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Human GABARAPL1 Protein expressed in Escherichia coli (E. coli) - ABIN2006228
Choi, Lee, Lee, Kim: Rapid detection of 6×-histidine-labeled recombinant proteins by immunochromatography using dye-labeled cellulose nanobeads. in Biotechnology letters 2015
GABARAPs are identified as the first known direct interaction partners of Nef that are essential for its plasma membrane localization.
these results indicate that miR-195 regulates cell proliferation, migration, angiogenesis and autophagy of hEPCs by targeting GABARAPL1
Our data demonstrated that a specific decrease of GABARAPL1 expression in breast cancers was associated with both DNA methylation and histone deacetylation and that CREB-1 recruitment on GABARAPL1
Androgen deprivation downregulates Gabarapl1 in an AR dependent manner, resulting in the increase of autophagy flux
Results showed that the mRNA and protein levels of GABARAPL1 and GATE-16 were decreased in the cerebellum of multiple system atrophy relative to controls
GABARAPL1 plays an important role in cell proliferation, invasion, and autophagic flux, as well as in mitochondrial homeostasis and cellular metabolic programs in a breast cancer cell line.
Kaplan-Meier survival analysis showed a significant association between low GABARAPL1 expression and poor prognosis of HCC patients.
Lipidation of the LC3/GABARAP family of autophagy proteins relies on a membrane-curvature-sensing domain in Atg3.
Data demonstrate that HSP90 interacts and protects GABARAPL1 from its degradation by the proteasome.
analysis of specific functions of GABARAPL1 [review]
Atg8 interacting motif (AIM) in Stbd1 is necessary for GABARAPL1 binding.
Results indicate that the presence of a tryptophan residue in the LIR motif increases the binding affinity of GABARAPL-1/NBR1-LIR complex.
Gabarapl1 mRNA expression in breast tumours is a good indicator of the risk of recurrence, specifically in lymph nodes positive patients.
Gec1/GABARAPL1 was more expressed than GABARAP in the central nervous system (CNS), while GABARAP was more expressed in endocrine glands.
GEC1 interacts with the kappa opioid receptor and enhances expression of the receptor
GEC1-kappa opioid receptor binding involves hydrophobic interactions: GEC1 has chaperone-like effect.
Caspase cleavage of Atg4D stimulates GABARAP-L1 processing and triggers mitochondrial targeting and apoptosis.
Cells that lacked GABARAPs and mice that lacked Gate-16 alone were defective in the IFN-gamma-induced clearance of vacuolar pathogens such as Toxoplasma. GABARAPs are uniquely required for antimicrobial host defense through cytosolic distribution of interferon-inducible GTPases.
study of cerebral GABARAPL1 protein expression provides insight into its role in the development and homeostasis of the mouse brain
GABARAPL1 negatively regulates Wnt/beta-catenin signaling by mediating Dvl2 degradation through the autophagy pathway.
because of its stronger binding for hKOPR, GEC1 is able to be recruited by hKOPR sufficiently without membrane association via its C-terminal modification; however, du GABARAP appears to require C-terminal modifications to enhance KOPR expression.
Expression of mouse Atg8L in HEK293 cells led to cleavage of its C-terminus. (Atg8L/Apg8l)and is the fourth modifier of mammalian Atg8 conjugation. (ATG8L/Apg8L)
Increases cell-surface expression of kappa-type opioid receptor through facilitating anterograde intracellular trafficking of the receptor (By similarity).
GABA(A) receptor-associated protein like 1
, gamma-aminobutyric acid receptor-associated protein-like 1
, GABA(A) receptor-associated protein-like 1
, GABA(A) receptors associated protein like 3
, early estrogen-regulated protein
, glandular epithelial cell protein 1
, MDBK gamma-aminobutyric acid-receptor-associated protein
, gamma-aminobutyric acid (GABA(A)) receptor-associated protein-like 1