Axel Abelein

发表

High-yield Production of Amyloid-β Peptide Enabled by a Customized Spider Silk Domain

J. Johansson, N. Kronqvist, K. Nordling, 2020, Scientific Reports.

Formation of Dynamic Soluble Surfactant-induced Amyloid β Peptide Aggregation Intermediates*

D. Otzen, J. S. Pedersen, J. Danielsson, 2013, The Journal of Biological Chemistry.

Increased CSF-decorin predicts brain pathological changes driven by Alzheimer’s Aβ amyloidosis

B. Winblad, P. Visser, B. Tijms, 2022, Acta neuropathologica communications.

Isotope‐labeled amyloid‐β does not transmit to the brain in a prion‐like manner after peripheral administration

M. Lalowski, M. Baumann, R. Soliymani, 2022, EMBO reports.

Decorin is an early CSF biomarker of Alzheimer’s Aβ amyloidosis

B. Winblad, P. Visser, J. Bergquist, 2021, Alzheimer's & Dementia.

Intravenous treatment with a molecular chaperone designed against β-amyloid toxicity improves Alzheimer’s disease pathology in mouse models

P. Nilsson, Janne Johansson, S. Tambaro, 2022, Molecular therapy : the journal of the American Society of Gene Therapy.

Molecular Structure of Cu(II)-Bound Amyloid-β Monomer Implicated in Inhibition of Peptide Self-Assembly in Alzheimer’s Disease

M. Piccioli, Andrea Giachetti, S. Ciofi‐Baffoni, 2022, JACS Au.

Autophagy Impairment in App Knock-in Alzheimer’s Model Mice

B. Winblad, N. Bogdanovic, P. Nilsson, 2022, Frontiers in Aging Neuroscience.

Amyloid Fibril Formation of Arctic Amyloid-β 1–42 Peptide is Efficiently Inhibited by the BRICHOS Domain

Janne Johansson, Rakesh Kumar, Gefei Chen, 2022, ACS chemical biology.

Modulation of Alzheimer's amyloid β peptide self-assembly : Insights into molecular mechanisms of peptide aggregation associated with Alzheimer's disease

Axel Abelein, 2015 .

Modulation of amyloid β peptide self-assembly : Aggregation mechanisms associated with Alzheimer's disease

Axel Abelein, 2013 .

Bri2 BRICHOS client specificity and chaperone activity are governed by assembly state

A. Fisahn, J. Johansson, M. Landreh, 2017, Nature Communications.

A. Fisahn, J. Johansson, M. Haslbeck, 2016, The Biochemical journal.

Characterization of Mn(II) ion binding to the amyloid-β peptide in Alzheimer's disease.

J. Abrahams, B. Strodel, A. Gräslund, 2016, Journal of trace elements in medicine and biology : organ of the Society for Minerals and Trace Elements.

Ionic Strength Modulation of the Free Energy Landscape of Aβ40 Peptide Fibril Formation.

J. Danielsson, A. Gräslund, A. Barth, 2016, Journal of the American Chemical Society.

The hairpin conformation of the amyloid β peptide is an important structural motif along the aggregation pathway

J. Abrahams, J. Danielsson, A. Gräslund, 2014, JBIC Journal of Biological Inorganic Chemistry.

A "spindle and thread" mechanism unblocks p53 translation by modulating N-terminal disorder.

L. Nilsson, J. Siau, F. Ghadessy, 2022, Structure.

Metal ion coordination delays amyloid-β peptide self-assembly by forming an aggregation–inert complex

J. Danielsson, A. Gräslund, S. Wärmländer, 2020, The Journal of Biological Chemistry.

Spidroin N-terminal domain forms amyloid-like fibril based hydrogels and provides a protein immobilization platform

R. Strömberg, C. Holland, N. Kronqvist, 2022, Nature Communications.

High intracellular stability of the spidroin N‐terminal domain in spite of abundant amyloidogenic segments revealed by in‐cell hydrogen/deuterium exchange mass spectrometry

J. Johansson, H. Jörnvall, D. Lane, 2019, The FEBS journal.

Biophysical Studies of the Amyloid β‐Peptide: Interactions with Metal Ions and Small Molecules

J. Danielsson, A. Gräslund, Ann Tiiman, 2013, Chembiochem : a European journal of chemical biology.

Molecular Mechanisms of Amyloid-β Self-Assembly Seeded by In Vivo-Derived Fibrils and Inhibitory Effects of the BRICHOS Chaperone

A. Fisahn, P. Nilsson, Janne Johansson, 2023, ACS chemical neuroscience.

Amyloid inhibition by molecular chaperones in vitro can be translated to Alzheimer's pathology in vivo

Janne Johansson, Axel Abelein, 2023, RSC medicinal chemistry.

Abilities of the BRICHOS domain to prevent neurotoxicity and fibril formation are dependent on a highly conserved Asp residue

A. Fisahn, N. Kronqvist, A. Rising, 2022, RSC Chemical Biology.

Intravenous treatment with a molecular chaperone designed against amyloid-β toxicity improves features of Alzheimer disease pathology in mouse models.

P. Nilsson, Janne Johansson, S. Tambaro, 2022, Molecular therapy : the journal of the American Society of Gene Therapy.

Augmentation of Bri2 molecular chaperone activity against amyloid-β reduces neurotoxicity in mouse hippocampus in vitro

A. Fisahn, M. Landreh, H. Hebert, 2020, Communications Biology.

Augmentation of Bri2 molecular chaperone activity against amyloid-β reduces neurotoxicity in mouse hippocampus in vitro

A. Fisahn, J. Johansson, M. Landreh, 2020, Communications Biology.

High-yield Production of Amyloid-β Peptide Enabled by a Customized Spider Silk Domain

J. Johansson, N. Kronqvist, K. Nordling, 2020, Scientific Reports.

Bri2 BRICHOS client specificity and chaperone activity are governed by assembly state

A. Fisahn, J. Johansson, M. Landreh, 2017, Nature Communications.

Short hydrophobic loop motifs in BRICHOS domains determine chaperone activity against amorphous protein aggregation but not against amyloid formation

P. Koeck, H. Hebert, C. Jegerschöld, 2023, Communications biology.

A new kid in the folding funnel: Molecular chaperone activities of the BRICHOS domain

M. Landreh, Janne Johansson, Gefei Chen, 2023, Protein science : a publication of the Protein Society.

Zinc as chaperone-mimicking agent for retardation of amyloid β peptide fibril formation

Astrid Gräslund, J. Danielsson, A. Gräslund, 2015, Proceedings of the National Academy of Sciences.

Functionalization of amyloid fibrils via the Bri2 BRICHOS domain

J. Johansson, N. Dantuma, Rakesh Kumar, 2020, Scientific Reports.

Hydrophobicity and conformational change as mechanistic determinants for nonspecific modulators of amyloid β self-assembly.

C. Dobson, A. Gräslund, Christofer Lendel, 2012, Biochemistry.

Molecular chaperone ability to inhibit amyloid-derived neurotoxicity, but not amorphous protein aggregation, depends on a conserved pH-sensitive Asp residue

A. Fisahn, N. Kronqvist, A. Rising, 2021, bioRxiv.

The synthesis and characterization of Bri2 BRICHOS coated magnetic particles and their application to protein fishing: Identification of novel binding proteins.

L. Ferrucci, J. Johansson, M. Aon, 2021, Journal of pharmaceutical and biomedical analysis.

Misfolded alpha-synuclein detection by RT-QuIC in dementia with lewy bodies: a systematic review and meta-analysis

D. Ferreira, M. Baquero, C. Cháfer-Pericás, 2023, Frontiers in Molecular Biosciences.

Transient small molecule interactions kinetically modulate amyloid β peptide self‐assembly

J. Danielsson, A. Gräslund, Christofer Lendel, 2012, FEBS letters.

Smallest Secondary Nucleation Competent Aβ Aggregates Probed by an ATP-Independent Molecular Chaperone Domain

J. Johansson, N. Kronqvist, Ann Tiiman, 2021, Biochemistry.

Hydrophobicity and conformational change as mechanistic determinants for nonspecific modulators of amyloid β self-assembly.

C. Dobson, A. Gräslund, Christofer Lendel, 2012, Biochemistry.

The hairpin conformation of the amyloid β peptide is an important structural motif along the aggregation pathway

J. Abrahams, J. Danielsson, A. Gräslund, 2014, JBIC Journal of Biological Inorganic Chemistry.

Metal Binding of Alzheimer’s Amyloid-β and Its Effect on Peptide Self-Assembly

Axel Abelein, 2023, Accounts of chemical research.

Metal ion coordination delays amyloid-β peptide self-assembly by forming an aggregation-inert complex.

J. Danielsson, A. Gräslund, S. Wärmländer, 2020, Journal of Biological Chemistry.