威尼斯赌博游戏_威尼斯赌博app-【官网】

图片

威尼斯赌博游戏_威尼斯赌博app-【官网】

图片

Prof. Dr. Regina Fluhrer

Lehrstuhlinhaberin
Biochemie und Molekularbiologie
Telefon: +49 (0) 821 598-71014
E-Mail:
Raum: A-EG-021 Neus?? (Universit?tsmedizin Augsburg / Gutenbergstra?e 7)
Adresse: Gutenbergstra?e 7, 86356 Neus??
Postanschrift: Universit?tsstra?e 2, 86159 Augsburg

Vita

Prof. Dr. rer. nat. Regina Fluhrer studierte Lebensmittelchemie an der Ludwig-Maximilians-Universit?t München (LMU) und der Technischen Universit?t München (TUM). Im Rahmen ihrer Promotion (2000–2003) am Institut für Stoffwechselbiochemie der LMU München untersuchte sie die katalytischen Spezifit?ten der beiden Aspartylproteasen BACE-1 (?-site APP cleaving enzyme), einem Schlüsselfaktor bei der Entstehung der Alzheimererkrankung, und BACE-2. Als Postdoktorandin (2003–2005) begann Prof. Fluhrer sich zunehmend für Intramembranproteasen zu interessieren. 2008 schloss sie ihre Habilitationsarbeit ab und leitete bis 2019 eine wissenschaftliche Arbeitsgruppe an der LMU München sowie am Deutschen Zentrum für Neurodegenerative Erkrankungen (DZNE), die sich schwerpunktm??ig mit der Funktion der Signalpeptid-Peptidase-Familie (SPP/SPPL) besch?ftigt.

Für ihre Forschungsarbeiten erhielt sie den B?hringer-Ingelheim-APOPIS-Preis für Nachwuchswissenschaftler. Von 2006 bis 2019 leitete Prof. Fluhrer hauptverantwortlich die Seminare der Biochemie/Molekularbiologie für Studierende der Human- und Zahnmedizin an der LMU München.

Seit April 2019 ist sie Inhaberin des Lehrstuhls für Biochemie und Molekularbiologie an der neu gegründeten medizinischen Fakult?t der Universit?t Augsburg. Sie engagiert sich in zahlreichen Gremien für die Weiterentwicklung des medizinischen Curriculums und wurde dafür 2012 mit dem Preis für gute Lehre des bayerischen Staatsministers ausgezeichnet.

Forschungsschwerpunkte

  • Die?Forschung?der Arbeitsgruppe von Prof. Fluhrer besch?ftigt sich schwerpunktm??ig mit Proteolyse-Vorg?ngen, die in zellul?ren Membranen stattfinden.?
  • Künftige Forschungsprojekte werden sich u.a. mit der Regulation von Intramembranproteasen im Kontext von Tumorentwicklung, Adipositas, Typ II Diabetes du Immunologischen Erkrankungen besch?ftigen.
  • Weiterhin werden wir untersuchen, wie sich verschiedene Umwelteinflüsse und Ern?hrungsgewohnheiten auf diese Proteasen auswirken.

Forschung Biochemie / Molekularbiologie

Mitgliedschaften

  • Mitglied der Gesellschaft für Biochemie und Molekularbiologie e.V. (GBM)
  • Mitglied des Arbeitskreises Biochemie in der 威尼斯赌博游戏_威尼斯赌博app-【官网】izin in der GBM
  • Mitglied der International Proteolysis Society (IPS)
  • Mitglied in PROTEOCURE

Publikationen

2024 | 2023 | 2022 | 2020 | 2019 | 2018 | 2017 | 2016 | 2015 | 2014 | 2013 | 2012 | 2011 | 2010 | 2009 | 2008 | 2007 | 2006 | 2005 | 2003 | 2002 | 2001

2024

Sharrouf Kinda, Schlosser Christine, Mildenberger Sandra, Fluhrer Regina, Hoeppner Sabine. In vitro cleavage of tumor necrosis factor α (TNFα) by Signal-Peptide-Peptidase-like 2b (SPPL2b) resembles mechanistic principles observed in the cellular context. https://doi.org/10.1016/j.cbi.2024.111006
BibTeX | RIS | DOI
Maccioni Riccardo, Travisan Caterina, Badman Jack, Zerial Stefania, Wagener Annika, Andrade-Talavera Yuniesky, Picciau Federico, Grassi Caterina, Chen Gefei, Lemoine Laetitia, Fisahn André, Jiang Richeng, Fluhrer Regina, Mentrup Torben, Schr?der Bernd, Nilsson Per, Tambaro Simone. Signal peptide peptidase-like 2b modulates the amyloidogenic pathway and exhibits an Aβ-dependent expression in Alzheimer's disease. https://doi.org/10.1016/j.pneurobio.2024.102585
BibTeX | RIS | DOI
Mentrup Torben, Leinung Nadja, Patel Mehul, Fluhrer Regina, Schr?der Bernd. The role of SPP/SPPL intramembrane proteases in membrane protein homeostasis. https://doi.org/10.1111/febs.16941
PDF | BibTeX | RIS | DOI

2023

Smit P., Buehring-Uhle C., Nather C., Negraschus A., Goldmann U., Papadopoulou Alkmini A., Riviere J., Morath V., Henkel E., Bromberger T., Goetze K., Heinz L., Fluhrer Regina, Moser M., Superti-Furga G., Bassermann F., Eichner R.. Inhibiting MGAT1-mediated N-glycosylation reduces proliferation and adhesion of AML cells and increases affinities of anti-SLC3A2 directed immunotherapies [Abstract]. https://doi.org/10.1159/000533576
PDF | BibTeX | RIS | DOI
Hoeppner Sabine, Schr?der Bernd, Fluhrer Regina. Structure and function of SPP/SPPL proteases: insights from biochemical evidence and predictive modeling. https://doi.org/10.1111/febs.16968
PDF | BibTeX | RIS | DOI

2022

Heard Amanda, Landmann Jack H., Hansen Ava R., Papadopolou Alkmini, Hsu Yu-Sung, Selli Mehmet Emrah, Warrington John M., Lattin John, Chang Jufang, Ha Helen, Haug-Kr?per Martina, Doray Balraj, Gill Saar, Ruella Marco, Hayer Katharina E., Weitzman Matthew D., Green Abby M., Fluhrer Regina, Singh Nathan. Antigen glycosylation regulates efficacy of CAR T cells targeting CD19. https://doi.org/10.1038/s41467-022-31035-7
PDF | BibTeX | RIS | DOI
Papadopoulou Alkmini A., Stelzer Walter, Silber Mara, Schlosser Christine, Spitz Charlotte, Haug-Kr?per Martina, Straub Tobias, Müller Stephan A., Lichtenthaler Stefan F., Muhle-Goll Claudia, Langosch Dieter, Fluhrer Regina. Helical stability of the GnTV transmembrane domain impacts on SPPL3 dependent cleavage. https://doi.org/10.1038/s41598-022-24772-8
PDF | BibTeX | RIS | DOI
Mentrup Torben, Stumpff-Niggemann Anna Yamina, Leinung Nadja, Schlosser Christine, Schubert Katja, Wehner Rebekka, Tunger Antje, Schatz Valentin, Neubert Patrick, Gradtke Ann-Christine, Wolf Janina, Rose-John Stefan, Saftig Paul, Dalpke Alexander, Jantsch Jonathan, Schmitz Marc, Fluhrer Regina, Jacobsen Ilse D., Schr?der Bernd. Phagosomal signalling of the C-type lectin receptor Dectin-1 is terminated by intramembrane proteolysis. https://doi.org/10.1038/s41467-022-29474-3
PDF | BibTeX | RIS | DOI
Bühring-Uhle C., Smit P., Negraschus A., Morath V., Goldmann U., Papadopoulou Alkmini A., Heider M., Riviere J., G?tze K., Heinz L., Fluhrer Regina, Moser M., Superti-Furga G., Bassermann F., Eichner R.. SPPL3 and its substrate glycosyltransferases regulate the N-glycosylation of SLC3A2 and alter the affinities of anti-SLC3A2 immunotherapies in AML [Abstract]. https://doi.org/10.1159/000526456
PDF | BibTeX | RIS | DOI

2020

Spitz Charlotte, Schlosser Christine, Guschtschin-Schmidt Nadja, Stelzer Walter, Menig Simon, G?tz Alexander, Haug-Kr?per Martina, Scharnagl Christina, Langosch Dieter, Muhle-Goll Claudia, Fluhrer Regina. Non-canonical shedding of TNFα by SPPL2a is determined by the conformational flexibility of its transmembrane helix. https://doi.org/10.1016/j.isci.2020.101775
PDF | BibTeX | RIS | DOI
Mentrup Torben, Cabrera-Cabrera Florencia, Fluhrer Regina, Schr?der Bernd. Physiological functions of SPP/SPPL intramembrane proteases. https://doi.org/10.1007/s00018-020-03470-6
PDF | BibTeX | RIS | DOI
Papadopoulou Alkmini A., Fluhrer Regina. Signalling functions of intramembrane aspartyl-proteases. https://doi.org/10.3389/fcvm.2020.591787
PDF | BibTeX | RIS | DOI
Brugger Manuel S., Baumgartner Kathrin, Mauritz Sophie C. F., Gerlach Stefan C., R?der Florian, Schlosser Christine, Fluhrer Regina, Wixforth Achim, Westerhausen Christoph. Vibration enhanced cell growth induced by surface acoustic waves as in vitro wound healing model. https://doi.org/10.1073/pnas.2005203117
PDF | BibTeX | RIS | DOI

2019

Mentrup Torben, Theodorou Kosta, Cabrera-Cabrera Florencia, Helbig Andreas O., Happ Kathrin, Gijbels Marion, Gradtke Ann-Christine, Rabe Bj?rn, Fukumori Akio, Steiner Harald, Tholey Andreas, Fluhrer Regina, Donners Marjo, Schr?der Bernd. Atherogenic LOX-1 signaling is controlled by SPPL2-mediated intramembrane proteolysis. https://doi.org/10.1084/jem.20171438
PDF | BibTeX | RIS | DOI
Fluhrer Regina, Hampe Wolfgang, editors. Biochemie hoch 2 und Molekularbiologie.
BibTeX | RIS
Fluhrer Regina. Intramembrane proteases in neurodegenerative diseases.
PDF | BibTeX | RIS | URL
Fluhrer Regina. Intramembrane proteases in the immune system.
PDF | BibTeX | RIS | URL
Papadopoulou Alkmini A., Müller Stephan A, Mentrup Torben, Shmueli Merav D, Niemeyer Johannes, Haug‐Kr?per Martina, von Blume Julia, Mayerhofer Artur, Feederle Regina, Schr?der Bernd, Lichtenthaler Stefan F., Fluhrer Regina. Signal peptide peptidase‐like 2c (SPPL2c) impairs vesicular transport and cleavage of SNARE proteins. https://doi.org/10.15252/embr.201846451
PDF | BibTeX | RIS | DOI
Niemeyer Johannes, Mentrup Torben, Heidasch Ronny, Müller Stephan A, Biswas Uddipta, Meyer Rieke, Papadopoulou Alkmini A., Dederer Verena, Haug‐Kr?per Martina, Adamski Vivian, Lüllmann-Rauch Renate, Bergmann Martin, Mayerhofer Artur, Saftig Paul, Wennemuth Gunther, Jessberger Rolf, Fluhrer Regina, Lichtenthaler Stefan F., Lemberg Marius K, Schr?der Bernd. The intramembrane protease SPPL2c promotes male germ cell development by cleaving?phospholamban. https://doi.org/10.15252/embr.201846449
PDF | BibTeX | RIS | DOI
Fluhrer Regina, Schr?der Bernd. What is the role of the intramembrane proteases in cancer?.
PDF | BibTeX | RIS | URL

2018

Fluhrer Regina. A unique family of intramembrane proteases. https://doi.org/10.26320/SCIENTIA179
PDF | BibTeX | RIS | DOI | URL
Fluhrer Regina. Health report: the challenge of cleaving proteins in the membrane.
PDF | BibTeX | RIS | URL
Fluhrer Regina. Intramembrane proteases - regulators of cellular pathways.
PDF | BibTeX | RIS | URL
Lichtenthaler Stefan F., Lemberg Marius K., Fluhrer Regina. Proteolytic ectodomain shedding of membrane proteins in mammals - hardware, concepts, and recent developments. https://doi.org/10.15252/embj.201899456
PDF | BibTeX | RIS | DOI

2017

Jules Felix, Sauvageau Etienne, Dumaresq-Doiron Karine, Mazzaferri Javier, Haug-Kr?per Martina, Fluhrer Regina, Costantino Santiago, Lefrancois Stephane. CLN5 is cleaved by members of the SPP/SPPL family to produce a mature soluble protein. https://doi.org/10.1016/j.yexcr.2017.04.024
PDF | BibTeX | RIS | DOI
Mentrup Torben, Fluhrer Regina, Schr?der Bernd. Latest emerging functions of SPP/SPPL intramembrane proteases. https://doi.org/10.1016/j.ejcb.2017.03.002
PDF | BibTeX | RIS | DOI
Mentrup Torben, Loock Ann-Christine, Fluhrer Regina, Schr?der Bernd. Signal peptide peptidase and SPP-like proteases: possible therapeutic targets?. https://doi.org/10.1016/j.bbamcr.2017.06.007
PDF | BibTeX | RIS | DOI

2016

Hüttl Susann, Helfrich F., Mentrup Torben, Held S., Fukumori Akio, Steiner Harald, Saftig Paul, Fluhrer Regina, Schroder B.. Substrate determinants of signal peptide peptidase-like 2a (SPPL2a)-mediated intramembrane proteolysis of the invariant chain CD74. https://doi.org/10.1042/bcj20160156
PDF | BibTeX | RIS | DOI

2015

Mentrup Torben, H?sler Robert, Fluhrer Regina, Saftig Paul, Schr?der Bernd. A cell-based assay reveals nuclear translocation of intracellular domains released by SPPL proteases. https://doi.org/10.1111/tra.12287
PDF | BibTeX | RIS | DOI
Kamp Frits, Winkler Edith, Trambauer Johannes, Ebke Amelie, Fluhrer Regina, Steiner Harald. Intramembrane proteolysis of β-amyloid precursor protein by γ-secretase is an unusually slow process. https://doi.org/10.1016/j.bpj.2014.12.045
PDF | BibTeX | RIS | DOI
Fleck Daniel, Voss Matthias, Brankatschk Ben, Giudici Camilla, Hampel Heike, Schwenk Benjamin, Edbauer Dieter, Fukumori Akio, Steiner Harald, Kremmer Elisabeth, Haug-Kr?per Martina, Rossner Moritz J., Fluhrer Regina, Willem Michael, Haass Christian. Proteolytic processing of neuregulin 1 type III by three intramembrane-cleaving proteases. https://doi.org/10.1074/jbc.m115.697995
PDF | BibTeX | RIS | DOI
Kuhn Peer-Hendrik, Voss Matthias, Haug-Kr?per Martina, Schr?der Bernd, Schepers Ute, Br?se Stefan, Haass Christian, Lichtenthaler Stefan F., Fluhrer Regina. Secretome analysis identifies novel signal peptide peptidase-like 3 (Sppl3) substrates and reveals a role of Sppl3 in multiple Golgi glycosylation pathways. https://doi.org/10.1074/mcp.m115.048298
PDF | BibTeX | RIS | DOI

2014

Fluhrer Regina. Intramembrane cleaving proteases (I-CLiPs) as guardians of shuttling proteins. https://doi.org/10.4161/cc.28089
PDF | BibTeX | RIS | DOI
Voss Matthias, Künzel Ulrike, Higel Fabian, Kuhn Peer‐Hendrik, Colombo Alessio, Fukumori Akio, Haug‐Kr?per Martina, Klier B?rbel, Grammer Gudula, Seidl Andreas, Schr?der Bernd, Obst Reinhard, Steiner Harald, Lichtenthaler Stefan F., Haass Christian, Fluhrer Regina. Shedding of glycan‐modifying enzymes by signal peptide peptidase‐like 3 (SPPL3) regulates cellular N‐glycosylation. https://doi.org/10.15252/embj.201488375
PDF | BibTeX | RIS | DOI
Schneppenheim Janna, Hüttl Susann, Kruchen Anne, Fluhrer Regina, Müller Ingo, Saftig Paul, Schneppenheim Reinhard, Martin Christa L., Schr?der Bernd. Signal-peptide-peptidase-like 2a is required for CD74 intramembrane proteolysis in human B cells. https://doi.org/10.1016/j.bbrc.2014.07.051
PDF | BibTeX | RIS | DOI
Schneppenheim Janna, Hüttl Susann, Mentrup Torben, Lüllmann-Rauch Renate, Rothaug M., Engelke Michael, Dittmann Kai, Dressel Ralf, Araki M., Araki K., Wienands Jürgen, Fluhrer Regina, Saftig Paul, Schroder B.. The intramembrane proteases signal peptide peptidase-like 2a and 2b have distinct functions in vivo. https://doi.org/10.1128/mcb.00038-14
PDF | BibTeX | RIS | DOI

2013

Voss Matthias, Schr?der Bernd, Fluhrer Regina. Mechanism, specificity, and physiology of signal peptide peptidase (SPP) and SPP-like proteases. https://doi.org/10.1016/j.bbamem.2013.03.033
PDF | BibTeX | RIS | DOI
Poggi Marjorie, Kara Imène, Brunel Jean-Michel, Landrier Jean-Fran?ois, Govers Roland, Bonardo Bernadette, Fluhrer Regina, Haass Christian, Alessi Marie-Christine, Peiretti Franck. Palmitoylation of TNF alpha is involved in the regulation of TNF receptor 1 signalling. https://doi.org/10.1016/j.bbamcr.2012.11.009
PDF | BibTeX | RIS | DOI
Bronckers Antonius LJJ, Gueneli Nur, Lüllmann-Rauch Renate, Schneppenheim Janna, Moraru Andreea P, Himmerkus Nina, Bervoets Theodore J, Fluhrer Regina, Everts Vincent, Saftig Paul, Schr?der Bernd. The intramembrane protease SPPL2A is critical for tooth enamel formation. https://doi.org/10.1002/jbmr.1895
PDF | BibTeX | RIS | DOI
Zahn Claudia, Kaup Matthias, Fluhrer Regina, Fuchs Hendrik. The transferrin receptor-1 membrane stub undergoes intramembrane proteolysis by signal peptide peptidase-like 2b. https://doi.org/10.1111/febs.12176
PDF | BibTeX | RIS | DOI

2012

Voss Matthias, Fukumori Akio, Kuhn Peer-Hendrik, Künzel Ulrike, Klier B?rbel, Grammer Gudula, Haug-Kr?per Martina, Kremmer Elisabeth, Lichtenthaler Stefan F., Steiner Harald, Schr?der Bernd, Haass Christian, Fluhrer Regina. Foamy virus envelope protein is a substrate for signal peptide peptidase-like 3 (SPPL3). https://doi.org/10.1074/jbc.m112.371369
PDF | BibTeX | RIS | DOI
Schneppenheim Janna, Dressel Ralf, Hüttl Susann, Lüllmann-Rauch Renate, Engelke Michael, Dittmann Kai, Wienands Jürgen, Eskelinen Eeva-Liisa, Hermans-Borgmeyer Irm, Fluhrer Regina, Saftig Paul, Schr?der Bernd. The intramembrane protease SPPL2a promotes B cell development and controls endosomal traffic by cleavage of the invariant chain. https://doi.org/10.1084/jem.20121069
PDF | BibTeX | RIS | DOI

2011

Fluhrer Regina, Kamp Frits, Grammer Gudula, Nuscher Brigitte, Steiner Harald, Beyer Klaus, Haass Christian. The nicastrin ectodomain adopts a highly thermostable structure. https://doi.org/10.1515/bc.2011.169
PDF | BibTeX | RIS | DOI
Fluhrer Regina, Martin Lucas, Klier B?rbel, Haug-Kr?per Martina, Grammer Gudula, Nuscher Brigitte, Haass Christian. The α-helical content of the transmembrane domain of the British dementia protein-2 (Bri2) determines its processing by signal peptide peptidase-like 2b (SPPL2b). https://doi.org/10.1074/jbc.m111.328104
PDF | BibTeX | RIS | DOI

2010

Fukumori Akio, Fluhrer Regina, Steiner Harald, Haass Christian. Three-amino acid spacing of presenilin endoproteolysis suggests a general stepwise cleavage of gamma-secretase-mediated intramembrane proteolysis. https://doi.org/10.1523/jneurosci.1443-10.2010
PDF | BibTeX | RIS | DOI

2009

Fluhrer Regina, Steiner Harald, Haass Christian. Intramembrane proteolysis by signal peptide peptidases: a comparative discussion of GXGD-type aspartyl proteases. https://doi.org/10.1074/jbc.r800040200
PDF | BibTeX | RIS | DOI
Fluhrer Regina, Haass Christian. Intramembrane proteolysis by γ-secretase and signal peptide peptidases. https://doi.org/10.1007/978-3-540-87941-1_2
PDF | BibTeX | RIS | DOI
Martin Lucas, Fluhrer Regina, Haass Christian. Substrate requirements for SPPL2b-dependent regulated intramembrane proteolysis. https://doi.org/10.1074/jbc.m807485200
PDF | BibTeX | RIS | DOI

2008

Steiner Harald, Fluhrer Regina, Haass Christian. Intramembrane proteolysis by γ-secretase. https://doi.org/10.1074/jbc.r800010200
PDF | BibTeX | RIS | DOI
Fluhrer Regina, Fukumori Akio, Martin Lucas, Grammer Gudula, Haug-Kr?per Martina, Klier B?rbel, Winkler Edith, Kremmer Elisabeth, Condron Margaret M., Teplow David B., Steiner Harald, Haass Christian. Intramembrane proteolysis of GXGD-type aspartyl proteases is slowed by a familial Alzheimer disease-like mutation. https://doi.org/10.1074/jbc.m806092200
PDF | BibTeX | RIS | DOI

2007

Prager Kai, Wang-Eckhardt Lihua, Fluhrer Regina, Killick Richard, Barth Esther, Hampel Heike, Haass Christian, Walter Jochen. A structural switch of presenilin 1 by glycogen synthase kinase 3beta-mediated phosphorylation regulates the interaction with beta-catenin and its nuclear signaling. https://doi.org/10.1074/jbc.m608437200
PDF | BibTeX | RIS | DOI
Martin Lucas, Fluhrer Regina, Reiss Karina, Kremmer Elisabeth, Saftig Paul, Haass Christian. Regulated intramembrane proteolysis of Bri2 (Itm2b) by ADAM10 and SPPL2a/SPPL2b. https://doi.org/10.1074/jbc.m706661200
PDF | BibTeX | RIS | DOI
Fluhrer Regina, Haass Christian. Signal peptide peptidases and gamma-secretase: cousins of the same protease family?. https://doi.org/10.1159/000101835
PDF | BibTeX | RIS | DOI

2006

Fluhrer Regina, Grammer Gudula, Israel Lars, Condron Margaret M., Haffner Christof, Friedmann Elena, B?hland Claudia, Imhof Axel, Martoglio Bruno, Teplow David B., Haass Christian. A γ-secretase-like intramembrane cleavage of TNFα by the GxGD aspartyl protease SPPL2b. https://doi.org/10.1038/ncb1450
PDF | BibTeX | RIS | DOI

2005

Krawitz Peter, Haffner Christof, Fluhrer Regina, Steiner Harald, Schmid Bettina, Haass Christian. Differential localization and identification of a critical aspartate suggest non-redundant proteolytic functions of the presenilin homologues SPPL2b and SPPL3. https://doi.org/10.1074/jbc.m501645200
PDF | BibTeX | RIS | DOI

2003

Fluhrer Regina, Multhaup Gerd, Schlicksupp Andrea, Okochi Masayasu, Takeda Masatoshi, Lammich Sven, Willem Michael, Westmeyer Gil, Bode Wolfram, Walter Jochen, Haass Christian. Identification of a beta-secretase activity, which truncates amyloid beta-peptide after its presenilin-dependent generation. https://doi.org/10.1074/jbc.m211485200
PDF | BibTeX | RIS | DOI
Fluhrer Regina, Friedlein Arno, Haass Christian, Walter Jochen. Phosphorylation of presenilin 1 at the caspase recognition site regulates its proteolytic processing and the progression of apoptosis. https://doi.org/10.1074/jbc.m306653200
PDF | BibTeX | RIS | DOI
Fluhrer Regina. Zwei neuartige Aspartylproteasen BACE-1 und BACE-2: Charakterisierung und Vergleich der katalytischen Spezifit?ten bei der Proteolyse des Alzheimer-β-Amyloid-Vorl?ufer-Proteins.
PDF | BibTeX | RIS | URL

München, Univ., Diss., 2003

2002

Fluhrer Regina, Capell Anja, Westmeyer Gil, Willem Michael, Hartung Bianka, Condron Margaret M., Teplow David B., Haass Christian, Walter Jochen. A non-amyloidogenic function of BACE-2 in the secretory pathway. https://doi.org/10.1046/j.1471-4159.2002.00908.x
PDF | BibTeX | RIS | DOI
Capell Anja, Meyn Liane, Fluhrer Regina, Teplow David B., Walter Jochen, Haass Christian. Apical sorting of beta-secretase limits amyloid beta-peptide production. https://doi.org/10.1074/jbc.m109119200
PDF | BibTeX | RIS | DOI

2001

Walter Jochen, Fluhrer Regina, Hartung Bianka, Willem Michael, Kaether Christoph, Capell Anja, Lammich Sven, Multhaup Gerd, Haass Christian. Phosphorylation regulates intracellular trafficking of beta-secretase. https://doi.org/10.1074/jbc.m011116200
PDF | BibTeX | RIS | DOI

Suche