an ...

Abstract	A prion-like mechanism has been developed to explain the observed promotion of amyloid aggregation caused by conversion of structurally intact SOD1 to a misfolded form. Superoxide dismutase [Cu-Zn], or SOD1, is a homo-dimeric protein that functions as an antioxidant by scavenging for superoxide. The misfolding and aggregation of SOD1 is linked to inherited, or familial, amyotrophic lateral sclerosis (FALS), a progressive and fatal neurodegenerative disease. Aberrant SOD1 folding has also been strongly implicated in disease causation for sporadic ALS, or SALS, which accounts for ~90% of ALS cases. Studies have found that mutant, misfolded SOD1 can convert wtSOD1 in a prion-like fashion, and that misfolded wtSOD1 can be propagated by release and uptake of protein aggregates. Here it is demonstrated that enervating the SOD1 electrostatic loop can lead to an experimentally observed gain of interaction (GOI) responsible for the formation of SOD1 amyloid-like filaments. This enervation is caused in turn by the formation of transient, non-obligate oligomers between pathogenic SOD1 mutants and wt SOD1.
MeSH term(s)	Computer Simulation ; Dimerization ; Humans ; Molecular Dynamics Simulation ; Prions/metabolism ; Protein Conformation ; Protein Folding ; Superoxide Dismutase-1/chemistry ; Superoxide Dismutase-1/metabolism
Chemical Substances	Prions ; SOD1 protein, human ; Superoxide Dismutase-1 (EC 1.15.1.1)
Language	English
Publishing date	2017-05-04
Publishing country	United States
Document type	Journal Article
ZDB-ID	2267670-3
ISSN	1932-6203 ; 1932-6203
ISSN (online)	1932-6203
ISSN	1932-6203
DOI	10.1371/journal.pone.0177284
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Article ; Online: A mechanism for propagated SOD1 misfolding from frustration analysis of a G85R mutant protein assembly.

Healy, Eamonn F

Biochemical and biophysical research communications

2016 Volume 478, Issue 4, Page(s) 1634–1639

Abstract: Application of landscape theory and the dehydron hypothesis to a crystal structure of a G85R mutant superoxide dismutase (SOD1) tetrameric complex allows for the description of a prion-like hypothesis that serves to explain propagated SOD1 misfolding. We ...

Abstract	Application of landscape theory and the dehydron hypothesis to a crystal structure of a G85R mutant superoxide dismutase (SOD1) tetrameric complex allows for the description of a prion-like hypothesis that serves to explain propagated SOD1 misfolding. We have developed two conformational-change scenarios, one local to the ESL at the complex interface, and a second displacement at the ESL of the otherdimeric subunit. When taken together these provide for a prion-like mechanism that can serve to explain the observed conversion of wtSOD1 to a misfolded form by the G85R mutant.
MeSH term(s)	Amyotrophic Lateral Sclerosis/enzymology ; Amyotrophic Lateral Sclerosis/genetics ; Crystallography, X-Ray ; Humans ; Hydrogen Bonding ; Molecular Dynamics Simulation ; Mutant Proteins/chemistry ; Mutant Proteins/metabolism ; Mutation, Missense ; Prions/chemistry ; Protein Conformation ; Protein Folding ; Protein Multimerization ; Protein Subunits/chemistry ; Protein Subunits/genetics ; Protein Subunits/metabolism ; Static Electricity ; Superoxide Dismutase-1/chemistry ; Superoxide Dismutase-1/genetics ; Superoxide Dismutase-1/metabolism
Chemical Substances	Mutant Proteins ; Prions ; Protein Subunits ; SOD1 protein, human ; Superoxide Dismutase-1 (EC 1.15.1.1)
Language	English
Publishing date	2016--30
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	205723-2
ISSN	1090-2104 ; 0006-291X ; 0006-291X
ISSN (online)	1090-2104 ; 0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2016.08.172
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Article ; Online: A model for non-obligate oligomer formation in protein aggregration.

Healy, Eamonn F

Biochemical and biophysical research communications

2015 Volume 465, Issue 3, Page(s) 523–527

Abstract: Using solvent-exposed intramolecular backbone hydrogen bonds as physico-chemical descriptors for protein packing, a role for transient, non-obligate oligomers in the formation of aberrant protein aggregates is presented. Oligomeric models of the both ... ...

Abstract	Using solvent-exposed intramolecular backbone hydrogen bonds as physico-chemical descriptors for protein packing, a role for transient, non-obligate oligomers in the formation of aberrant protein aggregates is presented. Oligomeric models of the both wild type (wt) and select mutant variants of superoxide dismutase (SOD1) are proposed to provide a structural basis for investigating the etiology of Amyotrophic Lateral Sclerosis (ALS).
MeSH term(s)	Binding Sites ; Hydrogen Bonding ; Models, Chemical ; Molecular Docking Simulation ; Multiprotein Complexes/chemistry ; Multiprotein Complexes/ultrastructure ; Protein Binding ; Protein Conformation ; Superoxide Dismutase/chemistry ; Superoxide Dismutase/ultrastructure ; Superoxide Dismutase-1
Chemical Substances	Multiprotein Complexes ; Superoxide Dismutase (EC 1.15.1.1) ; Superoxide Dismutase-1 (EC 1.15.1.1)
Language	English
Publishing date	2015-09-25
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	205723-2
ISSN	1090-2104 ; 0006-291X ; 0006-291X
ISSN (online)	1090-2104 ; 0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2015.08.052
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Article ; Online: A prion-like mechanism for the propagated misfolding of SOD1 from in silico modeling of solvated near-native conformers.

Eamonn F Healy

PLoS ONE, Vol 12, Iss 5, p e

2017 Volume 0177284

Abstract	A prion-like mechanism has been developed to explain the observed promotion of amyloid aggregation caused by conversion of structurally intact SOD1 to a misfolded form. Superoxide dismutase [Cu-Zn], or SOD1, is a homo-dimeric protein that functions as an antioxidant by scavenging for superoxide. The misfolding and aggregation of SOD1 is linked to inherited, or familial, amyotrophic lateral sclerosis (FALS), a progressive and fatal neurodegenerative disease. Aberrant SOD1 folding has also been strongly implicated in disease causation for sporadic ALS, or SALS, which accounts for ~90% of ALS cases. Studies have found that mutant, misfolded SOD1 can convert wtSOD1 in a prion-like fashion, and that misfolded wtSOD1 can be propagated by release and uptake of protein aggregates. Here it is demonstrated that enervating the SOD1 electrostatic loop can lead to an experimentally observed gain of interaction (GOI) responsible for the formation of SOD1 amyloid-like filaments. This enervation is caused in turn by the formation of transient, non-obligate oligomers between pathogenic SOD1 mutants and wt SOD1.
Keywords	Medicine ; R ; Science ; Q
Subject code	612
Language	English
Publishing date	2017-01-01T00:00:00Z
Publisher	Public Library of Science (PLoS)
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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