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Article ; Online: Family screening for bicuspid aortic valve and aortic dilatation: a meta-analysis.

Bray, Jonathan J H / Freer, Rosie / Pitcher, Alex / Kharbanda, Rajesh

2023 Volume 44, Issue 33, Page(s) 3152–3164

Abstract: Aims: International guidelines recommend screening of first-degree relatives (FDR) of people with bicuspid aortic valves (BAVs). However, the prevalence of BAV and of aortic dilatation amongst family members is uncertain.: Methods and results: A ... ...

Abstract	Aims: International guidelines recommend screening of first-degree relatives (FDR) of people with bicuspid aortic valves (BAVs). However, the prevalence of BAV and of aortic dilatation amongst family members is uncertain. Methods and results: A systematic review and meta-analysis of original reports of screening for BAV. Databases including MEDLINE, Embase, and Cochrane CENTRAL were searched from inception to December 2021 using relevant search terms. Data were sought on the screened prevalence of BAV and aortic dilatation. The protocol was specified prior to the searches being performed, and standard meta-analytic techniques were used. Twenty-three observational studies met inclusion criteria (n = 2297 index cases; n = 6054 screened relatives). The prevalence of BAV amongst relatives was 7.3% [95% confidence interval (CI) 6.1%-8.6%] overall and per family was 23.6% (95% CI 18.1%-29.5%). The prevalence of aortic dilatation amongst relatives was 9.4% (95% CI 5.7%-13.9%). Whilst the prevalence of aortic dilatation was particularly high in relatives with BAV (29.2%; 95% CI 15.3%-45.1%), aortic dilatation alongside tricuspid aortic valves was a more frequent finding, as there were many more family members with tricuspid valves than BAV. The prevalence estimate amongst relatives with tricuspid valves (7.0%; 95% CI 3.2%-12.0%) was higher than reported in the general population. Conclusion: Screening family members of people with BAV can identify a cohort substantially enriched for the presence of bicuspid valve, aortic enlargement, or both. The implications for screening programmes are discussed, including in particular the substantial current uncertainties regarding the clinical implications of aortic findings.
MeSH term(s)	Humans ; Bicuspid Aortic Valve Disease ; Heart Valve Diseases/epidemiology ; Heart Valve Diseases/genetics ; Heart Valve Diseases/diagnosis ; Dilatation ; Aortic Valve ; Aortic Diseases/diagnosis ; Dilatation, Pathologic/epidemiology ; Retrospective Studies
Language	English
Publishing date	2023-06-07
Publishing country	England
Document type	Systematic Review ; Meta-Analysis ; Journal Article
ZDB-ID	603098-1
ISSN	1522-9645 ; 0195-668X
ISSN (online)	1522-9645
ISSN	0195-668X
DOI	10.1093/eurheartj/ehad320
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Article ; Online: An assessment of adherence to CARE reporting standards by case reports published in

Freer, Rosie / Rowett, Alexandra / Camm, C Fielder

European heart journal. Case reports

2020 Volume 4, Issue 5, Page(s) 1–5

Abstract: Background: Case reports are subject to significant variation in their content, and the absence of pertinent case details can limit their benefit to the medical community. To aid this, a reporting standard (CARE) has been developed. Case reports ... ...

Abstract	Background: Case reports are subject to significant variation in their content, and the absence of pertinent case details can limit their benefit to the medical community. To aid this, a reporting standard (CARE) has been developed. Case reports published in Methods: Case reports published in Results: In 2018, 130 case reports/series were published by Conclusions: There was good compliance with the CARE reporting standards by case reports published in
Keywords	covid19
Language	English
Publishing date	2020-09-26
Publishing country	England
Document type	Journal Article
ISSN	2514-2119
ISSN (online)	2514-2119
DOI	10.1093/ehjcr/ytaa251
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Article ; Online: Clinical support during COVID-19: An opportunity for service and learning? A cross-sectional survey of UK medical students.

Medical teacher

2023 Volume 45, Issue 8, Page(s) 859–870

Abstract: Purpose: Medical students providing support to clinical teams during Covid-19 may have been an opportunity for service and learning. We aimed to understand why the reported educational impact has been mixed to inform future placements.: Methods: We ... ...

Abstract	Purpose: Medical students providing support to clinical teams during Covid-19 may have been an opportunity for service and learning. We aimed to understand why the reported educational impact has been mixed to inform future placements. Methods: We conducted a cross-sectional survey of medical students at UK medical schools during the first Covid-19 'lockdown' period in the UK (March-July 2020). Analysis was informed by the conceptual framework of service and learning. Results: 1245 medical students from 37 UK medical schools responded. 57% of respondents provided clinical support across a variety of roles and reported benefits including increased preparedness for foundation year one compared to those who did not ( Conclusion: The conceptual framework of service and learning can help explain why student experiences have been heterogeneous. We highlight how this conceptual framework can be used to inform clinical placements in the future, in particular the risks, benefits, and structures.[Box: see text].
MeSH term(s)	Humans ; COVID-19/epidemiology ; Students, Medical ; Cross-Sectional Studies ; Learning ; United Kingdom/epidemiology
Language	English
Publishing date	2023-03-16
Publishing country	England
Document type	Journal Article
ZDB-ID	424426-6
ISSN	1466-187X ; 0142-159X
ISSN (online)	1466-187X
ISSN	0142-159X
DOI	10.1080/0142159X.2023.2184235
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Article: Supersaturated proteins are enriched at synapses and underlie cell and tissue vulnerability in Alzheimer's disease

Freer, Rosie / Sormanni, Pietro / Ciryam, Prajwal / Rammner, Burkhard / Rizzoli, Silvio O / Dobson, Christopher M / Vendruscolo, Michele

Heliyon. 2019 Nov., v. 5, no. 11

2019

Abstract: Neurodegenerative disorders progress across the brain in characteristic spatio-temporal patterns. A better understanding of the factors underlying the specific cell and tissue vulnerability responsible for such patterns could help identify the molecular ... ...

Abstract	Neurodegenerative disorders progress across the brain in characteristic spatio-temporal patterns. A better understanding of the factors underlying the specific cell and tissue vulnerability responsible for such patterns could help identify the molecular origins of these conditions. To investigate these factors, based on the observation that neurodegenerative disorders are closely associated with the presence of aberrant protein deposits, we made the hypothesis that the vulnerability of cells and tissues is associated to the overall levels of supersaturated proteins, which are those most metastable against aggregation. By analyzing single-cell transcriptomic and subcellular proteomics data on healthy brains of ages much younger than those typical of disease onset, we found that the most supersaturated proteins are enriched in cells and tissues that succumb first to neurodegeneration. Then, by focusing the analysis on a metastable subproteome specific to Alzheimer's disease, we show that it is possible to recapitulate the pattern of disease progression using data from healthy brains. We found that this metastable subproteome is significantly enriched for synaptic processes and mitochondrial energy metabolism, thus rendering the synaptic environment dangerous for aggregation. The present identification of protein supersaturation as a signature of cell and tissue vulnerability in neurodegenerative disorders could facilitate the search for effective treatments by providing clearer points of intervention.
Keywords	Alzheimer disease ; brain ; disease progression ; energy metabolism ; mitochondria ; neurodegenerative diseases ; proteomics ; transcriptomics
Language	English
Dates of publication	2019-11
Publishing place	Elsevier Ltd
Document type	Article
Note	NAL-AP-2-clean
ZDB-ID	2835763-2
ISSN	2405-8440
ISSN	2405-8440
DOI	10.1016/j.heliyon.2019.e02589
Database	NAL-Catalogue (AGRICOLA)

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Article: Supersaturated proteins are enriched at synapses and underlie cell and tissue vulnerability in Alzheimer's disease.

Freer, Rosie / Sormanni, Pietro / Ciryam, Prajwal / Rammner, Burkhard / Rizzoli, Silvio O / Dobson, Christopher M / Vendruscolo, Michele

Heliyon

2019 Volume 5, Issue 11, Page(s) e02589

Abstract	Neurodegenerative disorders progress across the brain in characteristic spatio-temporal patterns. A better understanding of the factors underlying the specific cell and tissue vulnerability responsible for such patterns could help identify the molecular origins of these conditions. To investigate these factors, based on the observation that neurodegenerative disorders are closely associated with the presence of aberrant protein deposits, we made the hypothesis that the vulnerability of cells and tissues is associated to the overall levels of supersaturated proteins, which are those most metastable against aggregation. By analyzing single-cell transcriptomic and subcellular proteomics data on healthy brains of ages much younger than those typical of disease onset, we found that the most supersaturated proteins are enriched in cells and tissues that succumb first to neurodegeneration. Then, by focusing the analysis on a metastable subproteome specific to Alzheimer's disease, we show that it is possible to recapitulate the pattern of disease progression using data from healthy brains. We found that this metastable subproteome is significantly enriched for synaptic processes and mitochondrial energy metabolism, thus rendering the synaptic environment dangerous for aggregation. The present identification of protein supersaturation as a signature of cell and tissue vulnerability in neurodegenerative disorders could facilitate the search for effective treatments by providing clearer points of intervention.
Language	English
Publishing date	2019-11-19
Publishing country	England
Document type	Journal Article
ZDB-ID	2835763-2
ISSN	2405-8440
ISSN	2405-8440
DOI	10.1016/j.heliyon.2019.e02589
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Article ; Online: Supersaturated proteins are enriched at synapses and underlie cell and tissue vulnerability in Alzheimer's disease

Rosie Freer / Pietro Sormanni / Prajwal Ciryam / Burkhard Rammner / Silvio O. Rizzoli / Christopher M. Dobson / Michele Vendruscolo

Heliyon, Vol 5, Iss 11, Pp e02589- (2019)

2019

Abstract	Neurodegenerative disorders progress across the brain in characteristic spatio-temporal patterns. A better understanding of the factors underlying the specific cell and tissue vulnerability responsible for such patterns could help identify the molecular origins of these conditions. To investigate these factors, based on the observation that neurodegenerative disorders are closely associated with the presence of aberrant protein deposits, we made the hypothesis that the vulnerability of cells and tissues is associated to the overall levels of supersaturated proteins, which are those most metastable against aggregation. By analyzing single-cell transcriptomic and subcellular proteomics data on healthy brains of ages much younger than those typical of disease onset, we found that the most supersaturated proteins are enriched in cells and tissues that succumb first to neurodegeneration. Then, by focusing the analysis on a metastable subproteome specific to Alzheimer's disease, we show that it is possible to recapitulate the pattern of disease progression using data from healthy brains. We found that this metastable subproteome is significantly enriched for synaptic processes and mitochondrial energy metabolism, thus rendering the synaptic environment dangerous for aggregation. The present identification of protein supersaturation as a signature of cell and tissue vulnerability in neurodegenerative disorders could facilitate the search for effective treatments by providing clearer points of intervention.
Keywords	Biophysics ; Neuroscience ; Alzheimer's disease ; Protein supersaturation ; Neuronal vulnerability ; Protein homeostasis ; Science (General) ; Q1-390 ; Social sciences (General) ; H1-99
Subject code	612
Language	English
Publishing date	2019-11-01T00:00:00Z
Publisher	Elsevier
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: A protein homeostasis signature in healthy brains recapitulates tissue vulnerability to Alzheimer's disease.

Freer, Rosie / Sormanni, Pietro / Vecchi, Giulia / Ciryam, Prajwal / Dobson, Christopher M / Vendruscolo, Michele

Science advances

2016 Volume 2, Issue 8, Page(s) e1600947

Abstract: In Alzheimer's disease, aggregates of Aβ and tau in amyloid plaques and neurofibrillary tangles spread progressively across brain tissues following a characteristic pattern, implying a tissue-specific vulnerability to the disease. We report a ... ...

Abstract	In Alzheimer's disease, aggregates of Aβ and tau in amyloid plaques and neurofibrillary tangles spread progressively across brain tissues following a characteristic pattern, implying a tissue-specific vulnerability to the disease. We report a transcriptional analysis of healthy brains and identify an expression signature that predicts-at ages well before the typical onset-the tissue-specific progression of the disease. We obtain this result by finding a quantitative correlation between the histopathological staging of the disease and the expression patterns of the proteins that coaggregate in amyloid plaques and neurofibrillary tangles, together with those of the protein homeostasis components that regulate Aβ and tau. Because this expression signature is evident in healthy brains, our analysis provides an explanatory link between a tissue-specific environmental risk of protein aggregation and a corresponding vulnerability to Alzheimer's disease.
MeSH term(s)	Adult ; Alzheimer Disease/genetics ; Alzheimer Disease/metabolism ; Alzheimer Disease/pathology ; Amyloid beta-Peptides/biosynthesis ; Amyloid beta-Peptides/genetics ; Brain/metabolism ; Brain/pathology ; Brain Mapping ; Disease Progression ; Homeostasis ; Humans ; Middle Aged ; Neurofibrillary Tangles/metabolism ; Neurofibrillary Tangles/pathology ; Organ Specificity ; Plaque, Amyloid/metabolism ; Plaque, Amyloid/pathology ; Protein Aggregation, Pathological/genetics ; Transcriptome ; tau Proteins/biosynthesis ; tau Proteins/genetics
Chemical Substances	Amyloid beta-Peptides ; tau Proteins
Language	English
Publishing date	2016
Publishing country	United States
Document type	Journal Article
ZDB-ID	2810933-8
ISSN	2375-2548 ; 2375-2548
ISSN (online)	2375-2548
ISSN	2375-2548
DOI	10.1126/sciadv.1600947
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Article ; Online: A transcriptional signature of Alzheimer's disease is associated with a metastable subproteome at risk for aggregation.

Ciryam, Prajwal / Kundra, Rishika / Freer, Rosie / Morimoto, Richard I / Dobson, Christopher M / Vendruscolo, Michele

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

2016 Volume 113, Issue 17, Page(s) 4753–4758

Abstract: It is well-established that widespread transcriptional changes accompany the onset and progression of Alzheimer's disease. Because of the multifactorial nature of this neurodegenerative disorder and its complex relationship with aging, however, it ... ...

Abstract	It is well-established that widespread transcriptional changes accompany the onset and progression of Alzheimer's disease. Because of the multifactorial nature of this neurodegenerative disorder and its complex relationship with aging, however, it remains unclear whether such changes are the result of nonspecific dysregulation and multisystem failure or instead are part of a coordinated response to cellular dysfunction. To address this problem in a systematic manner, we performed a meta-analysis of about 1,600 microarrays from human central nervous system tissues to identify transcriptional changes upon aging and as a result of Alzheimer's disease. Our strategy to discover a transcriptional signature of Alzheimer's disease revealed a set of down-regulated genes that encode proteins metastable to aggregation. Using this approach, we identified a small number of biochemical pathways, notably oxidative phosphorylation, enriched in proteins vulnerable to aggregation in control brains and encoded by genes down-regulated in Alzheimer's disease. These results suggest that the down-regulation of a metastable subproteome may help mitigate aberrant protein aggregation when protein homeostasis becomes compromised in Alzheimer's disease.
MeSH term(s)	Aged ; Aging/metabolism ; Alzheimer Disease/metabolism ; Brain/metabolism ; Female ; Gene Expression Profiling ; Gene Expression Regulation, Developmental ; Humans ; Nerve Tissue Proteins/metabolism ; Protein Aggregation, Pathological/metabolism ; Proteome/metabolism ; Transcriptome
Chemical Substances	Nerve Tissue Proteins ; Proteome
Language	English
Publishing date	2016-04-26
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.1516604113
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Article ; Online: A tau homeostasis signature is linked with the cellular and regional vulnerability of excitatory neurons to tau pathology.

Fu, Hongjun / Possenti, Andrea / Freer, Rosie / Nakano, Yoshikazu / Hernandez Villegas, Nancy C / Tang, Maoping / Cauhy, Paula V M / Lassus, Benjamin A / Chen, Shuo / Fowler, Stephanie L / Figueroa, Helen Y / Huey, Edward D / Johnson, Gail V W / Vendruscolo, Michele / Duff, Karen E

Nature neuroscience

2018 Volume 22, Issue 1, Page(s) 47–56

Abstract: Excitatory neurons are preferentially impaired in early Alzheimer's disease but the pathways contributing to their relative vulnerability remain largely unknown. Here we report that pathological tau accumulation takes place predominantly in excitatory ... ...

Abstract	Excitatory neurons are preferentially impaired in early Alzheimer's disease but the pathways contributing to their relative vulnerability remain largely unknown. Here we report that pathological tau accumulation takes place predominantly in excitatory neurons compared to inhibitory neurons, not only in the entorhinal cortex, a brain region affected in early Alzheimer's disease, but also in areas affected later by the disease. By analyzing RNA transcripts from single-nucleus RNA datasets, we identified a specific tau homeostasis signature of genes differentially expressed in excitatory compared to inhibitory neurons. One of the genes, BCL2-associated athanogene 3 (BAG3), a facilitator of autophagy, was identified as a hub, or master regulator, gene. We verified that reducing BAG3 levels in primary neurons exacerbated pathological tau accumulation, whereas BAG3 overexpression attenuated it. These results define a tau homeostasis signature that underlies the cellular and regional vulnerability of excitatory neurons to tau pathology.
MeSH term(s)	Adaptor Proteins, Signal Transducing/metabolism ; Alzheimer Disease/genetics ; Alzheimer Disease/metabolism ; Alzheimer Disease/pathology ; Animals ; Apoptosis Regulatory Proteins/metabolism ; Brain/metabolism ; Brain/pathology ; Homeostasis/physiology ; Humans ; Mice ; Mice, Transgenic ; Neurons/metabolism ; Neurons/pathology ; tau Proteins/genetics ; tau Proteins/metabolism
Chemical Substances	Adaptor Proteins, Signal Transducing ; Apoptosis Regulatory Proteins ; BAG3 protein, human ; tau Proteins
Language	English
Publishing date	2018-12-17
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1420596-8
ISSN	1546-1726 ; 1097-6256
ISSN (online)	1546-1726
ISSN	1097-6256
DOI	10.1038/s41593-018-0298-7
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Article ; Online: Spinal motor neuron protein supersaturation patterns are associated with inclusion body formation in ALS.

Ciryam, Prajwal / Lambert-Smith, Isabella A / Bean, Daniel M / Freer, Rosie / Cid, Fernando / Tartaglia, Gian Gaetano / Saunders, Darren N / Wilson, Mark R / Oliver, Stephen G / Morimoto, Richard I / Dobson, Christopher M / Vendruscolo, Michele / Favrin, Giorgio / Yerbury, Justin J

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

2017 Volume 114, Issue 20, Page(s) E3935–E3943

Abstract: Amyotrophic lateral sclerosis (ALS) is a heterogeneous degenerative motor neuron disease linked to numerous genetic mutations in apparently unrelated proteins. These proteins, including SOD1, TDP-43, and FUS, are highly aggregation-prone and form a ... ...

Abstract	Amyotrophic lateral sclerosis (ALS) is a heterogeneous degenerative motor neuron disease linked to numerous genetic mutations in apparently unrelated proteins. These proteins, including SOD1, TDP-43, and FUS, are highly aggregation-prone and form a variety of intracellular inclusion bodies that are characteristic of different neuropathological subtypes of the disease. Contained within these inclusions are a variety of proteins that do not share obvious characteristics other than coaggregation. However, recent evidence from other neurodegenerative disorders suggests that disease-affected biochemical pathways can be characterized by the presence of proteins that are supersaturated, with cellular concentrations significantly greater than their solubilities. Here, we show that the proteins that form inclusions of mutant SOD1, TDP-43, and FUS are not merely a subset of the native interaction partners of these three proteins, which are themselves supersaturated. To explain the presence of coaggregating proteins in inclusions in the brain and spinal cord, we observe that they have an average supersaturation even greater than the average supersaturation of the native interaction partners in motor neurons, but not when scores are generated from an average of other human tissues. These results suggest that inclusion bodies in various forms of ALS result from a set of proteins that are metastable in motor neurons, and thus prone to aggregation upon a disease-related progressive collapse of protein homeostasis in this specific setting.
MeSH term(s)	Amyotrophic Lateral Sclerosis/genetics ; Amyotrophic Lateral Sclerosis/metabolism ; Amyotrophic Lateral Sclerosis/physiopathology ; Brain/metabolism ; DNA-Binding Proteins/metabolism ; Humans ; Inclusion Bodies/metabolism ; Inclusion Bodies/physiology ; Motor Neurons/metabolism ; Mutation ; Protein Aggregates/physiology ; Protein Aggregation, Pathological/metabolism ; Protein Aggregation, Pathological/physiopathology ; Protein Folding ; RNA-Binding Protein FUS/metabolism ; Spinal Cord/metabolism ; Spinal Nerves/metabolism ; Spinal Nerves/physiopathology ; Superoxide Dismutase/metabolism ; Superoxide Dismutase-1/genetics
Chemical Substances	DNA-Binding Proteins ; FUS protein, human ; Protein Aggregates ; RNA-Binding Protein FUS ; TARDBP protein, human ; Superoxide Dismutase (EC 1.15.1.1) ; Superoxide Dismutase-1 (EC 1.15.1.1)
Language	English
Publishing date	2017-04-10
Publishing country	United States
Document type	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	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.1613854114
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