S. Barghorn

发表

Globular amyloid beta-peptide oligomer - a homogenous and stable neuropathological protein in Alzheimer's disease.

P. Keller, J. Harlan, V. Nimmrich, 2005, Journal of neurochemistry.

Toward a unified scheme for the aggregation of tau into Alzheimer paired helical filaments.

E. Mandelkow, S. Barghorn, E Mandelkow, 2002, Biochemistry.

Antibody Engineering and Therapeutics

Jamie K. Scott, F. Lund-Johansen, E. Ben-Jacob, 2013, mAbs.

Spectroscopic Approaches to the Conformation of Tau Protein in Solution and in Paired Helical Filaments

E. Mandelkow, S. Jeganathan, M. von Bergen, 2006, Neurodegenerative Diseases.

Structure, microtubule interactions, and paired helical filament aggregation by tau mutants of frontotemporal dementias.

E. Mandelkow, Q. Zheng-Fischhöfer, J. Biernat, 2000, Biochemistry.

Purification of recombinant tau protein and preparation of Alzheimer-paired helical filaments in vitro.

E. Mandelkow, J. Biernat, S. Barghorn, 2005, Methods in molecular biology.

Immunotherapy alleviates amyloid-associated synaptic pathology in an Alzheimer’s disease mouse model

J. Herms, S. Burgold, M. Dorostkar, 2014, Brain : a journal of neurology.

Mutations of Tau Protein in Frontotemporal Dementia Promote Aggregation of Paired Helical Filaments by Enhancing Local β-Structure*

E. Mandelkow, E. Mandelkow, J. Biernat, 2001, The Journal of Biological Chemistry.

Structural characterization of a soluble amyloid beta-peptide oligomer.

P. Hajduk, P. Richardson, Liping Yu, 2009, Biochemistry.

Antibody Engineering & Therapeutics, The Annual Meeting of The Antibody Society

Jamie K. Scott, F. Lund-Johansen, E. Ben-Jacob, 2014 .

N368-Tau fragments generated by legumain are detected only in trace amount in the insoluble Tau aggregates isolated from AD brain

K. Schlegel, L. Gasparini, R. Heym, 2019, Acta Neuropathologica Communications.

Generation and Therapeutic Efficacy of Highly Oligomer-Specific β-Amyloid Antibodies

H. Schoemaker, J. Sullivan, F. van Leuven, 2010, The Journal of Neuroscience.

Globular amyloid β‐peptide1−42 oligomer − a homogenous and stable neuropathological protein in Alzheimer's disease

P. Keller, J. Harlan, V. Nimmrich, 2005 .

Tau aggregation is driven by a transition from random coil to beta sheet structure.

Martin von Bergen, E. Mandelkow, E. Mandelkow, 2005, Biochimica et biophysica acta.

Amyloid β Oligomers (Aβ1–42 Globulomer) Suppress Spontaneous Synaptic Activity by Inhibition of P/Q-Type Calcium Currents

A. Draguhn, C. Bruehl, H. Schoemaker, 2008, The Journal of Neuroscience.

Aβ-globulomers are formed independently of the fibril pathway

S. Barghorn, Andreas Striebinger, H. Hillen, 2008, Neurobiology of Disease.

Targeting repulsive guidance molecule A to promote regeneration and neuroprotection in multiple sclerosis.

H. Schoemaker, P. Calabresi, H. Rus, 2015, Cell reports.

The core of tau-paired helical filaments studied by scanning transmission electron microscopy and limited proteolysis.

E. Mandelkow, E. Mandelkow, P. Davies, 2006, Biochemistry.

Tau paired helical filaments from Alzheimer's disease brain and assembled in vitro are based on beta-structure in the core domain.

E. Mandelkow, P. Davies, S. Barghorn, 2004, Biochemistry.

Decreased levels of repulsive guidance molecule A in association with beneficial effects of repeated intrathecal triamcinolone acetonide application in progressive multiple sclerosis patients

T. Müller, B. Mueller, S. Barghorn, 2015, Journal of Neural Transmission.

Globular amyloid b-peptide 1 ) 42 oligomer ) a homogenous and stable neuropathological protein in Alzheimer ’ s disease

P. Keller, J. Harlan, V. Nimmrich, 2005 .

A β‐amyloid oligomer directly modulates P/Q‐type calcium currents in Xenopus oocytes

H. Schoemaker, M. Mezler, V. Nimmrich, 2012, British journal of pharmacology.

Off-target binding of an anti-amyloid beta monoclonal antibody to platelet factor 4 causes acute and chronic toxicity in cynomolgus monkeys

Frank Oellien, E. Tarcsa, S. Barghorn, 2021, mAbs.