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ITM2C protein, human
Known as:
BRICHOS domain containing 2C protein, human
, integral membrane protein 2C, human
, BRI3 protein, human (BRICHOS domain containing)
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National Institutes of Health
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Related topics
Related topics
1 relation
Broader (1)
Membrane Proteins
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
2020
2020
Augmentation of Bri2 molecular chaperone activity against amyloid-β reduces neurotoxicity in mouse hippocampus in vitro
Gefei Chen
,
Y. Andrade-Talavera
,
+10 authors
J. Johansson
Communications Biology
2020
Corpus ID: 210716490
Molecular chaperones play important roles in preventing protein misfolding and its potentially harmful consequences…
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2020
2020
Recombinant BRICHOS chaperone domains delivered to mouse brain parenchyma by focused ultrasound and microbubbles are internalized by hippocampal and cortical neurons
L. Galan-Acosta
,
C. Sierra
,
+8 authors
J. Johansson
Molecular and Cellular Neuroscience
2020
Corpus ID: 218561548
2020
2020
Recombinant Bri3 BRICHOS domain is a molecular chaperone with effect against amyloid formation and non-fibrillar protein aggregation
Helen Poska
,
A. Leppert
,
+6 authors
Janne Johansson
Scientific Reports
2020
Corpus ID: 257028512
Molecular chaperones assist proteins in achieving a functional structure and prevent them from misfolding into aggregates…
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2018
2018
The Bri2 and Bri3 BRICHOS Domains Interact Differently with Aβ42 and Alzheimer Amyloid Plaques
Lisa Dolfe
,
S. Tambaro
,
+11 authors
J. Presto
Journal of Alzheimer's disease reports
2018
Corpus ID: 53387408
Alzheimer’s disease (AD) is the most common form of dementia and there is no successful treatment available. Evidence suggests…
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2018
2018
Of spiders, bugs, and men : Structural and functional studies of proteins involved in assembly
Wangshu Jiang
2018
Corpus ID: 91173337
Protein assembly enables complex machineries while being economical with genetic information. However, protein assembly also…
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Highly Cited
2017
Highly Cited
2017
Bri2 BRICHOS client specificity and chaperone activity are governed by assembly state
Gefei Chen
,
Axel Abelein
,
+12 authors
J. Johansson
Nature Communications
2017
Corpus ID: 36624222
Protein misfolding and aggregation is increasingly being recognized as a cause of disease. In Alzheimer’s disease the amyloid…
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2017
2017
BRICHOS – an anti-amyloid chaperone: evaluation of blood-brain barrier permeability of Bri2 BRICHOS
S. Tambaro
,
L. Galan-Acosta
,
A. Leppert
,
J. Presto
,
J. Johansson
Amyloid: Journal of Protein Folding Disorders
2017
Corpus ID: 42161597
Aggregation of the amyloid–b peptide (Ab) into toxic oligomers and amyloid fibrils is linked to the development of Alzheimer’s…
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2016
2016
Dementia-related Bri2 BRICHOS is a versatile molecular chaperone that efficiently inhibits Aβ42 toxicity in Drosophila.
Helen Poska
,
M. Haslbeck
,
+9 authors
J. Johansson
Biochemical Journal
2016
Corpus ID: 24674411
Formation of fibrils of the amyloid-β peptide (Aβ) is suggested to play a central role in neurodegeneration in Alzheimer's…
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2016
2016
BRICHOS interactions with amyloid proteins and implications for Alzheimer disease
Lisa Dolfe
2016
Corpus ID: 89520374
To date, about 30 diseases, in which amyloid fibrils form extracellular deposits, have been identified in humans. It is not known…
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2015
2015
Islet amyloid polypeptide (IAPP) in Type 2 diabetes and Alzheimer disease
M. Oskarsson
2015
Corpus ID: 1866187
The misfolding and aggregation of the beta cell hormone islet amyloid polypeptide (IAPP) into amyloid fibrils is the main…
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