Results 211 to 220 of about 97,306 (265)
The microbiota-proteostasis axis: implications in neurodegenerative diseases. [PDF]
Philos Trans R Soc Lond B Biol SciCzyż DM, Brown BM.
europepmc +1 more source
Proteostasis breakdown and aggregate diversity in aging and neurodegenerative disease. [PDF]
Front Aging NeurosciKhan ZN.
europepmc +1 more source
Functional interplay between heat shock protein 90 (HSP90) and heat shock factors (HSFs). [PDF]
Cell Stress ChaperonesChakraborty A +2 more
europepmc +1 more source
Synergies and trade-offs in the heat shock response mechanism. [PDF]
PLoS Comput BiolChauhan R, Das B, Sharma AK.
europepmc +1 more source
Proteomic Profiling Reveals Intracellular Regulatory Network Disturbance Induced by QseB Deletion in <i>Glaesserella parasuis</i>. [PDF]
MicroorganismsYan X, Gu C, Zhao M, He L.
europepmc +1 more source
Correction to "Model Peptides Enable Comparisons of Substrate Binding Modes of Hsp70 Molecular Chaperones". [PDF]
BiochemistryBhasne K +5 more
europepmc +1 more source
Some of the next articles are maybe not open access.
Related searches:
Related searches:
Of chromoplasts and chaperones
Trends in Plant Science, 2007Chromoplasts are carotenoid-accumulating plastids found in many fruits and flowers. In a new paper, Li and colleagues show that the Or gene of cauliflower induces differentiation of beta-carotene-containing chromoplasts in the (normally non-pigmented) curd tissue.
Giovanni, Giuliano, Gianfranco, Diretto
openaire +2 more sources
Nature Plants, 2019
Heat-shock protein 90 (HSP90) chaperones play an essential role in plant defence by assisting the folding of client proteins needed for immunity. A newly identified bacterial effector promotes disease by mimicking a HSP90 client, functioning as a minimal kinase that phosphorylates and inactivates the chaperone.
Huan, Chen +2 more
openaire +2 more sources
Heat-shock protein 90 (HSP90) chaperones play an essential role in plant defence by assisting the folding of client proteins needed for immunity. A newly identified bacterial effector promotes disease by mimicking a HSP90 client, functioning as a minimal kinase that phosphorylates and inactivates the chaperone.
Huan, Chen +2 more
openaire +2 more sources
Seminars in Cell & Developmental Biology, 2000
We discuss nuclear chaperones that bind correctly folded protein subunits and mediate molecular interactions, particularly between proteins and nucleic acids. The charge of these chaperones helps to prevent non-specific electrostatic interactions between the components.
A, Philpott, T, Krude, R A, Laskey
openaire +2 more sources
We discuss nuclear chaperones that bind correctly folded protein subunits and mediate molecular interactions, particularly between proteins and nucleic acids. The charge of these chaperones helps to prevent non-specific electrostatic interactions between the components.
A, Philpott, T, Krude, R A, Laskey
openaire +2 more sources