Search results for "Endoplasmic-reticulum-associated protein degradation"

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Folding and stability of the aquaglyceroporin GlpF: Implications for human aqua(glycero)porin diseases

2015

AbstractAquaporins are highly selective polytopic transmembrane channel proteins that facilitate the permeation of water across cellular membranes in a large diversity of organisms. Defects in aquaporin function are associated with common diseases, such as nephrogenic diabetes insipidus, congenital cataract and certain types of cancer. In general, aquaporins have a highly conserved structure; from prokaryotes to humans. The conserved structure, together with structural dynamics and the structural framework for substrate selectivity is discussed. The folding pathway of aquaporins has been a topic of several studies in recent years. These studies revealed that a conserved protein structure ca…

Models MolecularProtein activityAmino Acid MotifsMolecular Sequence DataBiophysicsGene ExpressionPorinsAquaporinDiabetes Insipidus NephrogenicEndoplasmic-reticulum-associated protein degradationAquaporinsBiochemistryCataractProtein Structure SecondaryProtein structureNeoplasmsEscherichia coliGlpFHumansProtein foldingConserved SequenceProtein StabilityChemistryurogenital systemEscherichia coli ProteinsAquaporinWaterCell BiologyTransmembrane proteinCell biologyFolding (chemistry)Membrane proteinBiochemistryMembrane proteinPorinProtein foldingBiochimica et Biophysica Acta (BBA) - Biomembranes
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