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1.
Annu Rev Biochem ; 87: 1-21, 2018 06 20.
Artículo en Inglés | MEDLINE | ID: mdl-29925256

RESUMEN

My initial research experience involved studying how bacteria synthesize nucleotide sugars, the donors for the formation of cell wall polysaccharides. During this time, I became aware that mammalian cells also have a surface coat of sugars and was intrigued as to whether these sugars might be arranged in specific sequences that function as information molecules in biologic processes. Thus began a long journey that has taken me from glycan structural analysis and determination of plant lectin-binding preferences to the biosynthesis of Asn-linked oligosaccharides and the mannose 6-phosphate (Man-6-P) lysosomal enzyme targeting pathway. The Man-6-P system represents an early example of a glycan serving as an information molecule in a fundamental cellular function. The remarkable advances in the field of glycobiology since I entered have uncovered scores of additional examples of oligosaccharide-lectin interactions mediating critical biologic processes. It has been a rewarding experience to participate in the efforts that have established a central role for glycans in biology.


Asunto(s)
Glicómica/historia , Proteínas Adaptadoras del Transporte Vesicular/historia , Proteínas Adaptadoras del Transporte Vesicular/metabolismo , Animales , Historia del Siglo XX , Historia del Siglo XXI , Humanos , Manosafosfatos/historia , Manosafosfatos/metabolismo , Redes y Vías Metabólicas , Hidrolasas Diéster Fosfóricas/historia , Hidrolasas Diéster Fosfóricas/metabolismo , Receptor IGF Tipo 2/historia , Receptor IGF Tipo 2/metabolismo , Transferasas (Grupos de Otros Fosfatos Sustitutos)/historia , Transferasas (Grupos de Otros Fosfatos Sustitutos)/metabolismo , Estados Unidos
2.
Proteins ; 88(9): 1251-1259, 2020 09.
Artículo en Inglés | MEDLINE | ID: mdl-32394426

RESUMEN

Ancestral sequence reconstruction has had recent success in decoding the origins and the determinants of complex protein functions. However, phylogenetic analyses of remote homologues must handle extreme amino acid sequence diversity resulting from extended periods of evolutionary change. We exploited the wealth of protein structures to develop an evolutionary model based on protein secondary structure. The approach follows the differences between discrete secondary structure states observed in modern proteins and those hypothesized in their immediate ancestors. We implemented maximum likelihood-based phylogenetic inference to reconstruct ancestral secondary structure. The predictive accuracy from the use of the evolutionary model surpasses that of comparative modeling and sequence-based prediction; the reconstruction extracts information not available from modern structures or the ancestral sequences alone. Based on a phylogenetic analysis of a sequence-diverse protein family, we showed that the model can highlight relationships that are evolutionarily rooted in structure and not evident in amino acid-based analysis.


Asunto(s)
Proteínas Adaptadoras del Transporte Vesicular/química , Proteínas Bacterianas/química , Evolución Molecular , Modelos Estadísticos , Proteínas Adaptadoras del Transporte Vesicular/historia , Animales , Bacterias/química , Bacterias/clasificación , Bacterias/metabolismo , Proteínas Bacterianas/historia , Simulación por Computador , Historia del Siglo XXI , Historia Antigua , Humanos , Mamíferos/clasificación , Mamíferos/metabolismo , Filogenia , Plantas/química , Plantas/clasificación , Plantas/metabolismo , Estructura Secundaria de Proteína
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