Protein nanostructures in food – Should we be worried?
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J. Carver | J. Gerrard | S. Gras | J. Raynes
[1] R. Beever,et al. Function of rodlets on the surface of fungal spores , 1978, Nature.
[2] A. Hofman,et al. A new variant of Creutzfeldt-Jakob disease in the UK , 1996, The Lancet.
[3] S. Cousens,et al. Transmissions to mice indicate that ‘new variant’ CJD is caused by the BSE agent , 1997, Nature.
[4] C. Kruif. Supra-aggregates of Casein Micelles as a Prelude to Coagulation , 1998 .
[5] C. Dobson. Protein misfolding, evolution and disease. , 1999, Trends in biochemical sciences.
[6] H. Busscher,et al. How a fungus escapes the water to grow into the air , 1999, Current Biology.
[7] K. Namba,et al. Amyloid protofilament formation of hen egg lysozyme in highly concentrated ethanol solution , 2008, Protein science : a publication of the Protein Society.
[8] D. Selkoe,et al. A de novo designed helix-turn-helix peptide forms nontoxic amyloid fibrils , 2000, Nature Structural Biology.
[9] J. Mackay,et al. The hydrophobin EAS is largely unstructured in solution and functions by forming amyloid-like structures. , 2001, Structure.
[10] P. Pudney,et al. Novel Amyloid Fibrillar Networks Derived from a Globular Protein: β-Lactoglobulin† , 2002 .
[11] D. Horne. Casein structure, self-assembly and gelation , 2002 .
[12] C. Dobson,et al. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases , 2002, Nature.
[13] R. de Vries,et al. Multiple steps during the formation of beta-lactoglobulin fibrils. , 2003, Biomacromolecules.
[14] P. Cooke,et al. Environmental Influences on Bovine κ-Casein: Reduction and Conversion to Fibrillar (Amyloid) Structures , 2003, Journal of protein chemistry.
[15] J. Rumfeldt,et al. Sonication of proteins causes formation of aggregates that resemble amyloid , 2004, Protein science : a publication of the Protein Society.
[16] L. Sagis,et al. Mesoscopic properties of semiflexible amyloid fibrils. , 2004, Langmuir : the ACS journal of surfaces and colloids.
[17] K. S. Kwak,et al. Processing optimization and functional properties of gelatin from shark (Isurus oxyrinchus) cartilage , 2004 .
[18] C. Dobson,et al. Observation of sequence specificity in the seeding of protein amyloid fibrils , 2004, Protein science : a publication of the Protein Society.
[19] F. Heitz,et al. High pressure induces scrapie-like prion protein misfolding and amyloid fibril formation. , 2004, Biochemistry.
[20] T. Tokuda,et al. Unexpectedly high incidence of visceral AA-amyloidosis in slaughtered cattle in Japan , 2005, Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis.
[21] J. Carver,et al. Casein proteins as molecular chaperones. , 2005, Journal of agricultural and food chemistry.
[22] P. Westermark,et al. Protein fibrils in nature can enhance amyloid protein A amyloidosis in mice: Cross-seeding as a disease mechanism , 2005, Proceedings of the National Academy of Sciences of the United States of America.
[23] C. Dobson,et al. Amyloid fibril formation by bovine milk kappa-casein and its inhibition by the molecular chaperones alphaS- and beta-casein. , 2005, Biochemistry.
[24] S. Teichmann,et al. The importance of sequence diversity in the aggregation and evolution of proteins , 2005, Nature.
[25] José Miguel Aguilera,et al. Why food microstructure , 2005 .
[26] C. Dobson,et al. Protein unfolding, amyloid fibril formation and configurational energy landscapes under high pressure conditions. , 2006, Chemical Society reviews.
[27] M. Subirade,et al. Food protein-based materials as nutraceutical delivery systems , 2006 .
[28] C. Dobson,et al. Protein misfolding, functional amyloid, and human disease. , 2006, Annual review of biochemistry.
[29] R. Boom,et al. Shear Pulses Nucleate Fibril Aggregation , 2006 .
[30] G. Howlett,et al. Shear flow induces amyloid fibril formation. , 2006, Biomacromolecules.
[31] E. Foegeding. Food Biophysics of Protein Gels: A Challenge of Nano and Macroscopic Proportions , 2006 .
[32] E. Linden,et al. Self-assembly and aggregation of proteins , 2007 .
[33] Yogendra Pratap Singh,et al. Amyloid peptides and proteins in review. , 2007, Reviews of physiology, biochemistry and pharmacology.
[34] D. Otzen,et al. Aggregation and fibrillation of bovine serum albumin. , 2007, Biochimica et biophysica acta.
[35] J. Gerrard,et al. Formation of amyloid-like fibrils by ovalbumin and related proteins under conditions relevant to food processing. , 2007, Journal of agricultural and food chemistry.
[36] L. B. Larsen,et al. Proteolysis of milk proteins lactosylated in model systems. , 2007, Molecular nutrition & food research.
[37] P. Westermark,et al. Amyloidogenic potential of foie gras , 2007, Proceedings of the National Academy of Sciences.
[38] D. Otzen,et al. Amyloid—a state in many guises: Survival of the fittest fibril fold , 2007, Protein science : a publication of the Protein Society.
[39] R. Boom,et al. Enzyme-Induced Formation of β-Lactoglobulin Fibrils by AspN Endoproteinase , 2008 .
[40] D. Cui,et al. Acceleration of murine AA amyloid deposition by bovine amyloid fibrils and tissue homogenates , 2008, Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis.
[41] Fred Jacobson,et al. Protein aggregation and bioprocessing , 2006, The AAPS Journal.
[42] M. Greger. Amyloid fibrils: potential food safety implications , 2008 .
[43] R. Boom,et al. Formation of fibrillar whey protein aggregates : Influence of heat and shear treatment, and resulting rheology , 2008 .
[44] Jamie R Lead,et al. Nanomaterials in the environment: Behavior, fate, bioavailability, and effects , 2008, Environmental toxicology and chemistry.
[45] J. Carver,et al. Unraveling the mysteries of protein folding and misfolding , 2008, IUBMB life.
[46] R. Boom,et al. Peptides are building blocks of heat-induced fibrillar protein aggregates of beta-lactoglobulin formed at pH 2. , 2008, Biomacromolecules.
[47] L. Sagis,et al. Effects of flow on hen egg white lysozyme (HEWL) fibril formation: length distribution, flexibility, and kinetics. , 2008, Journal of agricultural and food chemistry.
[48] M. A. Rao. The nanoscale food science, engineering, and technology section. , 2008, Journal of food science.
[49] J. Carver,et al. Amyloid fibril formation by bovine milk alpha s2-casein occurs under physiological conditions yet is prevented by its natural counterpart, alpha s1-casein. , 2008, Biochemistry.
[50] Jason T Giurleo,et al. Beta-lactoglobulin assembles into amyloid through sequential aggregated intermediates. , 2008, Journal of molecular biology.
[51] S. Radford,et al. Fibril Fragmentation Enhances Amyloid Cytotoxicity*♦ , 2009, The Journal of Biological Chemistry.
[52] J. Carver,et al. The two-faced nature of milk casein proteins: amyloid fibril formation and chaperone-like activity , 2009 .
[53] P. Westermark,et al. Serum amyloid A and protein AA: Molecular mechanisms of a transmissible amyloidosis , 2009, FEBS letters.
[54] M. A. Rao,et al. Factors affecting rheological characteristics of fibril gels: the case of beta-lactoglobulin and alpha-lactalbumin. , 2009, Journal of food science.
[55] D. Dunstan,et al. Shear-induced structure and mechanics of β-lactoglobulin amyloid fibrils , 2009 .
[56] S. Ikeda,et al. Slaughtered aged cattle might be one dietary source exhibiting amyloid enhancing factor activity , 2009, Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis.
[57] S. Gras. Surface- and Solution-Based Assembly of Amyloid Fibrils for Biomedical and Nanotechnology Applications , 2009 .
[58] A. Congiu Castellano,et al. Structural changes induced in proteins by therapeutic ultrasounds. , 2009, Ultrasonics.
[59] P. Cox,et al. Hydrophobins stabilised air-filled emulsions for the food industry , 2009 .
[60] Chuan-he Tang,et al. Formation and characterization of amyloid-like fibrils from soy β-conglycinin and glycinin. , 2010, Journal of agricultural and food chemistry.
[61] K. Sharrock,et al. Ethylene Ripening of Pears by Unconventional Means: Use of Experimental Thimble-Sized Ethylene Capsules inside Cartons and Clamshells , 2010 .
[62] Harjinder Singh,et al. In vitro digestion of beta-lactoglobulin fibrils formed by heat treatment at low pH. , 2010, Journal of agricultural and food chemistry.
[63] J. Gerrard,et al. Amyloid fibrils as a nanoscaffold for enzyme immobilization , 2009, Biotechnology progress.
[64] Yehui Zhang,et al. Formation of amyloid fibrils from kidney bean 7S globulin (Phaseolin) at pH 2.0. , 2010, Journal of agricultural and food chemistry.
[65] J. Carver,et al. αB-Crystallin inhibits the cell toxicity associated with amyloid fibril formation by κ-casein and the amyloid-β peptide , 2010, Cell Stress and Chaperones.
[66] Alexander K. Buell,et al. Nanostructured films from hierarchical self-assembly of amyloidogenic proteins. , 2010, Nature nanotechnology.
[67] N. Kosaka,et al. microRNA as a new immune-regulatory agent in breast milk , 2010, Silence.
[68] Qasim Chaudhry,et al. Chapter 1:Nanotechnologies in the Food Arena: New Opportunities, New Questions, New Concerns , 2010 .
[69] J. Carver,et al. The chaperone action of bovine milk αS1- and αS2-caseins and their associated form αS-casein. , 2011, Archives of biochemistry and biophysics.
[70] Yi Cao,et al. Photo-Induced Fibrillar Formation of Chicken Egg White Lysozyme Under Native Conditions , 2011 .
[71] D. Dunstan,et al. The effects of shear flow on protein structure and function , 2011, Biopolymers.
[72] Hélder D. Silva,et al. Nanoemulsions for Food Applications: Development and Characterization , 2012, Food and Bioprocess Technology.
[73] Qasim Chaudhry,et al. Applications of nanomaterials in food packaging with a consideration of opportunities for developing countries , 2011 .
[74] Rickey Y. Yada,et al. Nanotechnologies in agriculture: New tools for sustainable development , 2011 .
[75] A. Moosavi-Movahedi,et al. Beta casein-micelle as a nano vehicle for solubility enhancement of curcumin; food industry application , 2011 .
[76] Qasim Chaudhry,et al. Food applications of nanotechnologies: An overview of opportunities and challenges for developing countries , 2011 .
[77] Bernadene A Magnuson,et al. A brief review of the occurrence, use, and safety of food-related nanomaterials. , 2011, Journal of food science.
[78] J. Carver,et al. Darwinian transformation of a ‘scarcely nutritious fluid’ into milk , 2012, Journal of evolutionary biology.
[79] Nanotechnology and its impact on food and nutrition: a review. , 2012 .
[80] Isha Rastogi. Nanotechnology: Safety paradigms , 2012 .
[81] P. Venema,et al. Fibrillar structures in food. , 2012, Food & function.
[82] R. Setterquist,et al. Exosomes: current knowledge of their composition, biological functions, and diagnostic and therapeutic potentials. , 2012, Biochimica et biophysica acta.
[83] Joseph P. Kerry,et al. Nanotechnologies in the food industry – Recent developments, risks and regulation , 2012 .
[84] Hai Pan,et al. Photoinduced fibrils formation of chicken egg white lysozyme under native conditions , 2012, Proteins.
[85] J. Stenvang,et al. Inhibition of microRNA function by antimiR oligonucleotides , 2012, Silence.
[86] M. A. Rao,et al. Whey protein nanofibrils: the environment-morphology-functionality relationship in lyophilization, rehydration, and seeding. , 2012, Journal of agricultural and food chemistry.
[87] P. Dore,et al. Raman analysis of insulin denaturation induced by high‐pressure and thermal treatments , 2012 .
[88] Ruplal Choudhary,et al. Ultraviolet Pasteurization for Food Industry , 2012 .
[89] M. A. Rao,et al. β-Lactoglobulin nanofibrils: Effect of temperature on fibril formation kinetics, fibril morphology and the rheological properties of fibril dispersions , 2012 .
[90] J. Gerrard,et al. Amyloid fibrils as functionalizable components of nanocomposite materials , 2012, Biotechnology progress.
[91] David Posada,et al. Removal versus fragmentation of amyloid-forming precursors via membrane filtration. , 2012, Biotechnology and bioengineering.