Pages that link to "Q30157694"
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The following pages link to The in vivo and in vitro aggregation properties of globular proteins correlate with their conformational stability: the SH3 case (Q30157694):
Displayed 22 items.
- On the aggregation properties of FMRP--a link with the FXTAS syndrome? (Q24298281) (← links)
- Mapping the structure of amyloid nucleation precursors by protein engineering kinetic analysis (Q30009502) (← links)
- Microcanonical thermostatistics of coarse-grained proteins with amyloidogenic propensity. (Q30009951) (← links)
- A single mutation in an SH3 domain increases amyloid aggregation by accelerating nucleation, but not by destabilizing thermodynamically the native state (Q30157375) (← links)
- Influence of the stability of a fused protein and its distance to the amyloidogenic segment on fibril formation (Q33760952) (← links)
- Influence of pH control in the formation of inclusion bodies during production of recombinant sphingomyelinase-D in Escherichia coli (Q34253830) (← links)
- Aggregation propensity of neuronal receptors: potential implications in neurodegenerative disorders. (Q37474322) (← links)
- Protein folding and aggregation in bacteria (Q37722588) (← links)
- Association between foldability and aggregation propensity in small disulfide-rich proteins (Q41566585) (← links)
- Cytosolic selection systems to study protein stability. (Q41836712) (← links)
- Optimizing protein stability in vivo (Q41858624) (← links)
- Thermodynamic stability, unfolding kinetics, and aggregation of the N-terminal actin-binding domains of utrophin and dystrophin. (Q41951688) (← links)
- A single cysteine post-translational oxidation suffices to compromise globular proteins kinetic stability and promote amyloid formation. (Q47408751) (← links)
- In vivo amyloid aggregation kinetics tracked by time-lapse confocal microscopy in real-time. (Q50239011) (← links)
- Fluorescent dye ProteoStat to detect and discriminate intracellular amyloid-like aggregates in Escherichia coli. (Q50462869) (← links)
- Aggregating sequences that occur in many proteins constitute weak spots of bacterial proteostasis. (Q52803242) (← links)
- Thioflavin-S staining coupled to flow cytometry. A screening tool to detect in vivo protein aggregation (Q58434417) (← links)
- Formulations That Suppress Aggregation During Long-Term Storage of a Bispecific Antibody are Characterized by High Refoldability and Colloidal Stability (Q90476000) (← links)
- An Evaluation of the Potential of NMR Spectroscopy and Computational Modelling Methods to Inform Biopharmaceutical Formulations (Q91693962) (← links)
- Aggrescan3D (A3D) 2.0: prediction and engineering of protein solubility (Q91719617) (← links)
- Computational Assessment of Bacterial Protein Structures Indicates a Selection Against Aggregation (Q92528700) (← links)
- Nucleic acids in inclusion bodies obtained from E. coli cells expressing human interferon-gamma (Q97546256) (← links)