Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Helmut Romig"'
Autor:
Helmut Romig, Sandra Handschuh, Tom Bretschneider, Bernd Nosse, Marco Ferrara, Paul Nicklin, Stefan Hoerer, Gerald Juergen Roth, Christian A. Kuttruff
Publikováno v:
ACS medicinal chemistry letters. 8(12)
In an effort to find new therapeutic interventions addressing the unmet medical need of patients with idiopathic pulmonary fibrosis, we initiated a program to identify new autotaxin (ATX) inhibitors. Starting from a recently published compound (PF-83
Autor:
Wolfgang Rist, Daniel Bischoff, Klaus Klinder, Paul Nicklin, Tom Bretschneider, Andreas H. Luippold, Helmut Romig
Publikováno v:
SLAS discovery : advancing life sciences RD. 22(4)
Autotaxin (ATX) is a promising drug target for the treatment of several diseases, such as cancer and fibrosis. ATX hydrolyzes lysophosphatidyl choline (LPC) into bioactive lysophosphatidic acid (LPA). The potency of ATX inhibitors can be readily dete
Autor:
Angela Berry, Monika Ermann, Claudia Albrecht, Doris Riether, David S. Thomson, Eugene R. Hickey, Someina Khor, Helmut Romig, Achim Sauer, Lifen Wu, Jenkins James Edward, Nelamangala V. Nagaraja, Mark J. Gemkow, Angelo Ceci, Renee Zindell, Raj Betageri
Publikováno v:
Bioorganicmedicinal chemistry letters. 25(3)
Through a ligand-based pharmacophore model (S)-proline based compounds were identified as potent cannabinoid receptor 2 (CB2) agonists with high selectivity over the cannabinoid receptor 1 (CB1). Structure–activity relationship investigations for t
Autor:
Angela Berry, Claudia Albrecht, Pier F. Cirillo, Lifen Wu, Mark J. Gemkow, Alessandra Bartolozzi, Renee Zindell, Angelo Ceci, David S. Thomson, Helmut Romig, Achim Sauer, Eugene R. Hickey, Nelamangala V. Nagaraja, Doris Riether
Publikováno v:
Bioorganicmedicinal chemistry letters. 25(3)
A novel class of potent cannabinoid receptor 2 (CB2) agonists based on a (S)-piperidine scaffold was identified using ligand-based pharmacophore models. Optimization of solubility and metabolic stability led to the identification of several potent CB
Autor:
Barbara Steiner, Steffen Leutz, Walter E. Müller, Christian Haass, Celio A. Marques, Helmut Romig, Anne Eckert
Publikováno v:
Journal of Neuroscience Research. 64:183-192
The Swedish double mutation (KM670/671NL) of amyloid precursor protein (APPsw) is associated with early-onset familial Alzheimer's disease (FAD) and results in from three- to sixfold increased beta-amyloid production. The goal of the present study wa
Autor:
Ralf Baumeister, Anja Capell, Andreas Böttcher, Masayasu Okochi, Helmut Romig, Jochen Walter, Christian Haass, Harald Steiner, Stefan Eimer
Publikováno v:
Journal of Biological Chemistry. 275:40925-40932
The familial Alzheimer's disease-associated presenilins (PSs) occur as a dimeric complex of proteolytically generated fragments, which functionally supports endoproteolysis of Notch and the beta-amyloid precursor protein (betaAPP). A homologous gene,
Autor:
Katja Fechteler, Harald Steiner, John Hardy, Ralf Baumeister, Marcus Kostka, Helmut Romig, Liane Meyn, Melissa L. Grim, Gabriele Basset, Christian Haass, Brigitte Pesold, Anja Capell
Publikováno v:
Nature Cell Biology. 2:848-851
Endoproteolysis of beta-amyloid precursor protein (betaAPP) and Notch requires conserved aspartate residues in presenilins 1 and 2 (PS1 and PS2). Although PS1 and PS2 have therefore been proposed to be aspartyl proteases, no homology to other asparty
Autor:
Jochen Walter, Ralf Baumeister, David B. Teplow, Luka Kulic, Helmut Romig, Harald Steiner, Anja Capell, Gerd Multhaup, Christian Haass
Publikováno v:
Kulic, L; Walter, J; Multhaup, G; Teplow, DB; Baumeister, R; Romig, H; et al.(2000). Separation of presenilin function in amyloid β-peptide generation and endoproteolysis of Notch. Proceedings of the National Academy of Sciences of the United States of America, 97(11), 5913-5918. doi: 10.1073/pnas.100049897. UCLA: Retrieved from: http://www.escholarship.org/uc/item/7hs882q5
Most of the genetically inherited Alzheimer's disease cases are caused by mutations in the presenilin genes, PS1 and PS2. PS mutations result in the enhanced production of the highly amyloidogenic 42/43 amino acid variant of amyloid β-peptide (Aβ).
Presenilin-1 differentially facilitates endoproteolysis of the β-amyloid precursor protein and Notch
Autor:
Melissa G. Grim, Ralf Baumeister, Miriam Baader, Christian Haass, Harald Steiner, Anja Capell, Helmut Romig, Simone Keck
Publikováno v:
Nature Cell Biology. 2:205-211
Mutations in the presenilin-1 (PS1) gene are associated with Alzheimer's disease and cause increased secretion of the neurotoxic amyloid-beta peptide (Abeta). Critical intramembraneous aspartates at residues 257 and 385 are required for the function
Autor:
Christian Haass, Harald Steiner, Martin Citron, Dennis J. Selkoe, Helmut Romig, Anja Capell, Peter M. Kloetzel, Klaus Mendla, Brigitte Pesold
Publikováno v:
Journal of Biological Chemistry. 273:32322-32331
Numerous mutations causing early onset Alzheimer's disease have been identified in the presenilin (PS) genes, particularly the PS1 gene. Like the mutations identified within the beta-amyloid precursor protein gene, PS mutations cause the increased ge