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ProteomicsIdentification of novel constituents of ALIS from macrophage lysates (LPS+/-), LC MS/MS
Macrophages assemble aggresome-like induced structures or ALIS upon LPS or E. coli mediated TLR4 stimulation. These structures are positive for p62, LC3 and ubiquitinated proteins, form irrespective of autophagy, and persist within the cell system up to 48h. However, their composition is not well kn...
ORGANISM(S): Mus musculus (Mouse) 
2024-05-23 | PXD031163 | Pride
Lps Lc ms/ms Raw264.7 Alis Macrophages 
UnknownIntracellular targeting signals and lipid specificity determinants of the ALA/ALIS P4-ATPase complex reside in the catalytic ALA alpha-subunit.
Not available
S-EPMC2828965 | biostudies-literature
Genomics
M. avium complex from patients receiving amikacin liposome inhalation suspension (ALIS)
PRJNA1189166 | ENA
UnknownAccelerated Identification of Cell Active KRAS Inhibitory Macrocyclic Peptides using Mixture Libraries and Automated Ligand Identification System (ALIS) Technology.
Not available
S-EPMC9289880 | biostudies-literature
UnknownTLR-mediated aggresome-like induced structures comprise antimicrobial peptides and attenuate intracellular bacterial survival.
Not available
S-EPMC10916861 | biostudies-literature
UnknownLong-term amikacin liposome inhalation suspension in cystic fibrosis patients with chronic P. aeruginosa infection.
Not available
S-EPMC9076322 | biostudies-literature
UnknownImpact of initiation of amikacin liposome inhalation suspension on hospitalizations and other healthcare resource utilization measures: a retrospective cohort study in real-world settings.
Not available
S-EPMC9719199 | biostudies-literature
UnknownAmikacin Liposome Inhalation Suspension for Mycobacterium avium Complex Lung Disease: A 12-Month Open-Label Extension Clinical Trial.
Not available
S-EPMC8328368 | biostudies-literature
UnknownPB1 and UBA domains of p62 are essential for aggresome-like induced structure formation.
Not available
S-EPMC6640847 | biostudies-literature
UnknownTransient aggregation of ubiquitinated proteins is a cytosolic unfolded protein response to inflammation and endoplasmic reticulum stress.
Not available
S-EPMC3366003 | biostudies-literature
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