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Data from: A?42 fibril formation from predominantly oligomeric samples suggests a link between oligomer heterogeneity and fibril polymorphism
负责人:
关键词:
amyloid;oligomerization;aggregation kinetics;neurodegeneration;Alzheimer's disease
DOI:
doi:10.5061/dryad.7n4c218
摘要:
all process of A? aggregation and fibrillization. Here we show that A?42 spontaneously forms oligomers with a wide range of sizes in the same sample. These A?42 samples conta
Data from: A mix-and-click method to measure amyloid-? concentration with sub-micromolar sensitivity
负责人:
关键词:
Protein aggregation;A?42;Alzheimer disease;A?40;Fluorescamine;amyloid
DOI:
doi:10.5061/dryad.7mg3h
摘要:
concentration determination in A? oligomerization and fibrillization experiments.
Data from: Characterization of C-ring component assembly in flagellar motors from amino acid coevolution
负责人:
关键词:
oligomerization;bacterial flagellar motors;molecular complexes;direct coupling analysis;Thermotoga maritma;molecular dynamics;molecular evolution
DOI:
doi:10.5061/dryad.0mv6t
摘要:
Bacterial flagellar motility, an important virulence factor, is energized by a rotary motor localized within the flagellar basal body. The rotor
Data from: Differential gene expression analysis of symbiotic and aposymbiotic Exaiptasia anemones under immune challenge with Vibrio coralliilyticus
负责人:
关键词:
Anthozoan;aposymbiotic;immune;Cnidarian;transcriptome;Exaiptasia;symbiotic;gene expression;Exaiptasia pallida
DOI:
doi:10.5061/dryad.364j18m
摘要:
complement, coagulation, nucleotide-binding and oligomerization domain (NOD), and Toll for Vibrio exposure and coagulation and apoptosis for aposymbiosis.
Data from: Cryptic genetic variation shapes the adaptive evolutionary potential of enzymes
负责人:
关键词:
DOI:
doi:10.5061/dryad.qk653b3
摘要:
, the ortholog with the highest initial activity evolved to a less-optimal and phenotypically distinct outcome through changes in expression, oligomerization
Data from: The basic keratin 10-binding domain of the virulence-associated pneumococcal serine-rich protein PsrP adopts a novel MSCRAMM fold
负责人:
关键词:
CD;AUC;SAXS;ELISA
DOI:
doi:10.5061/dryad.605v1
摘要:
virulence factor whose functional binding region (BR) binds to keratin-10 (KRT10) and promotes pneumococcal biofilm formation through self-oligomerization. We prese

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