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Article: Comparative host interactomes of the SARS-CoV-2 nonstructural protein 3 and human coronavirus homologs.

Almasy, Katherine M / Davies, Jonathan P / Plate, Lars

bioRxiv : the preprint server for biology

2021

Abstract: Human coronaviruses have become an increasing threat to global health; three highly pathogenic strains have emerged since the early 2000s, including most recently SARS-CoV-2, the cause of COVID-19. A better understanding of the molecular mechanisms of ... ...

Abstract	Human coronaviruses have become an increasing threat to global health; three highly pathogenic strains have emerged since the early 2000s, including most recently SARS-CoV-2, the cause of COVID-19. A better understanding of the molecular mechanisms of coronavirus pathogenesis is needed, including how these highly virulent strains differ from those that cause milder, common-cold like disease. While significant progress has been made in understanding how SARS-CoV-2 proteins interact with the host cell, non-structural protein 3 (nsp3) has largely been omitted from the analyses. Nsp3 is a viral protease with important roles in viral protein biogenesis, replication complex formation, and modulation of host ubiquitinylation and ISGylation. Herein, we use affinity purification-mass spectrometry to study the host-viral protein-protein interactome of nsp3 from five coronavirus strains: pathogenic strains SARS-CoV-2, SARS-CoV, and MERS-CoV; and endemic common-cold strains hCoV-229E and hCoV-OC43. We divide each nsp3 into three fragments and use tandem mass tag technology to directly compare the interactors across the five strains for each fragment. We find that few interactors are common across all variants for a particular fragment, but we identify shared patterns between select variants, such as ribosomal proteins enriched in the N-terminal fragment (nsp3.1) dataset for SARS-CoV-2 and SARS-CoV. We also identify unique biological processes enriched for individual homologs, for instance nuclear protein important for the middle fragment of hCoV-229E, as well as ribosome biogenesis of the MERS nsp3.2 homolog. Lastly, we further investigate the interaction of the SARS-CoV-2 nsp3 N-terminal fragment with ATF6, a regulator of the unfolded protein response. We show that SARS-CoV-2 nsp3.1 directly binds to ATF6 and can suppress the ATF6 stress response. Characterizing the host interactions of nsp3 widens our understanding of how coronaviruses co-opt cellular pathways and presents new avenues for host-targeted antiviral therapeutics.
Language	English
Publishing date	2021-03-08
Publishing country	United States
Document type	Preprint
DOI	10.1101/2021.03.08.434440
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Article ; Online: Comparative Host Interactomes of the SARS-CoV-2 Nonstructural Protein 3 and Human Coronavirus Homologs.

Almasy, Katherine M / Davies, Jonathan P / Plate, Lars

Molecular & cellular proteomics : MCP

2021 Volume 20, Page(s) 100120

Abstract	Human coronaviruses have become an increasing threat to global health; three highly pathogenic strains have emerged since the early 2000s, including most recently SARS-CoV-2, the cause of COVID-19. A better understanding of the molecular mechanisms of coronavirus pathogenesis is needed, including how these highly virulent strains differ from those that cause milder, common-cold-like disease. While significant progress has been made in understanding how SARS-CoV-2 proteins interact with the host cell, nonstructural protein 3 (nsp3) has largely been omitted from the analyses. Nsp3 is a viral protease with important roles in viral protein biogenesis, replication complex formation, and modulation of host ubiquitinylation and ISGylation. Herein, we use affinity purification-mass spectrometry to study the host-viral protein-protein interactome of nsp3 from five coronavirus strains: pathogenic strains SARS-CoV-2, SARS-CoV, and MERS-CoV; and endemic common-cold strains hCoV-229E and hCoV-OC43. We divide each nsp3 into three fragments and use tandem mass tag technology to directly compare the interactors across the five strains for each fragment. We find that few interactors are common across all variants for a particular fragment, but we identify shared patterns between select variants, such as ribosomal proteins enriched in the N-terminal fragment (nsp3.1) data set for SARS-CoV-2 and SARS-CoV. We also identify unique biological processes enriched for individual homologs, for instance, nuclear protein import for the middle fragment of hCoV-229E, as well as ribosome biogenesis of the MERS nsp3.2 homolog. Lastly, we further investigate the interaction of the SARS-CoV-2 nsp3 N-terminal fragment with ATF6, a regulator of the unfolded protein response. We show that SARS-CoV-2 nsp3.1 directly binds to ATF6 and can suppress the ATF6 stress response. Characterizing the host interactions of nsp3 widens our understanding of how coronaviruses co-opt cellular pathways and presents new avenues for host-targeted antiviral therapeutics.
MeSH term(s)	Activating Transcription Factor 6/metabolism ; Coronavirus 229E, Human/metabolism ; Coronavirus 229E, Human/pathogenicity ; Coronavirus OC43, Human/metabolism ; Coronavirus OC43, Human/pathogenicity ; Coronavirus Papain-Like Proteases/genetics ; Coronavirus Papain-Like Proteases/metabolism ; Endoplasmic Reticulum-Associated Degradation ; HEK293 Cells ; Host-Pathogen Interactions/physiology ; Humans ; Middle East Respiratory Syndrome Coronavirus/metabolism ; Middle East Respiratory Syndrome Coronavirus/pathogenicity ; Protein Interaction Maps ; SARS-CoV-2/metabolism ; SARS-CoV-2/pathogenicity ; Unfolded Protein Response ; Viral Nonstructural Proteins/genetics ; Viral Nonstructural Proteins/metabolism
Chemical Substances	ATF6 protein, human ; Activating Transcription Factor 6 ; Nsp3 protein, Middle East respiratory syndrome coronavirus ; Viral Nonstructural Proteins ; Coronavirus Papain-Like Proteases (EC 3.4.22.2) ; papain-like protease, SARS-CoV-2 (EC 3.4.22.2)
Language	English
Publishing date	2021-06-27
Publishing country	United States
Document type	Comparative Study ; Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2075924-1
ISSN	1535-9484 ; 1535-9476
ISSN (online)	1535-9484
ISSN	1535-9476
DOI	10.1016/j.mcpro.2021.100120
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Article ; Online: Comparative host interactomes of the SARS-CoV-2 nonstructural protein 3 and human coronavirus homologs

Almasy, Katherine M / Davies, Jonathan P / Plate, Lars

bioRxiv

Abstract	Human coronaviruses have become an increasing threat to global health; three highly pathogenic strains have emerged since the early 2000s, including most recently SARS-CoV-2, the cause of COVID-19. A better understanding of the molecular mechanisms of coronavirus pathogenesis is needed, including how these highly virulent strains differ from those that cause milder, common-cold like disease. While significant progress has been made in understanding how SARS-CoV-2 proteins interact with the host cell, non-structural protein 3 (nsp3) has largely been omitted from the analyses. Nsp3 is a viral protease with important roles in viral protein biogenesis, replication complex formation, and modulation of host ubiquitinylation and ISGylation. Herein, we use affinity purification-mass spectrometry to study the host-viral protein-protein interactome of nsp3 from five coronavirus strains: pathogenic strains SARS-CoV-2, SARS-CoV, and MERS-CoV; and endemic common-cold strains hCoV-229E and hCoV-OC43. We divide each nsp3 into three fragments and use tandem mass tag technology to directly compare the interactors across the five strains for each fragment. We find that few interactors are common across all variants for a particular fragment, but we identify shared patterns between select variants, such as ribosomal proteins enriched in the N-terminal fragment (nsp3.1) dataset for SARS-CoV-2 and SARS-CoV. We also identify unique biological processes enriched for individual homologs, for instance nuclear protein important for the middle fragment of hCoV-229E, as well as ribosome biogenesis of the MERS nsp3.2 homolog. Lastly, we further investigate the interaction of the SARS-CoV-2 nsp3 N-terminal fragment with ATF6, a regulator of the unfolded protein response. We show that SARS-CoV-2 nsp3.1 directly binds to ATF6 and can suppress the ATF6 stress response. Characterizing the host interactions of nsp3 widens our understanding of how coronaviruses co-opt cellular pathways and presents new avenues for host-targeted antiviral therapeutics.
Keywords	covid19
Language	English
Publishing date	2021-03-08
Publisher	Cold Spring Harbor Laboratory
Document type	Article ; Online
DOI	10.1101/2021.03.08.434440
Database	COVID19

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Article ; Online: Small-molecule endoplasmic reticulum proteostasis regulator acts as a broad-spectrum inhibitor of dengue and Zika virus infections.

Almasy, Katherine M / Davies, Jonathan P / Lisy, Samantha M / Tirgar, Reyhaneh / Tran, Sirena C / Plate, Lars

Proceedings of the National Academy of Sciences of the United States of America

2021 Volume 118, Issue 3

Abstract: Flaviviruses, including dengue and Zika, are widespread human pathogens; however, no broadly active therapeutics exist to fight infection. Recently, remodeling of endoplasmic reticulum (ER) proteostasis by pharmacologic regulators, such as compound 147, ... ...

Abstract	Flaviviruses, including dengue and Zika, are widespread human pathogens; however, no broadly active therapeutics exist to fight infection. Recently, remodeling of endoplasmic reticulum (ER) proteostasis by pharmacologic regulators, such as compound 147, was shown to correct pathologic ER imbalances associated with protein misfolding diseases. Here, we establish an additional activity of compound 147 as an effective host-centered antiviral agent against flaviviruses. Compound 147 reduces infection by attenuating the infectivity of secreted virions without causing toxicity in host cells. Compound 147 is a preferential activator of the ATF6 pathway of the ER unfolded protein response, which requires targeting of cysteine residues primarily on protein disulfide isomerases (PDIs). We find that the antiviral activity of 147 is independent of ATF6 induction but does require modification of reactive thiols on protein targets. Targeting PDIs and additional non-PDI targets using RNAi and other small-molecule inhibitors was unable to recapitulate the antiviral effects, suggesting a unique polypharmacology may mediate the activity. Importantly, 147 can impair infection of multiple strains of dengue and Zika virus, indicating that it is suitable as a broad-spectrum antiviral agent.
MeSH term(s)	Antiviral Agents/pharmacology ; Dengue/drug therapy ; Dengue/virology ; Dengue Virus/drug effects ; Dengue Virus/pathogenicity ; Endoplasmic Reticulum/drug effects ; Humans ; Proteostasis/drug effects ; Small Molecule Libraries/pharmacology ; Unfolded Protein Response/drug effects ; Virus Replication/drug effects ; Zika Virus/drug effects ; Zika Virus/pathogenicity ; Zika Virus Infection/drug therapy ; Zika Virus Infection/virology
Chemical Substances	Antiviral Agents ; Small Molecule Libraries
Language	English
Publishing date	2021-01-13
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.2012209118
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Article: Comparative multiplexed interactomics of SARS-CoV-2 and homologous coronavirus non-structural proteins identifies unique and shared host-cell dependencies.

Davies, Jonathan P / Almasy, Katherine M / McDonald, Eli F / Plate, Lars

bioRxiv : the preprint server for biology

2020

Abstract: Human coronaviruses (hCoV) have become a threat to global health and society, as evident from the SARS outbreak in 2002 caused by SARS-CoV-1 and the most recent COVID-19 pandemic caused by SARS-CoV-2. Despite high sequence similarity between SARS-CoV-1 ... ...

Abstract	Human coronaviruses (hCoV) have become a threat to global health and society, as evident from the SARS outbreak in 2002 caused by SARS-CoV-1 and the most recent COVID-19 pandemic caused by SARS-CoV-2. Despite high sequence similarity between SARS-CoV-1 and -2, each strain has distinctive virulence. A better understanding of the basic molecular mechanisms mediating changes in virulence is needed. Here, we profile the virus-host protein-protein interactions of two hCoV non-structural proteins (nsps) that are critical for virus replication. We use tandem mass tag-multiplexed quantitative proteomics to sensitively compare and contrast the interactomes of nsp2 and nsp4 from three betacoronavirus strains: SARS-CoV-1, SARS-CoV-2, and hCoV-OC43 - an endemic strain associated with the common cold. This approach enables the identification of both unique and shared host cell protein binding partners and the ability to further compare the enrichment of common interactions across homologs from related strains. We identify common nsp2 interactors involved in endoplasmic reticulum (ER) Ca
Keywords	covid19
Language	English
Publishing date	2020-07-14
Publishing country	United States
Document type	Preprint
DOI	10.1101/2020.07.13.201517
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Article ; Online: Comparative Multiplexed Interactomics of SARS-CoV-2 and Homologous Coronavirus Nonstructural Proteins Identifies Unique and Shared Host-Cell Dependencies.

Davies, Jonathan P / Almasy, Katherine M / McDonald, Eli F / Plate, Lars

ACS infectious diseases

2020 Volume 6, Issue 12, Page(s) 3174–3189

Abstract: Human coronaviruses (hCoVs) have become a threat to global health and society, as evident from the SARS outbreak in 2002 caused by SARS-CoV-1 and the most recent COVID-19 pandemic caused by SARS-CoV-2. Despite a high sequence similarity between SARS-CoV- ... ...

Abstract	Human coronaviruses (hCoVs) have become a threat to global health and society, as evident from the SARS outbreak in 2002 caused by SARS-CoV-1 and the most recent COVID-19 pandemic caused by SARS-CoV-2. Despite a high sequence similarity between SARS-CoV-1 and -2, each strain has a distinctive virulence. A better understanding of the basic molecular mechanisms mediating changes in virulence is needed. Here, we profile the virus-host protein-protein interactions of two hCoV nonstructural proteins (nsps) that are critical for virus replication. We use tandem mass tag-multiplexed quantitative proteomics to sensitively compare and contrast the interactomes of nsp2 and nsp4 from three betacoronavirus strains: SARS-CoV-1, SARS-CoV-2, and hCoV-OC43-an endemic strain associated with the common cold. This approach enables the identification of both unique and shared host cell protein binding partners and the ability to further compare the enrichment of common interactions across homologues from related strains. We identify common nsp2 interactors involved in endoplasmic reticulum (ER) Ca
MeSH term(s)	COVID-19/metabolism ; COVID-19/virology ; Coronavirus OC43, Human/pathogenicity ; Endoplasmic Reticulum/metabolism ; HEK293 Cells ; Host-Pathogen Interactions/genetics ; Humans ; Membrane Proteins/metabolism ; Mitochondria/metabolism ; Protein Binding ; Protein Interaction Maps/genetics ; Severe acute respiratory syndrome-related coronavirus/pathogenicity ; SARS-CoV-2/pathogenicity ; Severe Acute Respiratory Syndrome/metabolism ; Severe Acute Respiratory Syndrome/virology ; Transfection ; Viral Nonstructural Proteins/genetics ; Viral Nonstructural Proteins/metabolism ; Virulence/genetics ; Virus Replication/genetics
Chemical Substances	Membrane Proteins ; NSP4 protein, SARS-CoV-2 ; Viral Nonstructural Proteins ; nonstructural protein, coronavirus ; nsp2 protein, SARS-CoV-2
Language	English
Publishing date	2020-12-02
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ISSN	2373-8227
ISSN (online)	2373-8227
DOI	10.1021/acsinfecdis.0c00500
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Dengue and Zika virus infection are impaired by small molecule ER proteostasis regulator 147 in an ATF6-independent manner

Almasy, Katherine M. / Davies, Jonathan P. / Lisy, Samantha M. / Tirgar, Reyhaneh / Tran, Sirena C. / Plate, Lars

bioRxiv

Abstract: Flaviviruses, including Dengue and Zika, are widespread human pathogens, however, no broadly active therapeutics exist to fight infection. Here, we establish the recently discovered pharmacologic modulator of ER proteostasis 147 as an effective host- ... ...

Abstract	Flaviviruses, including Dengue and Zika, are widespread human pathogens, however, no broadly active therapeutics exist to fight infection. Here, we establish the recently discovered pharmacologic modulator of ER proteostasis 147 as an effective host-centered antiviral strategy. Compound 147 reduces infection by attenuating viral replication without causing toxicity in host cells. 147 is a preferential activator of the ATF6 pathway of the unfolded protein response, which requires targeting of cysteine residues primarily on protein disulfide isomerases (PDIs). We find that the antiviral activity of 147 is independent of ATF6 induction but does require modification of reactive thiols on protein targets. Targeting PDIs using RNAi and other PDI small molecule inhibitors was unable to recapitulate the antiviral effects, suggesting additional identified protein targets of 147 may mediate the activity. Importantly, 147 can impair infection of multiple strains of Dengue and Zika virus, indicating that it is suitable as a broad-spectrum antiviral agent.
Keywords	covid19
Publisher	BioRxiv
Document type	Article ; Online
DOI	10.1101/2020.05.15.098624
Database	COVID19

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Article ; Online: Comparative multiplexed interactomics of SARS-CoV-2 and homologous coronavirus non-structural proteins identifies unique and shared host-cell dependencies

Davies, Jonathan P / Almasy, Katherine M / McDonald, Eli F / Plate, Lars

bioRxiv

Abstract	Human coronaviruses (hCoV) have become a threat to global health and society, as evident from the SARS outbreak in 2002 caused by SARS-CoV-1 and the most recent COVID-19 pandemic caused by SARS-CoV-2. Despite high sequence similarity between SARS-CoV-1 and -2, each strain has distinctive virulence. A better understanding of the basic molecular mechanisms mediating changes in virulence is needed. Here, we profile the virus-host protein-protein interactions of two hCoV non-structural proteins (nsps) that are critical for virus replication. We use tandem mass tag-multiplexed quantitative proteomics to sensitively compare and contrast the interactomes of nsp2 and nsp4 from three betacoronavirus strains: SARS-CoV-1, SARS-CoV-2, and hCoV-OC43 - an endemic strain associated with the common cold. This approach enables the identification of both unique and shared host cell protein binding partners and the ability to further compare the enrichment of common interactions across homologs from related strains. We identify common nsp2 interactors involved in endoplasmic reticulum (ER) Ca2+ signaling and mitochondria biogenesis. We also identifiy nsp4 interactors unique to each strain, such as E3 ubiquitin ligase complexes for SARS-CoV-1 and ER homeostasis factors for SARS-CoV-2. Common nsp4 interactors include N-linked glycosylation machinery, unfolded protein response (UPR) associated proteins, and anti-viral innate immune signaling factors. Both nsp2 and nsp4 interactors are strongly enriched in proteins localized at mitochondrial-associated ER membranes suggesting a new functional role for modulating host processes, such as calcium homeostasis, at these organelle contact sites. Our results shed light on the role these hCoV proteins play in the infection cycle, as well as host factors that may mediate the divergent pathogenesis of OC43 from SARS strains. Our mass spectrometry workflow enables rapid and robust comparisons of multiple bait proteins, which can be applied to additional viral proteins. Furthermore, the identified common interactions may present new targets for exploration by host-directed anti-viral therapeutics.
Keywords	covid19
Language	English
Publishing date	2020-07-15
Publisher	Cold Spring Harbor Laboratory
Document type	Article ; Online
DOI	10.1101/2020.07.13.201517
Database	COVID19

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Article ; Online: Similar Rates of Deleterious Copy Number Variants in Early-Onset Psychosis and Autism Spectrum Disorder.

Brownstein, Catherine A / Douard, Elise / Mollon, Josephine / Smith, Richard / Hojlo, Margaret A / Das, Ananth / Goldman, Maria / Garvey, Emily / Cabral, Kristin / Li, Jianqiao / Bowen, Joshua / Rao, Abhijit S / Genetti, Casie / Carroll, Devon / Knowles, Emma E M / Deaso, Emma / Agrawal, Pankaj B / Beggs, Alan H / D'Angelo, Eugene /

Almasy, Laura / Alexander-Bloch, Aaron / Saci, Zohra / Moreau, Clara A / Huguet, Guillaume / Deo, Anthony J / Jacquemont, Sébastien / Glahn, David C / Gonzalez-Heydrich, Joseph

The American journal of psychiatry

2022 Volume 179, Issue 11, Page(s) 853–861

Abstract: Objective: Copy number variants (CNVs) are strongly associated with neurodevelopmental and psychotic disorders. Early-onset psychosis (EOP), where symptoms appear before 18 years of age, is thought to be more strongly influenced by genetic factors than ... ...

Abstract	Objective: Copy number variants (CNVs) are strongly associated with neurodevelopmental and psychotic disorders. Early-onset psychosis (EOP), where symptoms appear before 18 years of age, is thought to be more strongly influenced by genetic factors than adult-onset psychotic disorders. However, the prevalence and effect of CNVs in EOP is unclear. Methods: The authors documented the prevalence of recurrent CNVs and the functional impact of deletions and duplications genome-wide in 137 children and adolescents with EOP compared with 5,540 individuals with autism spectrum disorder (ASD) and 16,504 population control subjects. Specifically, the frequency of 47 recurrent CNVs previously associated with neurodevelopmental and neuropsychiatric illnesses in each cohort were compared. Next, CNV risk scores (CRSs), indices reflecting the dosage sensitivity for any gene across the genome that is encapsulated in a deletion or duplication separately, were compared between groups. Results: The prevalence of recurrent CNVs was significantly higher in the EOP group than in the ASD (odds ratio=2.30) and control (odds ratio=5.06) groups. However, the difference between the EOP and ASD groups was attenuated when EOP participants with co-occurring ASD were excluded. CRS was significantly higher in the EOP group compared with the control group for both deletions (odds ratio=1.30) and duplications (odds ratio=1.09). In contrast, the EOP and ASD groups did not differ significantly in terms of CRS. Conclusions: Given the high frequency of recurrent CNVs in the EOP group and comparable CRSs in the EOP and ASD groups, the findings suggest that all children and adolescents with a psychotic diagnosis should undergo genetic screening, as is recommended in ASD.
MeSH term(s)	Child ; Adolescent ; Adult ; Humans ; DNA Copy Number Variations/genetics ; Autism Spectrum Disorder/epidemiology ; Autism Spectrum Disorder/genetics ; Psychotic Disorders/epidemiology ; Psychotic Disorders/genetics ; Cohort Studies ; Odds Ratio
Language	English
Publishing date	2022-08-24
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	280045-7
ISSN	1535-7228 ; 0002-953X
ISSN (online)	1535-7228
ISSN	0002-953X
DOI	10.1176/appi.ajp.21111175
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Article ; Online: A multimodal assessment of the genetic control over working memory.

Karlsgodt, Katherine H / Kochunov, Peter / Winkler, Anderson M / Laird, Angela R / Almasy, Laura / Duggirala, Ravindranath / Olvera, Rene L / Fox, Peter T / Blangero, John / Glahn, David C

The Journal of neuroscience : the official journal of the Society for Neuroscience

2010 Volume 30, Issue 24, Page(s) 8197–8202

Abstract: Working memory performance is significantly influenced by genetic factors. Here, we assessed genetic contributions to both working memory performance and neuroimaging measures focused on the network of brain regions associated with working memory by ... ...

Abstract	Working memory performance is significantly influenced by genetic factors. Here, we assessed genetic contributions to both working memory performance and neuroimaging measures focused on the network of brain regions associated with working memory by using a sample of 467 human participants from extended families. Imaging measures included diffusion tensor imaging indices in major white matter tracts thought to be associated with working memory and structural magnetic resonance imaging measures of frontal and parietal gray matter density. Analyses directly addressed whether working memory performance and neural structural integrity are influenced by common genetic factors (e.g., pleiotropy). While all cognitive measures, gray matter regions, and white matter tracts assessed were heritable, only performance on a spatial delayed response task and integrity of the superior longitudinal fasciculus (a primary fronto-parietal connection) shared genetic factors. As working memory may be a core component of other higher level processes, such as general intelligence, this finding has implications for the heritability of complex cognitive functions, as well as for our understanding of the transmission of cognitive deficits in mental and neurological disorders.
MeSH term(s)	Adult ; Aged ; Aged, 80 and over ; Anisotropy ; Brain/anatomy & histology ; Brain/blood supply ; Brain/physiology ; Brain Mapping ; Diffusion Magnetic Resonance Imaging ; Female ; Humans ; Image Processing, Computer-Assisted/methods ; Magnetic Resonance Imaging/methods ; Male ; Memory, Short-Term/physiology ; Mexican Americans/genetics ; Middle Aged ; Nerve Fibers, Myelinated/physiology ; Neural Pathways ; Neuropsychological Tests ; Oxygen/blood ; Pedigree ; Young Adult
Chemical Substances	Oxygen (S88TT14065)
Language	English
Publishing date	2010-06-16
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	604637-x
ISSN	1529-2401 ; 0270-6474
ISSN (online)	1529-2401
ISSN	0270-6474
DOI	10.1523/JNEUROSCI.0359-10.2010
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