H. Hillen

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.

Studies on cortisol metabolism during haemodialysis in man

H. Hillen, K. Deck, B. Fischer, 1979, European journal of clinical investigation.

Crystallization of human tumour necrosis factor

D. Stuart, N. Walker, W. Maechtle, 1990 .

Serine Protease Inhibitor Nafamostat Given Before Reperfusion Reduces Inflammatory Myocardial Injury by Complement and Neutrophil Inhibition

K. Werdan, A. Schlitt, M. Buerke, 2008, Journal of cardiovascular pharmacology.

Two-dimensional analysis of myocardial protein expression following myocardial ischemia and reperfusion in rabbits.

H. Darius, M. Buerke, Jürgen Meyer, 2002, Proteomics.

Is Science the Only Driver in Species Selection? An Internal Study to Evaluate Compound Requirements in the Minipig Compared to the Dog in Preclinical Studies

P. Germann, H. Hillen, J. Burkhardt, 2016, Toxicologic pathology.

Enzyme In Vivo : Evidence for a Regulatory Role of Endothelin Obesity Is Associated With Tissue-Specific Activation of Renal Angiotensin-Converting

T. Lüscher, J. Krieger, L. d’Uscio, 2000 .

Obesity is associated with tissue-specific activation of renal angiotensin-converting enzyme in vivo: evidence for a regulatory role of endothelin.

T. Lüscher, J. Krieger, L. d’Uscio, 2000, Hypertension.

Discovery and synthesis of (S)-3-[2-(3,4-dimethoxyphenyl)ethoxy]-2- (4,6-dimethylpyrimidin-2-yloxy)-3,3-diphenylpropionic acid (LU 302872), a novel orally active mixed ET(A)/ET(B) receptor antagonist.

H. Riechers, W. Amberg, D. Klinge, 1999, Journal of medicinal chemistry.

Editorial: Beta-Amyloid oligomer specific treatments for Alzheimer's disease

H. Hillen, 2023, Frontiers in Neuroscience.

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.

Structural characterization of a soluble amyloid beta-peptide oligomer.

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

The primary structure of bovine brain myelin lipophilin (proteolipid apoprotein).

W. Stoffel, W. Schröder, R. Deutzmann, 1983, Hoppe-Seyler's Zeitschrift fur physiologische Chemie.

The Beta Amyloid Dysfunction (BAD) Hypothesis for Alzheimer’s Disease

H. Hillen, 2019, Front. Neurosci..

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 .

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.

Proteome analysis of myocardial tissue following ischemia and reperfusion--effects of complement inhibition.

K. Werdan, M. Buerke, H. Schwertz, 2006, Biochimica et biophysica acta.

Aβ-globulomers are formed independently of the fibril pathway

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

Monomeric structures of the zymogen and active catalytic domain of complement protease c1r: further insights into the c1 activation mechanism.

W. Grabarse, N. Thielens, G. Arlaud, 2002, Structure.

Structure and molecular arrangement of proteolipid protein of central nervous system myelin.

W. Stoffel, H. Hillen, H. Giersiefen, 1984, Proceedings of the National Academy of Sciences of the United States of America.

Amino-acid sequence of human and bovine brain myelin proteolipid protein (lipophilin) is completely conserved.

W. Stoffel, B. Tunggal, H. Hillen, 1985, Biological chemistry Hoppe-Seyler.

Monoclonal antibodies against human endothelin-converting enzyme-1.

H. Hillen, B. Kröger, T. Subkowski, 1998, Journal of immunoassay.

Molecular characterization of human and bovine endothelin converting enzyme (ECE‐1)

G. Schmalzing, R. Otter, H. Seulberger, 1994, FEBS letters.

Enzyme de conversion de l'endotheline

E. Jacob, R. Otter, T. Meyer, 1994 .

Magnetic Resonance Imaging Detection and Time Course of Cerebral Microhemorrhages during Passive Immunotherapy in Living Amyloid Precursor Protein Transgenic Mice

Jean M. Severin, D. Llano, M. Day, 2010, Journal of Pharmacology and Experimental Therapeutics.

Analysis of the primary structure of the strongly hydrophobic brain myelin proteolipid apoprotein (lipophilin). Isolation and amino acid sequence determination of proteolytic fragments.

W. Stoffel, W. Schröder, R. Deutzmann, 1982, Hoppe-Seyler's Zeitschrift fur physiologische Chemie.

Primary structure of the C-terminal cyanogen bromide fragments II, III and IV from bovine brain proteolipid-apoprotein.

W. Stoffel, R. Deutzmann, H. Hillen, 1982, Hoppe-Seyler's Zeitschrift fur physiologische Chemie.

Two‐dimensional analysis of myocardial protein expression following myocardial ischemia and reperfusion in rabbits

H. Darius, M. Buerke, Jürgen Meyer, 2002 .

Plasma clearance of cortisol as a function of plasma cortisol levels in normal and obese persons and in patients with uraemia or cirrhosis of the liver.

H. Hillen, K. Deck, P. Baur, 1979, Acta Endocrinologica.

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

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