The Experts below are selected from a list of 247629 Experts worldwide ranked by ideXlab platform
James D House - One of the best experts on this subject based on the ideXlab platform.
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effect of barrel temperature and feed moisture on Protein Quality in pre cooked kabuli chickpea sorghum and maize flours
Food Science and Technology International, 2020Co-Authors: S Wang, Matthew G Nosworthy, James D House, Shannonhood Niefer, Michael T NickersonAbstract:The effect of barrel temperature (120 and 150 ℃, held constant in zones 4–6) and feed moisture (20 and 24%) on the Protein Quality of Kabuli chickpea, sorghum, and maize flours were examined, which...
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effect of processing on the in vitro and in vivo Protein Quality of beans phaseolus vulgaris and vicia faba
Nutrients, 2018Co-Authors: Matthew G Nosworthy, Gerardo Medina, Adam J Franczyk, Jason Neufeld, Paulyn Appah, Alphonsus Utioh, Peter Frohlich, James D HouseAbstract:In this work, the Protein Quality of different bean types after undergoing the preparatory methods of baking, cooking and extrusion was assayed. Protein Quality was assessed using a rodent bioassay to evaluate growth and Protein digestibility while amino acid composition was determined via HPLC. In vivo Protein digestibility was compared to an in vitro assessment method. The average Protein digestibility corrected amino acid score (PDCAAS) for processed beans was higher than the digestible indispensable amino acid score (DIAAS) (61% vs. 45%). Extrusion/cooking of Phaseolus varieties resulted in higher PDCAAS (66% on average) and DIAAS values (61% on average) than baked (52% and 48%) while baked faba beans had higher PDCAAS (66%) and DIAAS (61%) values. A significant correlation was found between PDCAAS and in vitro PDCAAS (R2 = 0.7497). This demonstrates which bean processing method will generate the optimal Protein Quality, which has benefits for both industrial production and individual domestic preparation.
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effect of processing on the in vitro and in vivo Protein Quality of red and green lentils lens culinaris
Food Chemistry, 2018Co-Authors: Matthew G Nosworthy, Gerardo Medina, Adam J Franczyk, Jason Neufeld, Paulyn Appah, Alphonsus Utioh, Peter Frohlich, James D HouseAbstract:In order to determine the effect of extrusion, baking and cooking on the Protein Quality of red and green lentils, a rodent bioassay was conducted and compared to an in vitro method of Protein Quality determination. On average, the Protein Digestibility-Corrected Amino Acid Score of red lentils (55.0) was higher than that of green lentils (50.8). Extruded lentil flour had higher scores (63.01 red, 57.09 green) than either cooked (57.40 red, 52.92 green) or baked (53.84 red, 47.14 green) flours. The average Digestible Indispensable Amino Acid Score of red lentils (0.54) was higher than green lentils (0.49). The Protein Efficiency Ratio of the extruded lentil flours (1.30 red, 1.34 green) was higher than that of the baked flour (0.98 red, 1.09 green). A correlation was found between in vivo and in vitro methods of determining Protein digestibility (R2=0.8934). This work could influence selection of processing method during product development.
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potential impact of the digestible indispensable amino acid score as a measure of Protein Quality on dietary regulations and health
Nutrition Reviews, 2017Co-Authors: Christopher P F Marinangeli, James D HouseAbstract:Regulatory frameworks for Protein content claims in Canada and the United States are underpinned by the Protein efficiency ratio and Protein digestibility-corrected amino acid score (PDCAAS), respectively, which are used to assess the Protein Quality of a given food. The digestible indispensable amino acid score (DIAAS) is a novel approach to measuring the Protein Quality of foods and is supported by the Food and Agriculture Organization of the United Nations. Methodological concerns about the PDCAAS are addressed by the DIAAS through introduction of the use of ileal amino acid digestibility coefficients and untruncated Protein scores. However, before the DIAAS is widely adopted within regulatory frameworks, a comprehensive assessment is required. Accordingly, this review addresses the potential impact of the DIAAS on regulation, communication, and public health, as well as knowledge gaps, analytical challenges, and cost of implementation. A pragmatic approach to addressing Protein Quality is advocated by suggesting the use of conservative coefficients of digestibility that are derived from in vitro methods. Before adopting the DIAAS as a framework for supporting Protein content claims, updated food-related regulations and policies should also be evaluated through a lens that anticipates the impact on consumer-facing nutrition communication, the adoption of dietary patterns that are nutritionally adequate, and a food value chain that fosters a spirit of food and nutritional innovation.
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impact of processing on the Protein Quality of pinto bean phaseolus vulgaris and buckwheat fagopyrum esculentum moench flours and blends as determined by in vitro and in vivo methodologies
Journal of Agricultural and Food Chemistry, 2017Co-Authors: Matthew G Nosworthy, Adam J Franczyk, Jason Neufeld, Paulyn Appah, Alphonsus Utioh, Anna Zimochkorzycka, James D HouseAbstract:Blending of Protein sources can increase Protein Quality by compensating for limiting amino acids present in individual sources, whereas processing grain flours by extrusion or baking can also alter Protein Quality. To determine the effect of baking and extrusion on the Protein Quality of blended flours from buckwheat and pinto beans, a rodent bioassay was performed and compared to an in vitro method of Protein Quality determination. Overall, extruded products had higher Protein efficiency ratio values, increased digestibility, and greater Protein digestibility corrected amino acid score (PDCAAS) values than baked products, with the extruded buckwheat/pinto blend having the greatest PDCAAS value of the experimental diets investigated. A correlation was found between both digestibility and PDCAAS values generated from in vitro and in vivo methods. The use of in vitro digestibility analysis should be investigated as a potential replacement for the current rodent assay for nutrient content claim purposes.
Michael Ehrmann - One of the best experts on this subject based on the ideXlab platform.
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htra proteases regulated proteolysis in Protein Quality control
Nature Reviews Molecular Cell Biology, 2011Co-Authors: Tim Clausen, Markus Kaiser, Robert Huber, Michael EhrmannAbstract:HTRA proteases perform a variety of Protein Quality control functions that are of key importance to cell fate. This Review discusses the emerging physiological implications and unique architectural and mechanistic features of bacterial, plant and mammalian HTRAs.
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htra proteases regulated proteolysis in Protein Quality control
Nature Reviews Molecular Cell Biology, 2011Co-Authors: Tim Clausen, Markus Kaiser, Robert Huber, Michael EhrmannAbstract:Controlled proteolysis underlies a vast diversity of protective and regulatory processes that are of key importance to cell fate. The unique molecular architecture of the widely conserved high temperature requirement A (HTRA) proteases has evolved to mediate critical aspects of ATP-independent Protein Quality control. The simple combination of a classic Ser protease domain and a carboxy-terminal peptide-binding domain produces cellular factors of remarkable structural and functional plasticity that allow cells to rapidly respond to the presence of misfolded or mislocalized polypeptides.
Matthew G Nosworthy - One of the best experts on this subject based on the ideXlab platform.
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effect of barrel temperature and feed moisture on Protein Quality in pre cooked kabuli chickpea sorghum and maize flours
Food Science and Technology International, 2020Co-Authors: S Wang, Matthew G Nosworthy, James D House, Shannonhood Niefer, Michael T NickersonAbstract:The effect of barrel temperature (120 and 150 ℃, held constant in zones 4–6) and feed moisture (20 and 24%) on the Protein Quality of Kabuli chickpea, sorghum, and maize flours were examined, which...
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effect of processing on the in vitro and in vivo Protein Quality of beans phaseolus vulgaris and vicia faba
Nutrients, 2018Co-Authors: Matthew G Nosworthy, Gerardo Medina, Adam J Franczyk, Jason Neufeld, Paulyn Appah, Alphonsus Utioh, Peter Frohlich, James D HouseAbstract:In this work, the Protein Quality of different bean types after undergoing the preparatory methods of baking, cooking and extrusion was assayed. Protein Quality was assessed using a rodent bioassay to evaluate growth and Protein digestibility while amino acid composition was determined via HPLC. In vivo Protein digestibility was compared to an in vitro assessment method. The average Protein digestibility corrected amino acid score (PDCAAS) for processed beans was higher than the digestible indispensable amino acid score (DIAAS) (61% vs. 45%). Extrusion/cooking of Phaseolus varieties resulted in higher PDCAAS (66% on average) and DIAAS values (61% on average) than baked (52% and 48%) while baked faba beans had higher PDCAAS (66%) and DIAAS (61%) values. A significant correlation was found between PDCAAS and in vitro PDCAAS (R2 = 0.7497). This demonstrates which bean processing method will generate the optimal Protein Quality, which has benefits for both industrial production and individual domestic preparation.
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effect of processing on the in vitro and in vivo Protein Quality of red and green lentils lens culinaris
Food Chemistry, 2018Co-Authors: Matthew G Nosworthy, Gerardo Medina, Adam J Franczyk, Jason Neufeld, Paulyn Appah, Alphonsus Utioh, Peter Frohlich, James D HouseAbstract:In order to determine the effect of extrusion, baking and cooking on the Protein Quality of red and green lentils, a rodent bioassay was conducted and compared to an in vitro method of Protein Quality determination. On average, the Protein Digestibility-Corrected Amino Acid Score of red lentils (55.0) was higher than that of green lentils (50.8). Extruded lentil flour had higher scores (63.01 red, 57.09 green) than either cooked (57.40 red, 52.92 green) or baked (53.84 red, 47.14 green) flours. The average Digestible Indispensable Amino Acid Score of red lentils (0.54) was higher than green lentils (0.49). The Protein Efficiency Ratio of the extruded lentil flours (1.30 red, 1.34 green) was higher than that of the baked flour (0.98 red, 1.09 green). A correlation was found between in vivo and in vitro methods of determining Protein digestibility (R2=0.8934). This work could influence selection of processing method during product development.
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impact of processing on the Protein Quality of pinto bean phaseolus vulgaris and buckwheat fagopyrum esculentum moench flours and blends as determined by in vitro and in vivo methodologies
Journal of Agricultural and Food Chemistry, 2017Co-Authors: Matthew G Nosworthy, Adam J Franczyk, Jason Neufeld, Paulyn Appah, Alphonsus Utioh, Anna Zimochkorzycka, James D HouseAbstract:Blending of Protein sources can increase Protein Quality by compensating for limiting amino acids present in individual sources, whereas processing grain flours by extrusion or baking can also alter Protein Quality. To determine the effect of baking and extrusion on the Protein Quality of blended flours from buckwheat and pinto beans, a rodent bioassay was performed and compared to an in vitro method of Protein Quality determination. Overall, extruded products had higher Protein efficiency ratio values, increased digestibility, and greater Protein digestibility corrected amino acid score (PDCAAS) values than baked products, with the extruded buckwheat/pinto blend having the greatest PDCAAS value of the experimental diets investigated. A correlation was found between both digestibility and PDCAAS values generated from in vitro and in vivo methods. The use of in vitro digestibility analysis should be investigated as a potential replacement for the current rodent assay for nutrient content claim purposes.
Judith Frydman - One of the best experts on this subject based on the ideXlab platform.
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mechanisms and functions of spatial Protein Quality control
Annual Review of Biochemistry, 2017Co-Authors: Emily M Sontag, Rahul S Samant, Judith FrydmanAbstract:A healthy proteome is essential for cell survival. Protein misfolding is linked to a rapidly expanding list of human diseases, ranging from neurodegenerative diseases to aging and cancer. Many of these diseases are characterized by the accumulation of misfolded Proteins in intra- and extracellular inclusions, such as amyloid plaques. The clear link between Protein misfolding and disease highlights the need to better understand the elaborate machinery that manages proteome homeostasis, or proteostasis, in the cell. Proteostasis depends on a network of molecular chaperones and clearance pathways involved in the recognition, refolding, and/or clearance of aberrant Proteins. Recent studies reveal that an integral part of the cellular management of misfolded Proteins is their spatial sequestration into several defined compartments. Here, we review the properties, function, and formation of these compartments. Spatial sequestration plays a central role in Protein Quality control and cellular fitness and represe...
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sorting out the trash the spatial nature of eukaryotic Protein Quality control
Current Opinion in Cell Biology, 2014Co-Authors: Emily M Sontag, Willianne I M Vonk, Judith FrydmanAbstract:Failure to maintain Protein homeostasis is associated with aggregation and cell death, and underies a growing list of pathologies including neurodegenerative diseases, aging, and cancer. Misfolded Proteins can be toxic and interfere with normal cellular functions, particularly during proteotoxic stress. Accordingly, molecular chaperones, the ubiquitin-proteasome system (UPS) and autophagy together promote refolding or clearance of misfolded Proteins. Here we discuss emerging evidence that the pathways of Protein Quality control (PQC) are intimately linked to cell architecture, and sequester Proteins into spatially and functionally distinct PQC compartments. This sequestration serves a number of functions, including enhancing the efficiency of Quality control; clearing the cellular milieu of potentially toxic species and facilitating asymmetric inheritance of damaged Proteins to promote rejuvenation of daughter cells.
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the ribosome as a hub for Protein Quality control
Molecular Cell, 2013Co-Authors: Sebastian Pechmann, Felix Willmund, Judith FrydmanAbstract:Cells face a constant challenge as they produce new Proteins. The newly synthesized polypeptides must be folded properly to avoid aggregation. If Proteins do misfold, they must be cleared to maintain a functional and healthy proteome. Recent work is revealing the complex mechanisms that work cotranslationally to ensure Protein Quality control during biogenesis at the ribosome. Indeed, the ribosome is emerging as a central hub in coordinating these processes, particularly in sensing the nature of the nascent Protein chain, recruiting Protein folding and translocation components, and integrating mRNA and nascent chain Quality control. The tiered and complementary nature of these decision-making processes confers robustness and fidelity to Protein homeostasis during Protein synthesis.
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cellular strategies of Protein Quality control
Cold Spring Harbor Perspectives in Biology, 2011Co-Authors: Bryan Chen, Marco Retzlaff, Thomas R Roos, Judith FrydmanAbstract:Eukaryotic cells must contend with a continuous stream of misfolded Proteins that compromise the cellular Protein homeostasis balance and jeopardize cell viability. An elaborate network of molecular chaperones and Protein degradation factors continually monitor and maintain the integrity of the proteome. Cellular Protein Quality control relies on three distinct yet interconnected strategies whereby misfolded Proteins can either be refolded, degraded, or delivered to distinct Quality control compartments that sequester potentially harmful misfolded species. Molecular chaperones play a critical role in determining the fate of misfolded Proteins in the cell. Here, we discuss the spatial and temporal organization of cellular Quality control strategies and their implications for human diseases linked to Protein misfolding and aggregation.
Arthur L Horwich - One of the best experts on this subject based on the ideXlab platform.
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molecular chaperones and Protein Quality control
Cell, 2006Co-Authors: Bernd Bukau, Jonathan S Weissman, Arthur L HorwichAbstract:In living cells, both newly made and preexisting polypeptide chains are at constant risk for misfolding and aggregation. In accordance with the wide diversity of misfolded forms, elaborate Quality-control strategies have evolved to counter these inevitable mishaps. Recent reports describe the removal of aggregates from the cytosol; reveal mechanisms for Protein Quality control in the endoplasmic reticulum; and provide new insight into two classes of molecular chaperones, the Hsp70 system and the AAA+ (Hsp100) unfoldases.
