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Article: After tough year, M&A market begins to rebound.

Goedert, Joseph

Health data management

2010 Volume 18, Issue 6, Page(s) 42–6, 48, 50 passim

MeSH term(s)	Commerce/trends ; Information Systems ; Organizational Affiliation/trends ; United States
Language	English
Publishing date	2010-06
Publishing country	United States
Document type	Journal Article
ISSN	1079-9869
ISSN	1079-9869
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Article ; Online: Immunoglobulin M seropositivity for Toscana virus in a random population sample in Sicily.

Amodio, Emanuele / Cusi, Maria Grazia / Valenti, Rosalia Maria / Valentini, Melissa / Mammina, Caterina / Gori-Savellini, Gianni / Vitale, Francesco / Romano, Nino / Goedert, James J / Calamusa, Giuseppe

International journal of infectious diseases : IJID : official publication of the International Society for Infectious Diseases

2012 Volume 16, Issue 8, Page(s) e633–5

Abstract: Objectives: High Toscana virus (TOSV) antibody seropositivity rates have been documented in the last decade, especially in the Mediterranean area. It is unclear if these rates are associated with a recent or past exposure to the virus. This is of ... ...

Abstract	Objectives: High Toscana virus (TOSV) antibody seropositivity rates have been documented in the last decade, especially in the Mediterranean area. It is unclear if these rates are associated with a recent or past exposure to the virus. This is of importance, as primary infection can cause neurologic complications, especially in adults. The aim of the present study was to assess the current active TOSV circulation in western Sicily. Methods: A cross-sectional seroprevalence study was conducted on 271 individuals aged 4-92 years, sampled from the general population of a small city. Each participant completed a self-administered questionnaire and provided serum, which was analyzed for the presence of specific anti-TOSV IgM and IgG. Results: Anti-TOSV IgM was detected in eight (3.0%) participants, of whom only three had anti-TOSV IgG. The prevalence of anti-TOSV IgM was highest in subjects aged 25-34 and 35-44 years (7.1% and 4.8%, respectively). All subjects positive for anti-TOSV IgM were resident in the suburban area. Conclusions: The detection of IgM documented the circulation of TOSV, a Phlebovirus, in a random population sample of Sicilian adults. The highest risk of TOSV seroconversion in subjects living in the suburbs appears to suggest a high density of TOSV vectors in peri-urban areas.
MeSH term(s)	Adolescent ; Adult ; Aged ; Aged, 80 and over ; Antibodies, Viral/blood ; Bunyaviridae Infections/epidemiology ; Bunyaviridae Infections/immunology ; Child ; Child, Preschool ; Cross-Sectional Studies ; Female ; Humans ; Immunoglobulin G/blood ; Immunoglobulin G/immunology ; Immunoglobulin M/blood ; Male ; Middle Aged ; Sandfly fever Naples virus/immunology ; Seroepidemiologic Studies ; Sicily/epidemiology ; Young Adult
Chemical Substances	Antibodies, Viral ; Immunoglobulin G ; Immunoglobulin M
Language	English
Publishing date	2012-06-21
Publishing country	Canada
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1331197-9
ISSN	1878-3511 ; 1201-9712
ISSN (online)	1878-3511
ISSN	1201-9712
DOI	10.1016/j.ijid.2012.04.012
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Article ; Online: Racism in the Countertransference.

Goedert, Mead

The Psychoanalytic quarterly

2022 Volume 89, Issue 4, Page(s) 715–740

Abstract: This paper examines racialized countertransferences and how these countertransferences impact treatment dyads. I explicate the ways in which clinicians may unconsciously avoid racialized dynamics within themselves and within treatments. Case examples are ...

Abstract	This paper examines racialized countertransferences and how these countertransferences impact treatment dyads. I explicate the ways in which clinicians may unconsciously avoid racialized dynamics within themselves and within treatments. Case examples are used to portray how race manifests within countertransference and how we might understand these types of countertransference reactions. Finally, I encourage further reflectiveness and openness related to race within ourselves and within our treatments.
Language	English
Publishing date	2022-03-21
Publishing country	United States
Document type	Journal Article
ZDB-ID	207522-2
ISSN	2167-4086 ; 0033-2828
ISSN (online)	2167-4086
ISSN	0033-2828
DOI	10.1080/00332828.2020.1805270
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Article ; Online: Cryo-EM structures of τ filaments from human brain.

Goedert, Michel

Essays in biochemistry

2021 Volume 65, Issue 7, Page(s) 949–959

Abstract: Electron cryo-microscopy (cryo-EM) has made it possible to determine near-atomic structures of τ filaments from human brain. Previous work had shown that the cores of paired helical and straight filaments of Alzheimer's disease are made of two identical, ...

Abstract	Electron cryo-microscopy (cryo-EM) has made it possible to determine near-atomic structures of τ filaments from human brain. Previous work had shown that the cores of paired helical and straight filaments of Alzheimer's disease are made of two identical, but differently arranged C-shaped protofilaments. In recent years, cryo-EM has shown that the Alzheimer τ fold is 79 amino acids long. Five of the eight β-strands give rise to two antiparallel β-sheets, with the other three forming a β-helix. High-affinity binding sites of positron emission tomography ligand APN-1607 (PM-PBB3) are in the β-helix region. The Alzheimer fold contrasts with the 94 amino acid-long Pick fold, which is J-shaped and comprises nine β-strands that give rise to four antiparallel β-sheets, in the absence of a β-helix. Chronic traumatic encephalopathy τ fold is similar to the Alzheimer fold, but differs in the β-helix region, which is larger and contains a non-proteinaceous density that is probably hydrophobic. These folds are mostly two-layered. By contrast, the 107 amino acid τ fold of the 4R tauopathy corticobasal degeneration is four-layered and comprises 11 β-strands. It contains an internal, probably hydrophilic, density that is surrounded by τ. The τ folds described here share the presence of microtubule-binding repeats 3 and 4, as well as 10-13 amino acids after repeat 4.
MeSH term(s)	Alzheimer Disease/metabolism ; Brain/metabolism ; Cryoelectron Microscopy ; Humans ; Tauopathies/metabolism ; tau Proteins/chemistry ; tau Proteins/metabolism
Chemical Substances	tau Proteins
Language	English
Publishing date	2021-11-30
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1744-1358 ; 0071-1365
ISSN (online)	1744-1358
ISSN	0071-1365
DOI	10.1042/EBC20210025
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Article: Immunoglobulin M seropositivity for Toscana virus in a random population sample in Sicily

International journal of infectious diseases. 2012 Aug., v. 16, no. 8

2012

Abstract: OBJECTIVES: High Toscana virus (TOSV) antibody seropositivity rates have been documented in the last decade, especially in the Mediterranean area. It is unclear if these rates are associated with a recent or past exposure to the virus. This is of ... ...

Abstract	OBJECTIVES: High Toscana virus (TOSV) antibody seropositivity rates have been documented in the last decade, especially in the Mediterranean area. It is unclear if these rates are associated with a recent or past exposure to the virus. This is of importance, as primary infection can cause neurologic complications, especially in adults. The aim of the present study was to assess the current active TOSV circulation in western Sicily. METHODS: A cross-sectional seroprevalence study was conducted on 271 individuals aged 4–92 years, sampled from the general population of a small city. Each participant completed a self-administered questionnaire and provided serum, which was analyzed for the presence of specific anti-TOSV IgM and IgG. RESULTS: Anti-TOSV IgM was detected in eight (3.0%) participants, of whom only three had anti-TOSV IgG. The prevalence of anti-TOSV IgM was highest in subjects aged 25–34 and 35–44 years (7.1% and 4.8%, respectively). All subjects positive for anti-TOSV IgM were resident in the suburban area. CONCLUSIONS: The detection of IgM documented the circulation of TOSV, a Phlebovirus, in a random population sample of Sicilian adults. The highest risk of TOSV seroconversion in subjects living in the suburbs appears to suggest a high density of TOSV vectors in peri-urban areas.
Keywords	risk ; immunoglobulin G ; immunoglobulin M ; questionnaires ; blood serum ; seroprevalence ; Sandfly fever Naples phlebovirus ; antibodies ; suburban areas ; viruses ; seroconversion ; adults ; Sicily ; Mediterranean region
Language	English
Dates of publication	2012-08
Size	p. e633-e635.
Publishing place	Elsevier Ltd
Document type	Article
Note	2019-12-06
ZDB-ID	1331197-9
ISSN	1878-3511 ; 1201-9712
ISSN (online)	1878-3511
ISSN	1201-9712
DOI	10.1016/j.ijid.2012.04.012
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Tau proteinopathies and the prion concept.

Goedert, Michel

Progress in molecular biology and translational science

2020 Volume 175, Page(s) 239–259

Abstract: The ordered assembly of a small number of proteins into amyloid filaments is central to age-related neurodegenerative diseases. Tau is the most commonly affected of these proteins. In sporadic diseases, assemblies of tau form in a stochastic manner in ... ...

Abstract	The ordered assembly of a small number of proteins into amyloid filaments is central to age-related neurodegenerative diseases. Tau is the most commonly affected of these proteins. In sporadic diseases, assemblies of tau form in a stochastic manner in certain brain regions, from where they appear to spread in a deterministic way, giving rise to disease symptoms. Over the past decade, multiple lines of evidence have shown that assembled tau behaves like a prion. More recently, electron cryo-microscopy of tau filaments has shown that distinct conformers are present in different diseases, with no inter-individual variation for a given disease.
MeSH term(s)	Amino Acid Sequence ; Animals ; Brain/pathology ; Humans ; Neurodegenerative Diseases/pathology ; Phenotype ; Prions/metabolism ; Tauopathies/pathology ; tau Proteins/chemistry ; tau Proteins/genetics ; tau Proteins/metabolism
Chemical Substances	Prions ; tau Proteins
Language	English
Publishing date	2020-09-08
Publishing country	Netherlands
Document type	Journal Article ; Review
ZDB-ID	2471995-X
ISSN	1878-0814 ; 0079-6603 ; 1877-1173
ISSN (online)	1878-0814
ISSN	0079-6603 ; 1877-1173
DOI	10.1016/bs.pmbts.2020.08.003
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Uc I Zs 357: Show issues

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Article ; Online: Aaron Klug and the study of Alzheimer's disease.

Goedert, Michel

Alzheimer's & dementia : the journal of the Alzheimer's Association

2019 Volume 15, Issue 6, Page(s) 859–861

Language	English
Publishing date	2019-04-19
Publishing country	United States
Document type	Journal Article
ZDB-ID	2211627-8
ISSN	1552-5279 ; 1552-5260
ISSN (online)	1552-5279
ISSN	1552-5260
DOI	10.1016/j.jalz.2019.03.001
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Article ; Online: Tau filaments in neurodegenerative diseases.

Goedert, Michel

FEBS letters

2018 Volume 592, Issue 14, Page(s) 2383–2391

Abstract: The ordered assembly of Tau protein into abnormal filamentous inclusions is a defining characteristic of many human neurodegenerative diseases. Thirty years ago, we reported that Tau is an integral component of the intraneuronal filaments of Alzheimer's ... ...

Abstract	The ordered assembly of Tau protein into abnormal filamentous inclusions is a defining characteristic of many human neurodegenerative diseases. Thirty years ago, we reported that Tau is an integral component of the intraneuronal filaments of Alzheimer's disease. All six brain Tau isoforms make up those filaments. Twenty years ago, we and others showed that mutations in MAPT, the Tau gene, cause familial forms of frontotemporal dementia, thus proving that dysfunction of Tau protein is sufficient to cause neurodegeneration and dementia. More recently, we showed that high-resolution structures of Tau filaments from human brain can be determined by electron cryo-microscopy. These filaments may form the seeds that underlie the prion-like properties of aggregated tau.
MeSH term(s)	Alzheimer Disease/metabolism ; Alzheimer Disease/pathology ; Animals ; Brain/metabolism ; Humans ; Neurodegenerative Diseases/genetics ; Neurodegenerative Diseases/metabolism ; Neurodegenerative Diseases/pathology ; Protein Aggregates/physiology ; Protein Aggregation, Pathological/complications ; Protein Aggregation, Pathological/pathology ; Protein Isoforms/chemistry ; Protein Isoforms/genetics ; Protein Isoforms/metabolism ; tau Proteins/chemistry ; tau Proteins/genetics ; tau Proteins/metabolism
Chemical Substances	Protein Aggregates ; Protein Isoforms ; tau Proteins
Language	English
Publishing date	2018-07-06
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	212746-5
ISSN	1873-3468 ; 0014-5793
ISSN (online)	1873-3468
ISSN	0014-5793
DOI	10.1002/1873-3468.13108
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Article ; Online: Molecular pathology of neurodegenerative diseases by cryo-EM of amyloids.

Scheres, Sjors H W / Ryskeldi-Falcon, Benjamin / Goedert, Michel

Nature

2023 Volume 621, Issue 7980, Page(s) 701–710

Abstract: Abnormal assembly of tau, α-synuclein, TDP-43 and amyloid-β proteins into amyloid filaments defines most human neurodegenerative diseases. Genetics provides a direct link between filament formation and the causes of disease. Developments in cryo-electron ...

Abstract	Abnormal assembly of tau, α-synuclein, TDP-43 and amyloid-β proteins into amyloid filaments defines most human neurodegenerative diseases. Genetics provides a direct link between filament formation and the causes of disease. Developments in cryo-electron microscopy (cryo-EM) have made it possible to determine the atomic structures of amyloids from postmortem human brains. Here we review the structures of brain-derived amyloid filaments that have been determined so far and discuss their impact on research into neurodegeneration. Whereas a given protein can adopt many different filament structures, specific amyloid folds define distinct diseases. Amyloid structures thus provide a description of neuropathology at the atomic level and a basis for studying disease. Future research should focus on model systems that replicate the structures observed in disease to better understand the molecular mechanisms of disease and develop improved diagnostics and therapies.
MeSH term(s)	Humans ; alpha-Synuclein ; Amyloid/chemistry ; Amyloid/classification ; Amyloid/ultrastructure ; Amyloid beta-Peptides ; Cryoelectron Microscopy ; Neurodegenerative Diseases/metabolism ; Neurodegenerative Diseases/pathology ; Pathology, Molecular ; Protein Folding
Chemical Substances	alpha-Synuclein ; Amyloid ; Amyloid beta-Peptides ; MAPT protein, human ; TARDBP protein, human
Language	English
Publishing date	2023-09-27
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	120714-3
ISSN	1476-4687 ; 0028-0836
ISSN (online)	1476-4687
ISSN	0028-0836
DOI	10.1038/s41586-023-06437-2
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Article ; Online: The ordered assembly of tau is the gain-of-toxic function that causes human tauopathies.

Goedert, Michel

Alzheimer's & dementia : the journal of the Alzheimer's Association

2016 Volume 12, Issue 10, Page(s) 1040–1050

Abstract: A pathological pathway leading from soluble to insoluble and filamentous tau underlies human tauopathies. This ordered assembly causes disease and is the gain-of-toxic function. It involves the transition from an intrinsically disordered monomer to a ... ...

Abstract	A pathological pathway leading from soluble to insoluble and filamentous tau underlies human tauopathies. This ordered assembly causes disease and is the gain-of-toxic function. It involves the transition from an intrinsically disordered monomer to a highly structured filament. Based on recent findings, one can divide the ordered assembly into propagation of pathology and neurodegeneration. Short tau fibrils constitute the major species of seed-competent tau in the brains of mice transgenic for human P301S tau. The molecular species of aggregated tau that are essential for neurodegeneration remain to be identified.
MeSH term(s)	Amyloid ; Animals ; Brain/pathology ; Disease Models, Animal ; Humans ; Mice ; Mice, Transgenic ; Neurofibrillary Tangles/pathology ; Phosphorylation ; Protein Aggregates ; Tauopathies/genetics ; Tauopathies/pathology ; tau Proteins/metabolism
Chemical Substances	Amyloid ; Protein Aggregates ; tau Proteins
Language	English
Publishing date	2016-09-26
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	2211627-8
ISSN	1552-5279 ; 1552-5260
ISSN (online)	1552-5279
ISSN	1552-5260
DOI	10.1016/j.jalz.2016.09.001
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