Cooperation of N- and C-terminal substrate transmembrane domain segments in intramembrane proteolysis by γ-secretase
暂无分享,去创建一个
D. Langosch | S. Lichtenthaler | Walter Stelzer | H. Steiner | M. Wozny | N. Werner | Gökhan Güner | Marlene Aßfalg | Philipp Högel
[1] T. Straub,et al. Helical stability of the GnTV transmembrane domain impacts on SPPL3 dependent cleavage , 2022, Scientific Reports.
[2] M. Zacharias,et al. Altered Hinge Conformations in APP Transmembrane Helix Mutants May Affect Enzyme-Substrate Interactions of γ-Secretase. , 2020, ACS chemical neuroscience.
[3] R. Fluhrer,et al. Non-canonical Shedding of TNFα by SPPL2a Is Determined by the Conformational Flexibility of Its Transmembrane Helix , 2020, iScience.
[4] C. Haass,et al. γ‐Secretase cleavage of the Alzheimer risk factor TREM2 is determined by its intrinsic structural dynamics , 2020, The EMBO journal.
[5] S. Lichtenthaler,et al. The substrate repertoire of γ-secretase/presenilin. , 2020, Seminars in cell & developmental biology.
[6] C. Mulle,et al. Seizure protein 6 controls glycosylation and trafficking of kainate receptor subunits GluK2 and GluK3 , 2020, The EMBO journal.
[7] M. Zacharias,et al. The dynamics of γ-secretase and its substrates. , 2020, Seminars in cell & developmental biology.
[8] M. Wolfe. Substrate recognition and processing by γ-secretase. , 2020, Biochimica et biophysica acta. Biomembranes.
[9] P. Griffin,et al. Protein dynamics and conformational changes explored by hydrogen/deuterium exchange mass spectrometry. , 2019, Current opinion in structural biology.
[10] D. Langosch,et al. Conformationally Flexible Sites within the Transmembrane Helices of Amyloid Precursor Protein and Notch1 Receptor. , 2019, Biochemistry.
[11] O. Bocharova,et al. Familial L723P mutation can shift the distribution between the alternative APP transmembrane domain cleavage cascades by local unfolding of the ε-cleavage site suggesting a straightforward mechanism of Alzheimer's disease pathogenesis. , 2019, ACS chemical biology.
[12] D. Huster,et al. Modulating Hinge Flexibility in the APP Transmembrane Domain Alters γ-Secretase Cleavage. , 2019, Biophysical journal.
[13] D. Langosch,et al. The Metastable XBP1u Transmembrane Domain Defines Determinants for Intramembrane Proteolysis by Signal Peptide Peptidase. , 2019, Cell reports.
[14] Yigong Shi,et al. Recognition of the Amyloid Precursor Protein by Human gamma-secretase , 2019 .
[15] Yigong Shi,et al. Recognition of the amyloid precursor protein by human γ-secretase , 2019, Science.
[16] M. Zacharias,et al. Structural Modeling of γ-Secretase Aβ n Complex Formation and Substrate Processing. , 2019, ACS chemical neuroscience.
[17] Yigong Shi,et al. Structural basis of Notch recognition by human γ-secretase , 2018, Nature.
[18] S. Tagami,et al. Making the final cut: pathogenic amyloid-β peptide generation by γ-secretase , 2018, Cell stress.
[19] Chunyu Wang,et al. Coupled Transmembrane Substrate Docking and Helical Unwinding in Intramembrane Proteolysis of Amyloid Precursor Protein , 2018, Scientific Reports.
[20] B. Luy,et al. Increased H-Bond Stability Relates to Altered ε-Cleavage Efficiency and Aβ Levels in the I45T Familial Alzheimer’s Disease Mutant of APP , 2018, bioRxiv.
[21] R. Osman,et al. Unwinding of the Substrate Transmembrane Helix in Intramembrane Proteolysis. , 2018, Biophysical journal.
[22] P. Cruz,et al. One Peptide Reveals the Two Faces of α-Helix Unfolding-Folding Dynamics. , 2018, The journal of physical chemistry. B.
[23] D. Langosch,et al. Glycine Perturbs Local and Global Conformational Flexibility of a Transmembrane Helix. , 2018, Biochemistry.
[24] D. Langosch,et al. Substrate processing in intramembrane proteolysis by γ-secretase – the role of protein dynamics , 2017, Biological chemistry.
[25] C. Sanders,et al. Structural and biochemical differences between the Notch and the amyloid precursor protein transmembrane domains , 2017, Science Advances.
[26] D. Seth,et al. Transmembrane Substrate Determinants for γ-Secretase Processing of APP CTFβ. , 2016, Biochemistry.
[27] D. Langosch,et al. The Impact of the ‘Austrian’ Mutation of the Amyloid Precursor Protein Transmembrane Helix is Communicated to the Hinge Region , 2016 .
[28] Yan Yan,et al. Alzheimer’s disease-associated mutations increase amyloid precursor protein resistance to γ-secretase cleavage and the Aβ42/Aβ40 ratio , 2016, Cell Discovery.
[29] D. Selkoe,et al. The amyloid-beta forming tripeptide cleavage mechanism of γ-secretase , 2016, eLife.
[30] E. Kremmer,et al. Generation and deposition of Aβ43 by the virtually inactive presenilin‐1 L435F mutant contradicts the presenilin loss‐of‐function hypothesis of Alzheimer's disease , 2016, EMBO molecular medicine.
[31] D. Selkoe,et al. Nicastrin functions to sterically hinder γ-secretase–substrate interactions driven by substrate transmembrane domain , 2015, Proceedings of the National Academy of Sciences.
[32] D. Langosch,et al. Understanding intramembrane proteolysis: from protein dynamics to reaction kinetics. , 2015, Trends in biochemical sciences.
[33] R. Fluhrer,et al. Intramembrane proteolysis of β-amyloid precursor protein by γ-secretase is an unusually slow process. , 2015, Biophysical journal.
[34] Daniel Hornburg,et al. Side-chain to main-chain hydrogen bonding controls the intrinsic backbone dynamics of the amyloid precursor protein transmembrane helix. , 2014, Biophysical journal.
[35] Piotr Cieplak,et al. Sequence‐derived structural features driving proteolytic processing , 2014, Proteomics.
[36] S. Urban,et al. Proteolysis inside the Membrane Is a Rate-Governed Reaction Not Driven by Substrate Affinity , 2013, Cell.
[37] Dieter Langosch,et al. The backbone dynamics of the amyloid precursor protein transmembrane helix provides a rationale for the sequential cleavage mechanism of γ-secretase. , 2013, Journal of the American Chemical Society.
[38] M. Wolfe. Processive proteolysis by γ-secretase and the mechanism of Alzheimer’s disease , 2012, Biological chemistry.
[39] Charles R. Sanders,et al. The Amyloid Precursor Protein Has a Flexible Transmembrane Domain and Binds Cholesterol , 2012, Science.
[40] B. de Strooper,et al. The mechanism of γ-Secretase dysfunction in familial Alzheimer disease , 2012, The EMBO journal.
[41] Daniel Hornburg,et al. Residue-specific side-chain packing determines the backbone dynamics of transmembrane model helices. , 2010, Biophysical journal.
[42] D. Fairlie,et al. Update 1 of: Proteases universally recognize beta strands in their active sites. , 2010, Chemical reviews.
[43] A. Heck,et al. Sequence-specific conformational flexibility of SNARE transmembrane helices probed by hydrogen/deuterium exchange. , 2008, Biophysical journal.
[44] M. Sudol. The WW Domain , 2008 .
[45] C. Sanders,et al. Substrate specificity of γ-secretase and other intramembrane proteases , 2008, Cellular and Molecular Life Sciences.
[46] K. Teilum,et al. Application of Hydrogen Exchange Kinetics to Studies of Protein Folding , 2008 .
[47] Richard M. Page,et al. Generation of Aβ38 and Aβ42 Is Independently and Differentially Affected by Familial Alzheimer Disease-associated Presenilin Mutations and γ-Secretase Modulation* , 2008, Journal of Biological Chemistry.
[48] Chunyu Wang,et al. {gamma}-Secretase Substrate Concentration Modulates the Abeta42/Abeta40 Ratio: IMPLICATIONS FOR ALZHEIMER DISEASE. , 2007, The Journal of biological chemistry.
[49] S. Englander. Hydrogen exchange and mass spectrometry: A historical perspective , 2006, Journal of the American Society for Mass Spectrometry.
[50] B. de Strooper,et al. Contribution of Presenilin Transmembrane Domains 6 and 7 to a Water-containing Cavity in the γ-Secretase Complex* , 2006, Journal of Biological Chemistry.
[51] D. Fairlie,et al. Proteases universally recognize beta strands in their active sites. , 2005, Chemical reviews.
[52] Hui Xiao,et al. Mapping protein energy landscapes with amide hydrogen exchange and mass spectrometry: I. A generalized model for a two‐state protein and comparison with experiment , 2005, Protein science : a publication of the Protein Society.
[53] M. Vooijs,et al. Ectodomain Shedding and Intramembrane Cleavage of Mammalian Notch Proteins Are Not Regulated through Oligomerization* , 2004, Journal of Biological Chemistry.
[54] G. Belfort,et al. Protein unfolding at interfaces: Slow dynamics of α‐helix to β‐sheet transition , 2004 .
[55] G. Belfort,et al. Protein unfolding at interfaces: slow dynamics of alpha-helix to beta-sheet transition. , 2004, Proteins.
[56] J. Regula,et al. Reconstitution of γ-secretase activity , 2003, Nature Cell Biology.
[57] J. Hardy,et al. The Amyloid Hypothesis of Alzheimer ’ s Disease : Progress and Problems on the Road to Therapeutics , 2009 .
[58] A. Warshel,et al. What are the dielectric “constants” of proteins and how to validate electrostatic models? , 2001, Proteins.
[59] Jason C. Crane,et al. The folding mechanism of a -sheet: the WW domain1 , 2001 .
[60] M. Gruebele,et al. The folding mechanism of a beta-sheet: the WW domain. , 2001, Journal of molecular biology.
[61] Graeme Irvine Stevenson,et al. L-685,458, an Aspartyl Protease Transition State Mimic, Is a Potent Inhibitor of Amyloid β-Protein Precursor γ-Secretase Activity , 2000 .
[62] C. Masters,et al. Novel Leu723Pro amyloid precursor protein mutation increases amyloid β42(43) peptide levels and induces apoptosis , 2000, Annals of neurology.
[63] A. Nadin,et al. L-685,458, an aspartyl protease transition state mimic, is a potent inhibitor of amyloid beta-protein precursor gamma-secretase activity. , 2000, Biochemistry.
[64] H. Qian,et al. Hydrogen exchange kinetics of proteins in denaturants: a generalized two-process model. , 1999, Journal of molecular biology.
[65] A. Fersht. Structure and mechanism in protein science , 1998 .
[66] K Schulten,et al. VMD: visual molecular dynamics. , 1996, Journal of molecular graphics.