about
Cold-adaptation in sea-water-borne signal proteins: sequence and NMR structure of the pheromone En-6 from the Antarctic ciliate Euplotes nobiliiNuclear Magnetic Resonance Structure Shows that the Severe Acute Respiratory Syndrome Coronavirus-Unique Domain Contains a Macrodomain FoldMolecular cold-adaptation: comparative analysis of two homologous families of psychrophilic and mesophilic signal proteins of the protozoan ciliate, EuplotesNMR structure of the protein NP_247299.1: comparison with the crystal structureComparison of NMR and crystal structures for the proteins TM1112 and TM1367Comparison of NMR and crystal structures highlights conformational isomerism in protein active sitesAntarctic and Arctic populations of the ciliate Euplotes nobilii show common pheromone-mediated cell-cell signaling and cross-matingThe J-UNIO protocol for automated protein structure determination by NMR in solutionNMR-profiles of protein solutionsAPSY-NMR for protein backbone assignment in high-throughput structural biology.Revisiting fifty years of research on pheromone signaling in ciliates.Molecular Structures and Coding Genes of the Water-Borne Protein Pheromones of Euplotes petzi, an Early Diverging Polar Species of Euplotes.
P50
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P50
description
onderzoeker
@nl
name
Bill Pedrini
@ast
Bill Pedrini
@en
Bill Pedrini
@es
Bill Pedrini
@nl
Bill Pedrini
@sl
type
label
Bill Pedrini
@ast
Bill Pedrini
@en
Bill Pedrini
@es
Bill Pedrini
@nl
Bill Pedrini
@sl
prefLabel
Bill Pedrini
@ast
Bill Pedrini
@en
Bill Pedrini
@es
Bill Pedrini
@nl
Bill Pedrini
@sl