LIVIVO - Search results -

Search results

Result 1 - 10 of total 83

Search options

Article: Amyloid beta vaccination: reduced plaques and improved cognition.

Younkin, S G

2000 Volume 7, Issue 1, Page(s) 18–19

Abstract: Studies in three different transgenic mouse models suggest that the amyloid beta-protein contributes to memory loss in Alzheimer disease. Immunization with an amyloid beta-peptide fragment reduces learning and memory impairments in mice, and this ... ...

Abstract	Studies in three different transgenic mouse models suggest that the amyloid beta-protein contributes to memory loss in Alzheimer disease. Immunization with an amyloid beta-peptide fragment reduces learning and memory impairments in mice, and this approach may eventually be used to prevent and/or treat this disease in people.
MeSH term(s)	Alzheimer Disease/therapy ; Amyloid beta-Peptides/immunology ; Animals ; Cognition Disorders/therapy ; Disease Models, Animal ; Mice ; Mice, Transgenic ; Neurofibrillary Tangles ; Vaccines/administration & dosage
Chemical Substances	Amyloid beta-Peptides ; Vaccines
Language	English
Publishing date	2000-11-16
Publishing country	United States
Document type	Journal Article
ZDB-ID	1220066-9
ISSN	1546-170X ; 1078-8956
ISSN (online)	1546-170X
ISSN	1078-8956
DOI	10.1038/83929
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 4212: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 39: Show issues

Order via subito

This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

Details ▾
- See ZB MED holdings
- Order with fees

Article: The role of A beta 42 in Alzheimer's disease.

Younkin, S G

Journal of physiology, Paris

1998 Volume 92, Issue 3-4, Page(s) 289–292

Abstract: Our recent studies of plasma, fibroblasts, transfected cells and transgenic mice show that a fundamental effect of the mutations linked to familial Alzheimer's disease (FAD) is to increase the extracellular concentration of A beta 42. This effect of the ... ...

Abstract	Our recent studies of plasma, fibroblasts, transfected cells and transgenic mice show that a fundamental effect of the mutations linked to familial Alzheimer's disease (FAD) is to increase the extracellular concentration of A beta 42. This effect of the FAD-linked mutations is likely to be directly related to the pathogenesis of Alzheimer's disease (AD) because A beta 42 is deposited early and selectively in the senile plaques that are an invariant feature of all forms of AD. Thus our results provide strong evidence that the FAD-linked mutations all cause AD by increasing the extracellular concentration of A beta 42 (43), thereby fostering A beta deposition, and they support the hypothesis that cerebral A beta deposition is an essential early event in the pathogenesis of all forms of AD. Interactions between the basal forebrain cholinergic system and A beta that could influence AD pathogenesis are discussed.
MeSH term(s)	Age of Onset ; Alzheimer Disease/genetics ; Alzheimer Disease/physiopathology ; Amyloid beta-Peptides/physiology ; Animals ; Clinical Trials as Topic ; Humans ; Mutation ; Peptide Fragments/physiology
Chemical Substances	Amyloid beta-Peptides ; Peptide Fragments ; amyloid beta-protein (1-42)
Language	English
Publishing date	1998-06
Publishing country	France
Document type	Journal Article ; Review
ZDB-ID	1141200-8
ISSN	1769-7115 ; 0928-4257
ISSN (online)	1769-7115
ISSN	0928-4257
DOI	10.1016/s0928-4257(98)80035-1
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Uc I Zs.88: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article: [The AAP and PS1/2 mutations linked to early onset familial Alzheimer's disease increase the extracellular concentration and A beta 1-42 (43)].

Younkin, S G

Rinsho shinkeigaku = Clinical neurology

1997 Volume 37, Issue 12, Page(s) 1099

MeSH term(s)	Alzheimer Disease/genetics ; Amyloid beta-Peptides/analysis ; Amyloid beta-Protein Precursor/genetics ; Humans ; Membrane Proteins/genetics ; Mutation ; Peptide Fragments/analysis ; Presenilin-1 ; Presenilin-2
Chemical Substances	Amyloid beta-Peptides ; Amyloid beta-Protein Precursor ; Membrane Proteins ; PSEN1 protein, human ; PSEN2 protein, human ; Peptide Fragments ; Presenilin-1 ; Presenilin-2 ; amyloid beta-protein (1-42)
Language	Japanese
Publishing date	1997-12
Publishing country	Japan
Document type	Journal Article
ZDB-ID	604200-4
ISSN	1882-0654 ; 0009-918X
ISSN (online)	1882-0654
ISSN	0009-918X
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.B 1455: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular ab Jg. 2022: Lesesaal (EG)
Zs.MO 223: Show issues

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article: Evidence that A beta 42 is the real culprit in Alzheimer's disease.

Younkin, S G

Annals of neurology

1995 Volume 37, Issue 3, Page(s) 287–288

MeSH term(s)	Adult ; Alzheimer Disease/etiology ; Amyloid/chemistry ; Amyloid beta-Peptides/analysis ; Amyloid beta-Protein Precursor/genetics ; Animals ; Apolipoproteins E/genetics ; Cerebral Cortex/chemistry ; Down Syndrome/pathology ; Humans
Chemical Substances	Amyloid ; Amyloid beta-Peptides ; Amyloid beta-Protein Precursor ; Apolipoproteins E
Language	English
Publishing date	1995-03
Publishing country	United States
Document type	Comment ; Editorial
ZDB-ID	80362-5
ISSN	1531-8249 ; 0364-5134
ISSN (online)	1531-8249
ISSN	0364-5134
DOI	10.1002/ana.410370303
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 1370: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MO 478: Show issues

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article: The amyloid beta protein precursor mutations linked to familial Alzheimer's disease alter processing in a way that fosters amyloid deposition.

Younkin, S G

The Tohoku journal of experimental medicine

1994 Volume 174, Issue 3, Page(s) 217–223

Abstract: Normal processing of the amyloid beta protein precursor (BAPP) results in secretion of a soluble 4 kD protein essentially identical to the amyloid beta protein (A beta) that forms insoluble fibrillar deposits in Alzheimer's disease (AD). Strong evidence ... ...

Abstract	Normal processing of the amyloid beta protein precursor (BAPP) results in secretion of a soluble 4 kD protein essentially identical to the amyloid beta protein (A beta) that forms insoluble fibrillar deposits in Alzheimer's disease (AD). Strong evidence that amyloid deposition plays a critical role in the development of AD has come from the identification of familial AD (FAD) kindreds in which the AD phenotype cosegregates with mutations in the beta APP gene that are located close to the NH2 or COOH end of the A beta peptide. The location of these mutations immediately suggests that they may cause AD by altering beta APP processing in a way that is amyloidogenic. In a previous study, we found that transfected cells expressing the NH2 side mutant secrete 6-fold more 4 kD A beta than those expressing wild type beta APP or COOH side mutants. We have now shown that the mutations on the COOH side of A beta alter processing to increase secretion of the more amyloidogenic A beta 1-42 form which constitutes only a small percentage of the total 4 kD A beta produced. Thus our data show that all of the FAD-linked beta APP mutations alter beta APP processing in a way that increases the likelihood of amyloid formation.
MeSH term(s)	Aging/metabolism ; Alzheimer Disease/genetics ; Alzheimer Disease/metabolism ; Amyloid/metabolism ; Amyloid Precursor Protein Secretases ; Amyloid beta-Peptides/metabolism ; Amyloid beta-Protein Precursor/genetics ; Amyloid beta-Protein Precursor/metabolism ; Aspartic Acid Endopeptidases ; Down Syndrome/complications ; Down Syndrome/genetics ; Down Syndrome/metabolism ; Endopeptidases/metabolism ; Humans ; Models, Neurological ; Nerve Tissue Proteins/genetics ; Nerve Tissue Proteins/metabolism ; Neuroblastoma/pathology ; Peptide Fragments/metabolism ; Phenotype ; Point Mutation ; Protein Processing, Post-Translational ; Recombinant Proteins/metabolism ; Transfection ; Tumor Cells, Cultured
Chemical Substances	Amyloid ; Amyloid beta-Peptides ; Amyloid beta-Protein Precursor ; Nerve Tissue Proteins ; Peptide Fragments ; Recombinant Proteins ; amyloid beta-protein (1-42) ; Amyloid Precursor Protein Secretases (EC 3.4.-) ; Endopeptidases (EC 3.4.-) ; Aspartic Acid Endopeptidases (EC 3.4.23.-) ; BACE1 protein, human (EC 3.4.23.46)
Language	English
Publishing date	1994-11
Publishing country	Japan
Document type	Journal Article
ZDB-ID	123477-8
ISSN	0040-8727
ISSN	0040-8727
DOI	10.1620/tjem.174.217
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Ua VI Zs.155: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article: Processing of the Alzheimer's disease beta A4 amyloid protein precursor (APP).

Younkin, S G

Brain pathology (Zurich, Switzerland)

1991 Volume 1, Issue 4, Page(s) 253–262

MeSH term(s)	Alzheimer Disease/genetics ; Alzheimer Disease/metabolism ; Alzheimer Disease/pathology ; Amyloid/metabolism ; Amyloid beta-Protein Precursor/genetics ; Amyloid beta-Protein Precursor/metabolism ; Humans ; Membrane Proteins/metabolism ; Mutation ; Neurofibrillary Tangles/metabolism ; Protein Processing, Post-Translational
Chemical Substances	Amyloid ; Amyloid beta-Protein Precursor ; Membrane Proteins
Language	English
Publishing date	1991-07
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	1051484-3
ISSN	1750-3639 ; 1015-6305
ISSN (online)	1750-3639
ISSN	1015-6305
DOI	10.1111/j.1750-3639.1991.tb00668.x
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 3585: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (2.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article: Presenilins as therapeutic targets for the treatment of Alzheimer's disease.

Golde, T E / Younkin, S G

Trends in molecular medicine

2001 Volume 7, Issue 6, Page(s) 264–269

Abstract: Studies demonstrating that accumulation and aggregation of the amyloid beta protein (Abeta) within the brain is likely to cause Alzheimer's disease (AD) have provided the rationale for therapeutic strategies aimed at influencing Abeta production, ... ...

Abstract	Studies demonstrating that accumulation and aggregation of the amyloid beta protein (Abeta) within the brain is likely to cause Alzheimer's disease (AD) have provided the rationale for therapeutic strategies aimed at influencing Abeta production, aggregation and clearance. gamma-secretase catalyzes the final cleavage that releases the Abeta from its precursor; therefore, it is a potential therapeutic target for the treatment of AD. Recent data show that the polytopic membrane proteins presenilin 1 and presenilin 2 are either catalytic components or essential co-factors of a membrane-bound proteolytic complex that possesses gamma-secretase activity. Although recent findings demonstrating that gamma-secretase inhibitors bind directly to presenilins (PSs) further support a catalytic role for PSs in gamma-secretase cleavage, additional studies are still needed to clarify the role of PSs in gamma-secretase cleavage and the use of targeting PSs to reduce Abeta production.
MeSH term(s)	Alzheimer Disease/therapy ; Amyloid Precursor Protein Secretases ; Amyloid beta-Protein Precursor/metabolism ; Animals ; Aspartic Acid Endopeptidases ; Catalysis ; Endopeptidases/metabolism ; Humans ; Membrane Proteins/genetics ; Membrane Proteins/immunology ; Membrane Proteins/metabolism ; Models, Biological ; Presenilin-1 ; Presenilin-2
Chemical Substances	Amyloid beta-Protein Precursor ; Membrane Proteins ; PSEN1 protein, human ; PSEN2 protein, human ; Presenilin-1 ; Presenilin-2 ; Amyloid Precursor Protein Secretases (EC 3.4.-) ; Endopeptidases (EC 3.4.-) ; Aspartic Acid Endopeptidases (EC 3.4.23.-) ; BACE1 protein, human (EC 3.4.23.46)
Language	English
Publishing date	2001-05-17
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	2036490-8
ISSN	1471-499X ; 1471-4914
ISSN (online)	1471-499X
ISSN	1471-4914
DOI	10.1016/s1471-4914(01)02064-0
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 4345: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (2.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article: Mayo and the mouse.

Younkin, S G / Stoddard, S

Nature

2000 Volume 404, Issue 6780, Page(s) 809

MeSH term(s)	Alzheimer Disease ; Animals ; Disease Models, Animal ; Licensure ; Mice ; Mice, Transgenic ; Organizations, Nonprofit ; Patents as Topic ; Technology Transfer
Language	English
Publishing date	2000-04-20
Publishing country	England
Document type	Comment ; Letter
ZDB-ID	120714-3
ISSN	1476-4687 ; 0028-0836
ISSN (online)	1476-4687
ISSN	0028-0836
DOI	10.1038/35009257
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 26: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 9: Show issues
Zs.MO 244: Show issues

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article: Biochemical detection of Abeta isoforms: implications for pathogenesis, diagnosis, and treatment of Alzheimer's disease.

Golde, T E / Eckman, C B / Younkin, S G

Biochimica et biophysica acta

1999 Volume 1502, Issue 1, Page(s) 172–187

Abstract: Prior to the identification of the various abnormal proteins deposited as fibrillar aggregates in the Alzheimer's disease (AD) brain, there was tremendous controversy over the importance of the various lesions with respect to primacy in the pathology of ... ...

Abstract	Prior to the identification of the various abnormal proteins deposited as fibrillar aggregates in the Alzheimer's disease (AD) brain, there was tremendous controversy over the importance of the various lesions with respect to primacy in the pathology of AD. Nevertheless, based on analogy to systemic amyloidosis, many investigators believed that the amyloid deposits in AD played a causal role and that characterization of these deposits would hold the key to understanding this complex disease. Indeed, in retrospect, it was the initial biochemical purifications of the approximately 4 kDa amyloid beta-peptide (Abeta) from amyloid deposits in the mid 1980s that launched a new era of AD research (Glenner and Wong, Biochem. Biophys. Res. Commun. 122 (1984) 1121-1135; Wong et al., Proc. Natl. Acad Sci. USA 82 (1985) 8729 8732; and Masters et al., Proc. Natl. Acad Sci. USA 82 (1985) 4245-4249). Subsequent studies of the biology of Abeta together with genetic studies of AD have all supported the hypothesis that altered Abeta metabolism leading to aggregation plays a causal role in AD. Although there remains controversy as to whether Abeta deposited as classic amyloid or a smaller, aggregated, form causes AD, the relevance of studying the amyloid deposits has certainly been proven. Despite the significant advances in our understanding of the role of Abeta in AD pathogenesis, many important aspects of Abeta biology remain a mystery. This review will highlight those aspects of Abeta biology that have led to our increased understanding of the pathogenesis of AD as well as areas which warrant additional study.
MeSH term(s)	Alzheimer Disease/diagnosis ; Alzheimer Disease/etiology ; Alzheimer Disease/therapy ; Amino Acid Sequence ; Amyloid beta-Peptides/analysis ; Amyloid beta-Peptides/genetics ; Amyloid beta-Peptides/metabolism ; Animals ; Biomarkers/analysis ; Brain/metabolism ; Brain Chemistry ; Cell Line ; Electrophoresis, Polyacrylamide Gel ; Enzyme-Linked Immunosorbent Assay ; Humans ; Mass Spectrometry ; Membrane Proteins/analysis ; Membrane Proteins/genetics ; Molecular Sequence Data ; Mutation ; Peptide Fragments/analysis ; Peptide Fragments/genetics ; Presenilin-1 ; Presenilin-2 ; Protein Isoforms/analysis
Chemical Substances	Amyloid beta-Peptides ; Biomarkers ; Membrane Proteins ; PSEN1 protein, human ; PSEN2 protein, human ; Peptide Fragments ; Presenilin-1 ; Presenilin-2 ; Protein Isoforms ; amyloid beta-protein (1-42)
Language	English
Publishing date	1999-04-19
Publishing country	Netherlands
Document type	Comparative Study ; Journal Article ; Review
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/s0925-4439(00)00043-0
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Uc I Zs.247: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article: An analysis of the role of calcium in facilitation at the frog neuromuscular junction.

Younkin, S G

The Journal of physiology

1974 Volume 237, Issue 1, Page(s) 1–14

Abstract: 1. Under appropriate conditions stimulation of the neuromuscular junction by a single impulse or a brief train causes subsequent impulses to release increased amounts of transmitter. It has been proposed that this facilitation of transmitter release is ... ...

Abstract	1. Under appropriate conditions stimulation of the neuromuscular junction by a single impulse or a brief train causes subsequent impulses to release increased amounts of transmitter. It has been proposed that this facilitation of transmitter release is due to calcium which remains on release sites following the conditioning stimuli. This residual calcium hypothesis is examined in frog cutaneous pectoris muscle in the present study.2. The second component of facilitation is shown to depend on the amount of calcium present during tetanization as required by the residual calcium hypothesis.3. The quantitative behaviour of the facilitation accompanying tetani of a number of frequencies and durations is found to be consistent with the residual calcium hypothesis.4. Quantitative analysis of facilitation leads to a description of the time course of removal of calcium from release sites which is discussed.
MeSH term(s)	Animals ; Anura ; Calcium/physiology ; Electric Stimulation ; Electrophysiology ; In Vitro Techniques ; Iontophoresis ; Muscle Contraction ; Neural Conduction ; Neuromuscular Junction/physiology ; Pectoralis Muscles/innervation ; Rana pipiens
Chemical Substances	Calcium (SY7Q814VUP)
Language	English
Publishing date	1974-02
Publishing country	England
Document type	Journal Article
ZDB-ID	3115-x
ISSN	1469-7793 ; 0022-3751
ISSN (online)	1469-7793
ISSN	0022-3751
DOI	10.1113/jphysiol.1974.sp010466
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Uc I Zs.65: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

To top

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito