Intestinal mucin is a chaperone of multivalent copper
暂无分享,去创建一个
D. Fass | Y. Fridmann-Sirkis | K. Franz | T. Ilani | G. Javitt | K. Chacón | Nava Reznik | Annastassia D. Gallo | Katherine W. Rush | Noa A. Nairner | Y. Fridmann‐Sirkis
[1] D. Fass,et al. Helical self-assembly of a mucin segment suggests an evolutionary origin for von Willebrand factor tubules , 2022, Proceedings of the National Academy of Sciences of the United States of America.
[2] M. Curtis,et al. The Relationship between Mucins and Ulcerative Colitis: A Systematic Review , 2021, Journal of clinical medicine.
[3] Tessa R. Young,et al. Principles and practice of determining metal–protein affinities , 2021, The Biochemical journal.
[4] W. Hoffmann. Trefoil Factor Family (TFF) Peptides and their Different Roles in the Mucosal Innate Immune Defense and More: An Update. , 2021, Current medicinal chemistry.
[5] M. Petris,et al. Copper metabolism as a unique vulnerability in cancer. , 2020, Biochimica et biophysica acta. Molecular cell research.
[6] Patrice D Cani,et al. Mucus barrier, mucins and gut microbiota: the expected slimy partners? , 2020, Gut.
[7] M. Linder. Copper Homeostasis in Mammals, with Emphasis on Secretion and Excretion. A Review , 2020, International journal of molecular sciences.
[8] N. Elad,et al. Assembly Mechanism of Mucin and von Willebrand Factor Polymers , 2020, Cell.
[9] A. Bush,et al. Redox active metals in neurodegenerative diseases , 2019, JBIC Journal of Biological Inorganic Chemistry.
[10] A. Magistrato,et al. Copper trafficking in eukaryotic systems: current knowledge from experimental and computational efforts , 2019, Current opinion in structural biology.
[11] D. Fass,et al. Intestinal Gel-Forming Mucins Polymerize by Disulfide-Mediated Dimerization of D3 Domains , 2019, Journal of molecular biology.
[12] S. Lutsenko,et al. Copper Transport and Disease: What Can We Learn from Organoids? , 2019, Annual review of nutrition.
[13] T. Springer,et al. The von Willebrand factor D'D3 assembly and structural principles for factor VIII binding and concatemer biogenesis. , 2019, Blood.
[14] D. Thiele,et al. X-ray structures of the high-affinity copper transporter Ctr1 , 2019, Nature Communications.
[15] Ryan L. Collins,et al. The mutational constraint spectrum quantified from variation in 141,456 humans , 2020, Nature.
[16] Andrew C. R. Martin,et al. ZincBind—the database of zinc binding sites , 2019, Database J. Biol. Databases Curation.
[17] W. Janssen,et al. Mucociliary Defense: Emerging Cellular, Molecular, and Animal Models , 2018, Annals of the American Thoracic Society.
[18] J. DiNicolantonio,et al. Copper deficiency may be a leading cause of ischaemic heart disease , 2018, Open Heart.
[19] Eric P. Skaar,et al. The Impact of Dietary Transition Metals on Host-Bacterial Interactions. , 2018, Cell host & microbe.
[20] Elizabeth M. Nolan,et al. Defensins, lectins, mucins, and secretory immunoglobulin A: microbe-binding biomolecules that contribute to mucosal immunity in the human gut , 2016, Critical reviews in biochemistry and molecular biology.
[21] M. Linder,et al. Ceruloplasmin and other copper binding components of blood plasma and their functions: an update. , 2016, Metallomics : integrated biometal science.
[22] Gunnar C. Hansson,et al. Immunological aspects of intestinal mucus and mucins , 2016, Nature Reviews Immunology.
[23] D. Sokaras,et al. Kβ Valence to Core X-ray Emission Studies of Cu(I) Binding Proteins with Mixed Methionine - Histidine Coordination. Relevance to the Reactivity of the M- and H-sites of Peptidylglycine Monooxygenase. , 2016, Inorganic chemistry.
[24] M. McEvoy,et al. Tracking metal ions through a Cu/Ag efflux pump assigns the functional roles of the periplasmic proteins , 2014, Proceedings of the National Academy of Sciences.
[25] F. Bäckhed,et al. Microbial-induced meprin β cleavage in MUC2 mucin and a functional CFTR channel are required to release anchored small intestinal mucus , 2014, Proceedings of the National Academy of Sciences.
[26] M. Bäckström,et al. Intestinal MUC2 mucin supramolecular topology by packing and release resting on D3 domain assembly. , 2014, Journal of Molecular Biology.
[27] Lisa Gottschlich,et al. Evaluation of quantitative probes for weaker Cu(i) binding sites completes a set of four capable of detecting Cu(i) affinities from nanomolar to attomolar. , 2013, Metallomics : integrated biometal science.
[28] D. Thiele,et al. Charting the travels of copper in eukaryotes from yeast to mammals. , 2012, Biochimica et biophysica acta.
[29] Jeffrey T. Rubino,et al. Coordination chemistry of copper proteins: how nature handles a toxic cargo for essential function. , 2012, Journal of inorganic biochemistry.
[30] D. Medeiros,et al. The Cardiac Copper Chaperone Proteins Sco1 and CCS are Up-Regulated, but Cox 1 and Cox4 are Down-Regulated, by Copper Deficiency , 2011, Biological Trace Element Research.
[31] Philip Sutton,et al. Mucin dynamics and enteric pathogens , 2011, Nature Reviews Microbiology.
[32] D. Thiele,et al. Ctr1 Is an Apical Copper Transporter in Mammalian Intestinal Epithelial Cells in Vivo That Is Controlled at the Level of Protein Stability* , 2010, The Journal of Biological Chemistry.
[33] P. Emsley,et al. Features and development of Coot , 2010, Acta crystallographica. Section D, Biological crystallography.
[34] D. Baldantoni,et al. Copper binds the carboxy-terminus of trefoil protein 1 (TFF1), favoring its homodimerization and motogenic activity , 2010, Cellular and Molecular Life Sciences.
[35] Randy J. Read,et al. Acta Crystallographica Section D Biological , 2003 .
[36] Conrad Bessant,et al. Protein-folding location can regulate manganese-binding versus copper- or zinc-binding , 2008, Nature.
[37] J. Kaplan,et al. Human Copper Transporter hCTR1 Mediates Basolateral Uptake of Copper into Enterocytes , 2007, Journal of Biological Chemistry.
[38] D. Thiele,et al. Ctr1 drives intestinal copper absorption and is essential for growth, iron metabolism, and neonatal cardiac function. , 2006, Cell metabolism.
[39] R. Wapnir. Copper absorption and bioavailability. , 1998, The American journal of clinical nutrition.
[40] J. Dekker,et al. The human intestinal cell lines Caco-2 and LS174T as models to study cell-type specific mucin expression , 1996, Glycoconjugate Journal.
[41] G. Buettner,et al. Catalytic metals, ascorbate and free radicals: combinations to avoid. , 1996, Radiation research.
[42] M. Copin,et al. Expression of human mucin genes in respiratory, digestive, and reproductive tracts ascertained by in situ hybridization. , 1993, The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society.
[43] K. Robinson,et al. Carbohydrate-Dependent and Antimicrobial Peptide Defence Mechanisms Against Helicobacter pylori Infections. , 2019, Current topics in microbiology and immunology.
[44] Mathias Winterhalter,et al. Thermodynamic study of Cu2+ binding to the DAHK and GHK peptides by isothermal titration calorimetry (ITC) with the weaker competitor glycine , 2011, JBIC Journal of Biological Inorganic Chemistry.
[45] D. Winge,et al. Copper metallochaperones. , 2010, Annual review of biochemistry.
[46] G J Strous,et al. Mucin-type glycoproteins. , 1992, Critical reviews in biochemistry and molecular biology.