Optimizing photoactivation of PA‐mCherry for optical pooled CRISPR screens
Photoactivatable PA‐mCherry finds widespread use to optically tag individual cells. However, confocal 405 nm UV laser‐scanning (normal scan) is much less efficient than widefield UV illumination, limiting the use of PA‐mCherry on confocal instruments. We remedy this limitation by reporting that rapid and repeated confocal scanning with a low‐intensity,
Sravasti Mukherjee +3 more
wiley +1 more source
A Novel SIL1 Variant (p.E342K) Associated with Marinesco-Sjögren Syndrome Impairs Protein Stability and Function. [PDF]
Ruggieri AG +16 more
europepmc +1 more source
Genetic mapping of novel QTL for seed protein stability in food-grade soybean (Glycine max). [PDF]
Mitchell AA +9 more
europepmc +1 more source
<i>TSC2</i> GAP Domain V1646Cfs*7 Variant Alters Protein Stability and Interaction Networks in Tuberous Sclerosis Complex. [PDF]
Utami KH +7 more
europepmc +1 more source
The miR164e-NAC32 module orchestrates maize plant height via post-translational regulation of DELLA protein stability. [PDF]
Peng C +8 more
europepmc +1 more source
Kap1 Regulates Protein Stability of Nanog by Interfering with Fbxw8-Dependent Ubiquitination. [PDF]
Moon HJ +6 more
europepmc +1 more source
Protocol for monitoring the stability of transcription factor EB using global protein stability assay. [PDF]
Wang B +6 more
europepmc +1 more source
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The relevance of protein stability for biological function and molecular evolution is widely recognized. Protein stability, however, comes in two flavours: thermodynamic stability, which is related to a low amount of unfolded and partially-unfolded states in equilibrium with the native, functional protein; kinetic stability, which is related to a high ...
José Manuel Sánchez Ruiz
exaly +3 more sources
Stabilization centers and protein stability
Theoretical Chemistry Accounts: Theory, Computation, and Modeling (Theoretica Chimica Acta), 2001The well-balanced stability of protein structures allows large-scale fluctuations, which are indispensable in many biochemical functions, ensures the long-term persistence of the equilibrium structure and it regulates the degradation of proteins to provide amino acids for biosynthesis.
Á. Simon +5 more
openaire +1 more source
Abstract The maximum melting points of 14 proteins in respect to pH are reported, the correlation coefficient between the hydrophobic index and the melting point was +0.622, and that between the average residue volumes and the melting points was +0.960.
H B, Bull, K, Breese
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