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Autophagy is a constitutive process of lysosomal degradation required for maintaining the homeostasis of large molecular complexes and organelles in neurons. Here we reported a systemic investigation of neuronal autophagy targets through integrated proteomics and functional analysis. Proteomic profi...
ORGANISM(S): Homo sapiens (Human) Mus musculus (Mouse) 
2024-06-22 | PXD048730 | Pride
Sepsis-induced acute kidney injury (S-AKI) is the most common complication in hospitalized and critically ill patients, highlighted by a rapid decline of kidney function occurring a few hours or days after sepsis onset. Systemic inflammation elicited by microbial infections is believed to lead to ki...
ORGANISM(S): Mus Musculus (ncbitaxon:10090) 
Limited proteolysis combined with mass spectrometry of farrerol treated. Briefly, cell lysates containing approximately 500 μg of total protein sample were incubated with farrerol or vehicle (DMSO) for 10 min at 25 °C. Proteinase K (5 μg, Sigma–Aldrich) was added simultaneously to each sample for t...
ORGANISM(S): Homo Sapiens 
Although the tubule is the epicenter of damage, kidney fibroblast is increasingly appreciated in governing the prognosis of acute kidney injury (AKI). Smoothened (Smo), a heptahelical transmembrane protein, carries a hedgehog signal to mediate the communications between kidney fibroblasts and tubula...
ORGANISM(S): Mus Musculus (ncbitaxon:10090) 
2021-12-23 | MSV000088609 | MassIVE
The proteomic profiling of the kidney tissue scaffold derived from normal and fibrotic kidneys was carried out by an unbiased LC-MS/MS approach.
ORGANISM(S): Mus <genus> 
2023-03-15 | PXD034281 |
Diabetic kidney disease (DKD) is the most common microvascular complication of type 2 diabetes mellitus (2-DM). Currently, urine and kidney biopsy specimens are the major clinical resources for DKD diagnosis. The diagnostic values of blood in monitoring the onset and progression of DKD have not been...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2021-05-22 | MSV000087487 | GNPS
The RNA-binding protein FUS/TLS, mutation in which is causative of the fatal motor neuron disease ALS, is demonstrated to directly bind to the U1-snRNP and SMN complexes. ALS-causative mutations in FUS/TLS are shown to abnormally enhance their interaction with SMN and reduce interaction with U1-snRN...
ORGANISM(S): Homo sapiens 
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