Zobrazeno 1 - 10 of 10 pro vyhledávání: '"Martina Haug-Kröper"'
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Akademický článek
Helical stability of the GnTV transmembrane domain impacts on SPPL3 dependent cleavage
Autor: Alkmini A. Papadopoulou, Walter Stelzer, Mara Silber, Christine Schlosser, Charlotte Spitz, Martina Haug-Kröper, Tobias Straub, Stephan A. Müller, Stefan F. Lichtenthaler, Claudia Muhle-Goll, Dieter Langosch, Regina Fluhrer
Publikováno v: Scientific Reports, Vol 12, Iss 1, Pp 1-18 (2022)
Abstract Signal-Peptide Peptidase Like-3 (SPPL3) is an intramembrane cleaving aspartyl protease that causes secretion of extracellular domains from type-II transmembrane proteins. Numerous Golgi-localized glycosidases and glucosyltransferases have be
Externí odkaz: https://doaj.org/article/9faad70949594762948f92ade4978291
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2
Akademický článek
Non-canonical Shedding of TNFα by SPPL2a Is Determined by the Conformational Flexibility of Its Transmembrane Helix
Autor: Charlotte Spitz, Christine Schlosser, Nadja Guschtschin-Schmidt, Walter Stelzer, Simon Menig, Alexander Götz, Martina Haug-Kröper, Christina Scharnagl, Dieter Langosch, Claudia Muhle-Goll, Regina Fluhrer
Publikováno v: iScience, Vol 23, Iss 12, Pp 101775- (2020)
Summary: Ectodomain (EC) shedding defines the proteolytic removal of a membrane protein EC and acts as an important molecular switch in signaling and other cellular processes. Using tumor necrosis factor (TNF)α as a model substrate, we identify a no
Externí odkaz: https://doaj.org/article/c3b63148f6c64088b959a5bd718b3a1c
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3
Signal Peptide Peptidase-Like 2c (SPPL2c) impairs vesicular transport and cleavage of SNARE proteins
Autor: Regina Fluhrer, Stefan F. Lichtenthaler, Johannes Niemeyer, Stephan A. Müller, Julia von Blume, Bernd Schröder, Regina Feederle, Merav D. Shmueli, Artur Mayerhofer, Martina Haug-Kröper, Alkmini A Papadopoulou, Torben Mentrup
Publikováno v: EMBO reports 20(3), e46451 (2019). doi:10.15252/embr.201846451
EMBO Reports
Members of the GxGD-type intramembrane aspartyl proteases have emerged as key players not only in fundamental cellular processes such as B-cell development or protein glycosylation, but also in development of pathologies, such as Alzheimer's disease
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1bc37106768cfa96107d57a8a01ff477
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5
Proteolytic Processing of Neuregulin 1 Type III by Three Intramembrane-cleaving Proteases
Autor: Daniel Fleck, Camilla Giudici, Matthias Voss, Michael Willem, Dieter Edbauer, Elisabeth Kremmer, Moritz J. Rossner, Martina Haug-Kröper, Akio Fukumori, Christian Haass, Harald Steiner, Ben Brankatschk, Benjamin M. Schwenk, Regina Fluhrer, Heike Hampel
Publikováno v: The journal of biological chemistry 291(1), 318-333 (2015). doi:10.1074/jbc.M115.697995
J. Biol. Chem. 291, 318-333 (2016)
Numerous membrane-bound proteins undergo regulated intramembrane proteolysis. Regulated intramembrane proteolysis is initiated by shedding, and the remaining stubs are further processed by intramembrane-cleaving proteases (I-CLiPs). Neuregulin 1 type
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::35971ce3c86b99465f7c5da97b1b0cb9
https://doi.org/10.1074/jbc.m115.697995
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6
Secretome Analysis Identifies Novel Signal Peptide Peptidase-Like 3 (SPPL3) Substrates and Reveals a Role of SPPL3 in Multiple Golgi Glycosylation Pathways*
Autor: Bernd Schröder, Martina Haug-Kröper, Regina Fluhrer, Stefan Bräse, Ute Schepers, Matthias Voss, Peer-Hendrik Kuhn, Stefan F. Lichtenthaler, Christian Haass
Publikováno v: Molecular & cellular proteomics 14(6), 1584-1598 (2015). doi:10.1074/mcp.M115.048298
Signal peptide peptidase-like 3 (Sppl3) is a Golgi-resident intramembrane-cleaving protease that is highly conserved among multicellular eukaryotes pointing to pivotal physiological functions in the Golgi network which are only beginning to emerge. R
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e4413a9aae1537ba327ac3e21ec35e35
https://doi.org/10.1074/mcp.m115.048298
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7
CLN5 is cleaved by members of the SPP/SPPL family to produce a mature soluble protein
Autor: Regina Fluhrer, Etienne Sauvageau, Santiago Costantino, Martina Haug-Kröper, Javier Mazzaferri, Karine Dumaresq-Doiron, Felix Jules, Stephane Lefrancois
Publikováno v: Experimental Cell Research
Experimental Cell Research, Elsevier, 2017, ⟨10.1016/j.yexcr.2017.04.024⟩
Experimental cell research 357(1), 40-50 (2017). doi:10.1016/j.yexcr.2017.04.024
International audience; The Neuronal ceroid lipofuscinoses (NCLs) are a group of recessive disorders of childhood with overlapping symptoms including vision loss, ataxia, cognitive regression and premature death. 14 different genes have been linked t
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2025acac2c030e49186cb6128d9e9d7e
https://hal-riip.archives-ouvertes.fr/pasteur-01534650
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8
Intramembrane Proteolysis of GXGD-type Aspartyl Proteases Is Slowed by a Familial Alzheimer Disease-like Mutation
Autor: Harald Steiner, Elisabeth Kremmer, Regina Fluhrer, David B. Teplow, Edith Winkler, Gudula Grammer, Lucas Martin, Margaret M. Condron, Bärbel Klier, Christian Haass, Akio Fukumori, Martina Haug-Kröper
Publikováno v: J. Biol. Chem. 283, 30121-30128 (2008)
Fluhrer, R; Fukumori, A; Martin, L; Grammer, G; Haug-Kröper, M; Klier, B; et al.(2008). Intramembrane proteolysis of GXGD-type aspartyl proteases is slowed by a familial Alzheimer disease-like mutation. Journal of Biological Chemistry, 283(44), 30121-30128. doi: 10.1074/jbc.M806092200. UCLA: Retrieved from: http://www.escholarship.org/uc/item/2ht7q8wh
The Journal of biological chemistry, vol 283, iss 44
More than 150 familial Alzheimer disease (FAD)-associated missense mutations in presenilins (PS1 and PS2), the catalytic subunit of the γ-secretase complex, cause aberrant amyloid β-peptide (Aβ) production, by increasing the relative production of
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::713e4427d4b8e2e74165fb0c8d0fdec8
https://doi.org/10.1074/jbc.m806092200
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9
Shedding of glycan-modifying enzymes by signal peptide peptidase-like 3 (SPPL3) regulates cellular N-glycosylation
Autor: Stefan F. Lichtenthaler, Regina Fluhrer, Matthias Voss, Alessio Colombo, Martina Haug-Kröper, Harald Steiner, Gudula Grammer, Bärbel Klier, Fabian Higel, Christian Haass, Bernd Schröder, Andreas Seidl, Reinhard Obst, Peer-Hendrik Kuhn, Akio Fukumori, Ulrike Künzel
Publikováno v: The EMBO journal 33(24), 2890-2905 (2014). doi:10.15252/embj.201488375
Protein N-glycosylation is involved in a variety of physiological and pathophysiological processes such as autoimmunity, tumour progression and metastasis. Signal peptide peptidase-like 3 (SPPL3) is an intramembrane-cleaving aspartyl protease of the
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c191e80c15a9fb9a4d4d089c104136df
https://pubmed.ncbi.nlm.nih.gov/25414474
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10
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)
Autor: Gudula Grammer, Lucas Martin, Brigitte Nuscher, Regina Fluhrer, Bärbel Klier, Christian Haass, Martina Haug-Kröper
Publikováno v: The journal of biological chemistry 287(7), 5156-5163 (2011). doi:10.1074/jbc.M111.328104
Regulated intramembrane proteolysis is a widely accepted concept describing the processing of various transmembrane proteins via ectodomain shedding followed by an intramembrane cleavage. The resulting cleavage products can be involved in reverse sig
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cbdfbda0abaed1d5d10ecd472863c0f0
https://pubmed.ncbi.nlm.nih.gov/22194595
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