H. Steiner

发表

Regulated intramembrane proteolysis – lessons from amyloid precursor protein processing

Harald Steiner, Christian Haass, C. Haass, 2011, Journal of neurochemistry.

Presenilins mediate a dual intramembranous gamma-secretase cleavage of Notch-1.

T. Kudo, T. Iwatsubo, M. Takeda, 2002, The EMBO journal.

Presenilins mediate a dual intramembranous γ‐secretase cleavage of Notch‐1

T. Kudo, T. Iwatsubo, M. Takeda, 2002 .

Microbiota-derived short chain fatty acids modulate microglia and promote Aβ plaque deposition

M. Dichgans, M. Giera, A. Macpherson, 2021, eLife.

Microbiota-derived short chain fatty acids promote Aβ plaque deposition

M. Dichgans, M. Giera, A. Macpherson, 2020, bioRxiv.

Molecular Mechanisms of Protein Translocation into and Across the Mitochondrial Outer Membrane

W. Neupert, A. Mayer, R. Lill, 1996 .

Glycine 384 is required for presenilin-1 function and is conserved in bacterial polytopic aspartyl proteases

J. Hardy, C. Haass, R. Baumeister, 2000, Nature Cell Biology.

Insulin-degrading Enzyme Rapidly Removes the β-Amyloid Precursor Protein Intracellular Domain (AICD)*

C. Haass, D. Edbauer, M. Willem, 2002, The Journal of Biological Chemistry.

Presenilin-1 mutations of leucine 166 equally affect the generation of the Notch and APP intracellular domains independent of their effect on Aβ42 production

B. Ghetti, Hui Zheng, C. Haass, 2002, Proceedings of the National Academy of Sciences of the United States of America.

Uncovering gamma-secretase.

H. Steiner, 2004, Current Alzheimer research.

Identification of Distinct γ-Secretase Complexes with Different APH-1 Variants*

C. Haass, D. Edbauer, S. Prokop, 2004, Journal of Biological Chemistry.

Requirement of PEN-2 for Stabilization of the Presenilin N-/C-terminal Fragment Heterodimer within the γ-Secretase Complex*

C. Haass, D. Edbauer, S. Prokop, 2004, Journal of Biological Chemistry.

Co-expression of Nicastrin and Presenilin Rescues a Loss of Function Mutant of APH-1*

C. Haass, C. Kaether, D. Edbauer, 2004, Journal of Biological Chemistry.

Identification of distinct gamma-secretase complexes with different APH-1 variants.

C. Haass, D. Edbauer, S. Prokop, 2004, The Journal of biological chemistry.

SorLA Signaling by Regulated Intramembrane Proteolysis*

C. Haass, N. M. Seibel, W. Hampe, 2006, Journal of Biological Chemistry.

Secretion of the Notch-1 Abeta-like peptide during Notch signaling.

M. Takeda, S. Tagami, M. Okochi, 2006, The Journal of biological chemistry.

Purification, pharmacological modulation, and biochemical characterization of interactors of endogenous human gamma-secretase.

Birgit Dümpelfeld, C. Hopf, S. Hobson, 2009, Biochemistry.

PEN-2 Is an Integral Component of the γ-Secretase Complex Required for Coordinated Expression of Presenilin and Nicastrin*

Harald Steiner, Edith Winkler, Christian Haass, 2002, The Journal of Biological Chemistry.

Important functional role of residue x of the presenilin GxGD protease active site motif for APP substrate cleavage specificity and substrate selectivity of γ‐secretase

C. Haass, S. Lichtenthaler, P. Kuhn, 2013, Journal of neurochemistry.

The Nicastrin ectodomain adopts a highly thermostable structure

C. Haass, R. Fluhrer, F. Kamp, 2011, Biological chemistry.

Requirement for small side chain residues within the GxGD‐motif of presenilin for γ‐secretase substrate cleavage

C. Haass, H. Steiner, A. Fukumori, 2010, Journal of neurochemistry.

Chemical Cross-linking Provides a Model of the γ-Secretase Complex Subunit Architecture and Evidence for Close Proximity of the C-terminal Fragment of Presenilin with APH-1*

C. Haass, H. Steiner, E. Winkler, 2008, Journal of Biological Chemistry.

Length and overall sequence of the PEN‐2 C‐terminal domain determines its function in the stabilization of presenilin fragments

C. Haass, S. Prokop, H. Steiner, 2005, Journal of neurochemistry.

Expression of Alzheimer’s Disease-associated Presenilin-1 Is Controlled by Proteolytic Degradation and Complex Formation*

P. Kloetzel, D. Selkoe, M. Citron, 1998, The Journal of Biological Chemistry.

Intramembrane proteolysis by presenilins

C. Haass, H. Steiner, 2000, Nature Reviews Molecular Cell Biology.

Three-Amino Acid Spacing of Presenilin Endoproteolysis Suggests a General Stepwise Cleavage of γ-Secretase-Mediated Intramembrane Proteolysis

C. Haass, R. Fluhrer, H. Steiner, 2010, The Journal of Neuroscience.

Longitudinal Assessment of Cerebral β-Amyloid Deposition in Mice Overexpressing Swedish Mutant β-Amyloid Precursor Protein Using 18F-Florbetaben PET

P. Cumming, P. Bartenstein, G. Xiong, 2013, The Journal of Nuclear Medicine.

A high-content screen for small-molecule regulators of epithelial cell-adhesion molecule (EpCAM) cleavage yields a robust inhibitor

D. Niessing, O. Gires, Kenji Schorpp, 2018, The Journal of Biological Chemistry.

A Loss of Function Mutant of the Presenilin Homologue SEL-12 Undergoes Aberrant Endoproteolysis in Caenorhabditis elegans and Increases Aβ42 Generation in Human Cells*

S. Eimer, M. Okochi, C. Haass, 2000, The Journal of Biological Chemistry.

Intracellular Generation and Accumulation of Amyloid β-Peptide Terminating at Amino Acid 42*

Y. Ihara, C. Haass, U. Leimer, 1997, The Journal of Biological Chemistry.

Sheddases and intramembrane‐cleaving proteases: RIPpers of the membrane

S. Lichtenthaler, H. Steiner, 2007, EMBO reports.

Mutation of conserved aspartates affect maturation of presenilin 1 and presenilin 2 complexes

P. S. St George-Hyslop, P. Fraser, T. Kawarai, 2000, Acta neurologica Scandinavica. Supplementum.

Heme Binding to a Conserved Cys-Pro-Val Motif Is Crucial for the Catalytic Function of Mitochondrial Heme Lyases*

A. Zollner, W. Neupert, R. Lill, 1996, The Journal of Biological Chemistry.

Biogenesis of Mitochondrial Heme Lyases in Yeast

A. Zollner, W. Neupert, R. Lill, 1995, The Journal of Biological Chemistry.

Genes and mechanisms involved in beta-amyloid generation and Alzheimer's disease.

C. Haass, U. Leimer, H. Steiner, 1999, European archives of psychiatry and clinical neuroscience.

Proteolytic Processing of Neuregulin 1 Type III by Three Intramembrane-cleaving Proteases

E. Kremmer, M. Rossner, C. Haass, 2015, The Journal of Biological Chemistry.

Proteolytically generated soluble Tweak Receptor Fn14 is a blood biomarker for γ‐secretase activity

C. Nimsky, S. Riddell, G. Jocher, 2022, EMBO molecular medicine.

Binding of Bexarotene to the Amyloid Precursor Protein Transmembrane Domain in Liposomes Alters its α -Helical Conformation but Inhibits γ -Secretase Non-Selectively

C. Sanders, H. Scheidt, D. Huster, 2018 .

Intramembrane cleavage of TREM2 is determined by its intrinsic structural dynamics

C. Haass, H. Steiner, F. Hagn, 2019, bioRxiv.

Modulating Hinge Flexibility in the APP Transmembrane Domain Alters γ-Secretase Cleavage.

D. Huster, B. Luy, D. Langosch, 2019, Biophysical journal.

Modulating hinge flexibility in the APP transmembrane domain alters γ-secretase cleavage

D. Huster, B. Luy, D. Langosch, 2018, bioRxiv.

Modulating hinge flexibility in the APP transmembrane domain alters γ-secretase cleavage

D. Huster, B. Luy, D. Langosch, 2018, bioRxiv.

Mutation of conserved aspartates affects maturation of both aspartate mutant and endogenous presenilin 1 and presenilin 2 complexes.

P. Fraser, P. George-Hyslop, T. Kawarai, 2000, The Journal of biological chemistry.

Novel γ-Secretase Enzyme Modulators Directly Target Presenilin Protein*

C. Haass, K. Baumann, H. Steiner, 2011, The Journal of Biological Chemistry.

β-Amyloid Precursor Protein Mutants Respond to γ-Secretase Modulators*♦

Richard M. Page, C. Haass, R. Page, 2010, The Journal of Biological Chemistry.

Intramembrane Proteolysis of GXGD-type Aspartyl Proteases Is Slowed by a Familial Alzheimer Disease-like Mutation*

E. Kremmer, D. Teplow, C. Haass, 2008, Journal of Biological Chemistry.

Title Presenilin-dependent γ-secretase processing of β-amyloid precursor protein at a site corresponding to the S 3 cleavage of Notch Permalink

D. Teplow, G. Multhaup, C. Haass, 2013 .

Foamy Virus Envelope Protein Is a Substrate for Signal Peptide Peptidase-like 3 (SPPL3)*

E. Kremmer, B. Schröder, C. Haass, 2012, The Journal of Biological Chemistry.

Nuclear signaling

C. Haass, H. Steiner, 2001, Journal of Molecular Neuroscience.

Pore-forming scissors? A first structural glimpse of gamma-secretase.

W. Bode, C. Haass, M. Than, 2006, Trends in biochemical sciences.

Endoproteolysis of the ER Stress Transducer ATF6 in the Presence of Functionally Inactive Presenilins

R. Prywes, C. Haass, M. Shearman, 2001, Neurobiology of Disease.

Regulated Intramembrane Proteolysis and Degradation of Murine Epithelial Cell Adhesion Molecule mEpCAM

W. Zimmermann, B. Mack, O. Gires, 2013, PloS one.

Endoplasmic reticulum retention of the γ‐secretase complex component Pen2 by Rer1

C. Haass, C. Kaether, S. Kacmar, 2007 .

A γ‐secretase inhibitor blocks Notch signaling in vivo and causes a severe neurogenic phenotype in zebrafish

C. Haass, Andrea Geling, L. Bally-Cuif, 2002, EMBO reports.

Substrate determinants of signal peptide peptidase-like 2a (SPPL2a)-mediated intramembrane proteolysis of the invariant chain CD74.

P. Saftig, Susann Hüttl, B. Schröder, 2016, The Biochemical journal.

A Presenilin Dependent S3-Like γ-Secretase Cleavage of the β-Amyloid Precursor Protein

D. Teplow, G. Multhaup, C. Haass, 2002 .

Homodimerization Protects the Amyloid Precursor Protein C99 Fragment from Cleavage by γ-Secretase.

D. Langosch, H. Steiner, E. Winkler, 2015, Biochemistry.

Role of the intermembrane-space domain of the preprotein receptor Tom22 in protein import into mitochondria

R. Hodges, W. Neupert, F. Nargang, 1996, Molecular and cellular biology.

The PMR2 gene cluster encodes functionally distinct isoforms of a putative Na+ pump in the yeast plasma membrane.

H. Steiner, H. Rudolph, J. Strayle, 1995, The EMBO journal.

Bepridil and Amiodarone Simultaneously Target the Alzheimer's Disease β- and γ-Secretase via Distinct Mechanisms

Richard M. Page, J. Herms, C. Haass, 2010, The Journal of Neuroscience.

Cleavage and Cell Adhesion Properties of Human Epithelial Cell Adhesion Molecule (HEPCAM)*

N. Stoecklein, B. Lenarčič, K. Lauber, 2015, The Journal of Biological Chemistry.

Reconstitution of γ-secretase activity

J. Regula, C. Haass, D. Edbauer, 2003, Nature Cell Biology.

Shedding of glycan‐modifying enzymes by signal peptide peptidase‐like 3 (SPPL3) regulates cellular N‐glycosylation

R. Obst, B. Schröder, C. Haass, 2014, The EMBO journal.

Atherogenic LOX-1 signaling is controlled by SPPL2-mediated intramembrane proteolysis

A. Tholey, B. Schröder, Torben Mentrup, 2019, The Journal of experimental medicine.

Inhibition of gamma-secretase by the CK1 inhibitor IC261 does not depend on CK1delta.

K. Baumann, B. Schmidt, H. Steiner, 2010, Bioorganic & medicinal chemistry letters.

Secretion of the Notch-1 Aβ-like Peptide during Notch Signaling*

M. Takeda, S. Tagami, M. Okochi, 2006, Journal of Biological Chemistry.

Substrate recruitment by γ-secretase.

H. Steiner, A. Fukumori, L. P. Feilen, 2020, Seminars in cell & developmental biology.

GXGD-Type Intramembrane Proteases

C. Haass, H. Steiner, 2007 .

Alzheimer disease γ-secretase: a complex story of GxGD-type presenilin proteases

C. Haass, H. Steiner, 2002 .

Presenilin-dependent Intramembrane Proteolysis of CD44 Leads to the Liberation of Its Intracellular Domain and the Secretion of an Aβ-like Peptide*

Harald Steiner, Masatoshi Takeda, Christian Haass, 2002, The Journal of Biological Chemistry.

A Pathogenic Presenilin-1 Deletion Causes Abberrant Aβ42 Production in the Absence of Congophilic Amyloid Plaques*

J. Hardy, T. Révész, H. Kretzschmar, 2001, The Journal of Biological Chemistry.

Presenilin-1 differentially facilitates endoproteolysis of the β-amyloid precursor protein and Notch

C. Haass, R. Baumeister, H. Steiner, 2000, Nature Cell Biology.

A Loss of Function Mutation of Presenilin-2 Interferes with Amyloid β-Peptide Production and Notch Signaling*

S. Lincoln, J. Hardy, T. Iwatsubo, 1999, The Journal of Biological Chemistry.

Genes and mechanisms involved in β-amyloid generation and Alzheimer’s disease

H. Steiner, C. Haass, U. Leimer, 1999, European Archives of Psychiatry and Clinical Neuroscience.

Presenilin‐dependent γ‐secretase processing of β‐amyloid precursor protein at a site corresponding to the S3 cleavage of Notch

Klaus Fuchs, Harald Steiner, Christian Haass, 2001 .

Presenilin-dependent gamma-secretase processing of beta-amyloid precursor protein at a site corresponding to the S3 cleavage of Notch.

D. Teplow, G. Multhaup, C. Haass, 2001, EMBO reports.

Mitochondrial and Cytosolic Branched-chain Amino Acid Transaminases from Yeast, Homologs of the myc Oncogene-regulated Eca39 Protein*

D. A. Court, R. Lill, G. Kispál, 1996, The Journal of Biological Chemistry.

Making the final cut: pathogenic amyloid-β peptide generation by γ-secretase

S. Tagami, M. Okochi, H. Steiner, 2018, Cell stress.

Assembly, Trafficking and Function of γ-Secretase

C. Haass, C. Kaether, H. Steiner, 2006, Neurodegenerative Diseases.

The Biological and Pathological Function of the Presenilin-1 ΔExon 9 Mutation Is Independent of Its Defect to Undergo Proteolytic Processing*

M. Citron, C. Haass, Ralf Baumeister, 1999, The Journal of Biological Chemistry.

Intramembrane Proteolysis by γ-Secretase*

C. Haass, R. Fluhrer, H. Steiner, 2008, Journal of Biological Chemistry.

Clinical, pathophysiological and genetic features of motor symptoms in autosomal dominant Alzheimer's disease.

J. Morris, N. Fox, V. Buckles, 2019, Brain : a journal of neurology.

Protein Transport into and Across the Mitochondrial Outer Membrane: Recognition, Insertion and Translocation of Preproteins

A. Mayer, Petra Heckmeyer, D. A. Court, 1996 .

and R into mitochondria . preprotein receptor Tom 22 in protein import Role of the intermembrane-space domain of the

R. Hodges, W. Neupert, F. Nargang, 1996 .

Comparison of Strategies for the Determination of Sterol Sulfates via GC-MS Leading to a Novel Deconjugation-Derivatization Protocol

M. Giera, F. Kamp, C. Müller, 2019, Molecules.

Effective sample preparation procedure for the analysis of free neutral steroids, free steroid acids and sterol sulfates in different tissues by GC–MS

F. Kamp, C. Müller, F. Bracher, 2021, The Journal of Steroid Biochemistry and Molecular Biology.

Maturation and Pro-peptide Cleavage of β-Secretase*

G. Multhaup, C. Haass, J. Walter, 2000, The Journal of Biological Chemistry.

Presenilin-1 affects trafficking and processing of βAPP and is targeted in a complex with nicastrin to the plasma membrane

J. Rietdorf, C. Haass, C. Kaether, 2002, The Journal of cell biology.

The cell biology of Alzheimer's disease: uncovering the secrets of secretases

C. Haass, J. Walter, C. Kaether, 2001, Current Opinion in Neurobiology.

An Alzheimer‐associated TREM2 variant occurs at the ADAM cleavage site and affects shedding and phagocytic function

C. Haass, R. Feederle, S. Lichtenthaler, 2017, EMBO molecular medicine.

Presenilin and nicastrin regulate each other and determine amyloid β-peptide production via complex formation

C. Haass, D. Edbauer, H. Steiner, 2002, Proceedings of the National Academy of Sciences of the United States of America.

The 28-amino acid form of an APLP1-derived Aβ-like peptide is a surrogate marker for Aβ42 production in the central nervous system

T. Kudo, H. Kazui, T. Tokuda, 2009, EMBO molecular medicine.

Generation of Abeta38 and Abeta42 is independently and differentially affected by familial Alzheimer disease-associated presenilin mutations and gamma-secretase modulation.

Richard M. Page, A. Flohr, C. Haass, 2008, The Journal of biological chemistry.

Inhibition of amyloid-β plaque formation by α-synuclein

B. Hyman, M. Meyer-Luehmann, M. Prinz, 2015, Nature Medicine.

γ‐Secretase cleavage of the Alzheimer risk factor TREM2 is determined by its intrinsic structural dynamics

C. Haass, H. Steiner, F. Hagn, 2020, The EMBO journal.

Chronic γ-secretase inhibition reduces amyloid plaque-associated instability of pre- and postsynaptic structures

Richard M. Page, T Bonhoeffer, T. Bonhoeffer, 2013, Molecular Psychiatry.

Membrane lipid remodeling modulates γ-secretase processivity.

M. Giera, M. Simons, F. Kamp, 2023, The Journal of biological chemistry.

Aβ43‐producing PS1 FAD mutants cause altered substrate interactions and respond to γ‐secretase modulation

K. Baumann, R. Feederle, H. Steiner, 2019, EMBO Reports.

Identification of a rare presenilin 1 single amino acid deletion mutation (F175del) with unusual amyloid-β processing effects

A. Danek, M. Dieterich, A. Rominger, 2019, Neurobiology of Aging.

Substrate processing in intramembrane proteolysis by γ-secretase – the role of protein dynamics

D. Langosch, H. Steiner, 2017, Biological chemistry.

Substrate recruitment of γ‐secretase and mechanism of clinical presenilin mutations revealed by photoaffinity mapping

H. Steiner, A. Fukumori, Akio Fukumori, 2016, The EMBO journal.

Generation and deposition of Aβ43 by the virtually inactive presenilin‐1 L435F mutant contradicts the presenilin loss‐of‐function hypothesis of Alzheimer's disease

E. Kremmer, A. Giese, T. Arzberger, 2016, EMBO molecular medicine.

Intramembrane proteolysis of β-amyloid precursor protein by γ-secretase is an unusually slow process.

R. Fluhrer, F. Kamp, H. Steiner, 2015, Biophysical journal.

Generation of Alzheimer Disease-associated Amyloid β42/43 Peptide by γ-Secretase Can Be Inhibited Directly by Modulation of Membrane Thickness*

F. Kamp, H. Steiner, A. Fukumori, 2012, The Journal of Biological Chemistry.

Pathological activity of familial Alzheimer’s disease-associated mutant presenilin can be executed by six different γ-secretase complexes

E. Kremmer, C. Haass, H. Steiner, 2007, Neurobiology of Disease.

Reconstitution of gamma-secretase activity.

J. Regula, C. Haass, D. Edbauer, 2003, Nature cell biology.

Amyloid-PET predicts inhibition of de novo plaque formation upon chronic γ-secretase modulator treatment

A Rominger, P. Cumming, A. Rominger, 2015, Molecular Psychiatry.

Impact of partial volume effect correction on cerebral β-amyloid imaging in APP-Swe mice using [18F]-florbetaben PET

Jochen Herms, Harald Steiner, Karlheinz Baumann, 2014, NeuroImage.

Generation of Aβ38 and Aβ42 Is Independently and Differentially Affected by Familial Alzheimer Disease-associated Presenilin Mutations and γ-Secretase Modulation*

Richard M. Page, A. Flohr, C. Haass, 2008, Journal of Biological Chemistry.

Photo-controlled delivery of very long chain fatty acids to cell membranes and modulation of membrane protein function.

M. Giera, A. Kros, Frederick Campbell, 2020, Biochimica et biophysica acta. Biomembranes.

Active γ-Secretase Complexes Contain Only One of Each Component*

B. de Strooper, M. Wolfe, Y. Ihara, 2007, Journal of Biological Chemistry.

γ-Secretase Activity Is Associated with a Conformational Change of Nicastrin*

J. Schmitz, C. Haass, D. Edbauer, 2003, The Journal of Biological Chemistry.

The presenilin C‐terminus is required for ER‐retention, nicastrin‐binding and γ‐secretase activity

C. Haass, C. Kaether, D. Edbauer, 2004, The EMBO journal.

Maturation and pro-peptide cleavage of beta-secretase.

G. Multhaup, C. Haass, J. Walter, 2000, The Journal of biological chemistry.

γ-Secretase Inhibition Reduces Spine Density In Vivo via an Amyloid Precursor Protein-Dependent Pathway

H. Kretzschmar, G. Mitteregger, C. Volbracht, 2009, The Journal of Neuroscience.

Differential Localization and Identification of a Critical Aspartate Suggest Non-redundant Proteolytic Functions of the Presenilin Homologues SPPL2b and SPPL3*

P. Krawitz, C. Haass, R. Fluhrer, 2005, Journal of Biological Chemistry.

An in vivo assay for the identification of target proteases which cleave membrane‐associated substrates

C. Haass, H. Steiner, B. Pesold, 1999, FEBS letters.

Attenuated Aβ42 Responses to Low Potency γ-Secretase Modulators Can Be Overcome for Many Pathogenic Presenilin Mutants by Second-generation Compounds*

Richard M. Page, C. Haass, K. Baumann, 2011, The Journal of Biological Chemistry.

Different transmembrane domains determine the specificity and efficiency of the cleavage activity of the γ-secretase subunit presenilin

M. Okochi, D. Langosch, H. Steiner, 2023, The Journal of biological chemistry.

Cooperation of N- and C-terminal substrate transmembrane domain segments in intramembrane proteolysis by γ-secretase

D. Langosch, S. Lichtenthaler, Walter Stelzer, 2023, Communications Biology.

Active site geometry stabilization of a presenilin homolog by the lipid bilayer promotes intramembrane proteolysis

M. Zacharias, R. Feederle, H. Steiner, 2022, bioRxiv.

Secretases in Alzheimer's disease: Novel insights into proteolysis of APP and TREM2

S. Lichtenthaler, S. Tschirner, H. Steiner, 2021, Current Opinion in Neurobiology.

Pathogenic Aβ generation in familial Alzheimer’s disease: novel mechanistic insights and therapeutic implications

H. Steiner, A. Fukumori, J. Trambauer, 2020, Current Opinion in Neurobiology.

Ab43-producing PS1 FAD mutants cause altered substrate interactions and respond to c-secretase modulation

K. Baumann, R. Feederle, H. Steiner, 2019 .

The GxGD Motif of Presenilin Contributes to Catalytic Function and Substrate Identification of γ-Secretase

S. Eimer, M. Okochi, C. Haass, 2006, The Journal of Neuroscience.

Understanding intramembrane proteolysis: from protein dynamics to reaction kinetics.

D. Langosch, C. Scharnagl, H. Steiner, 2015, Trends in biochemical sciences.

Cross-Sectional Comparison of Small Animal [18F]-Florbetaben Amyloid-PET between Transgenic AD Mouse Models

P. Cumming, A. Rominger, J. Herms, 2014, PloS one.

Loss of PAFAH1B2 Reduces Amyloid-β Generation by Promoting the Degradation of Amyloid Precursor Protein C-Terminal Fragments

M. Boutros, T. Horn, O. Reiner, 2012, The Journal of Neuroscience.

Modulation of γ-Secretase Activity by a Carborane-Based Flurbiprofen Analogue

Jens Pietzsch, E. Hey‐Hawkins, H. Steiner, 2021, Molecules.

Amyloidogenic function of the Alzheimer's disease-associated presenilin 1 in the absence of endoproteolysis.

M. Citron, H. Loetscher, C. Haass, 1999, Biochemistry.

The yeast ER-intramembrane protease Ypf1 refines nutrient sensing by regulating transporter abundance.

M. Schuldiner, E. Kremmer, Michal Breker, 2014, Molecular cell.

Scaffold of the cyclooxygenase-2 (COX-2) inhibitor carprofen provides Alzheimer gamma-secretase modulators.

C. Haass, K. Baumann, R. Narlawar, 2006, Journal of medicinal chemistry.

N-Substituted carbazolyloxyacetic acids modulate Alzheimer associated γ-secretase

C. Haass, K. Baumann, R. Narlawar, 2007 .

Endoplasmic reticulum retention of the gamma-secretase complex component Pen2 by Rer1.

C. Haass, C. Kaether, S. Kacmar, 2007, EMBO reports.

γ-Secretase Complex Assembly within the Early Secretory Pathway*

C. Haass, C. Kaether, S. Prokop, 2005, Journal of Biological Chemistry.

Alzheimer disease gamma-secretase: a complex story of GxGD-type presenilin proteases.

C. Haass, H. Steiner, 2002, Trends in cell biology.

Nicastrin Interacts with γ-Secretase Complex Components via the N-terminal Part of Its Transmembrane Domain*

C. Haass, C. Kaether, D. Edbauer, 2003, Journal of Biological Chemistry.

Analyzing Amyloid-β Peptide Modulation Profiles and Binding Sites of γ-Secretase Modulators.

H. Steiner, A. Fukumori, B. Kretner, 2017, Methods in enzymology.

Intramembrane Proteolysis by Signal Peptide Peptidases: A Comparative Discussion of GXGD-type Aspartyl Proteases*

Harald Steiner, Christian Haass, C. Haass, 2009, Journal of Biological Chemistry.

Immature nicastrin stabilizes APH‐1 independent of PEN‐2 and presenilin: identification of nicastrin mutants that selectively interact with APH‐1

Harald Steiner, Christian Haass, C. Haass, 2004, Journal of neurochemistry.

N-Substituted carbazolyloxyacetic acids modulate Alzheimer associated gamma-secretase.

C. Haass, K. Baumann, R. Narlawar, 2007, Bioorganic & medicinal chemistry letters.

Bexarotene Binds to the Amyloid Precursor Protein Transmembrane Domain, Alters Its α-Helical Conformation, and Inhibits γ-Secretase Nonselectively in Liposomes.

C. Sanders, H. Scheidt, D. Huster, 2018, ACS chemical neuroscience.

AAontology: An ontology of amino acid scales for interpretable machine learning

D. Frishman, F. Kamp, H. Steiner, 2024, bioRxiv.

Protofibrils, the unifying toxic molecule of neurodegenerative disorders?

C. Haass, H. Steiner, 2001, Nature Neuroscience.

Monitoring of chronic γ-secretase modulator treatment by serial amyloid-PET

P. Cumming, A. Rominger, J. Herms, 2015, Molecular Psychiatry.

The GxGD Motif of Presenilin Contributes to Catalytic Function and Substrate Identification of (cid:1) -Secretase

S. Eimer, M. Okochi, C. Haass, 2006 .

The catalytic core of gamma-secretase: presenilin revisited.

H. Steiner, 2008, Current Alzheimer Research.

Enzyme-substrate hybrid β-sheet controls geometry and water access to the γ-secretase active site

L. Chávez-Gutiérrez, H. Steiner, M. Zacharias, 2023, Communications biology.

The 28-amino acid form of an APLP1-derived Aβ-like peptide is a surrogate marker for Aβ42 production in the central nervous system

T. Kudo, H. Kazui, T. Tokuda, 2009, EMBO molecular medicine.

Assembly, trafficking and function of gamma-secretase.

C. Kaether, H. Steiner, Christian Haass, 2006, Neuro-degenerative diseases.