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Development of LC3 (show MAP1LC3A Proteins)/GABARAP sensors containing a LIR (show CD300C Proteins) and a hydrophobic domain to monitor autophagy.
GABRP (show GABRP Proteins) plays an important role in placentation and this pathway may be a promising molecular target for the development of novel therapeutic strategies for preeclampsia.
KBTBD6 and KBTBD7 specifically bind to GABARAP proteins.GABARAP proteins mediate localized ubiquitylation of TIAM1 (show TIAM1 Proteins) by CUL3 (show CUL3 Proteins).
Data show that WAC (show WAC Proteins) directly binds to GM130 (show GOLGA2 Proteins) and that this binding is required for autophagosome formation through interacting with GABARAP regulating its subcellular localization.
The interaction of GABARAP with Mulan (show MUL1 Proteins)-Ube2E3 (show UBE2E3 Proteins) supports the role of Mulan (show MUL1 Proteins) as an important regulator of mitophagy.
The FLCN (show FLCN Proteins)-GABARAP association is modulated by the presence of either folliculin (show FLCN Proteins)-interacting protein (FNIP)-1 or FNIP2 (show FNIP2 Proteins) and further regulated by ULK1 (show ULK1 Proteins).
A functional complementation of an lgg-1 null mutant with human GABARAP, its closer homolog showed that it localizes to autophagosomes and can rescue LGG-1 functions in the early embryo.
PLEKHM1 (show PLEKHM1 Proteins) regulates autophagosome-lysosome fusion through homotypic fusion and protein sorting complex and LC3 (show MAP1LC3A Proteins)/GABARAP proteins.
GABARBP dramatically inhibited VEGF (show VEGFA Proteins)-induced endothelial cell proliferation, migration, and tube formation, as well as VEGFR-2 (show KDR Proteins) phosphorylation in vitro.
knockdown of LC3B (show MAP1LC3B Proteins) but not GABARAPs resulted in significant accumulation of p62/Sqstm1 (show SQSTM1 Proteins), one of the selective substrates for autophagy
DLG4/PSD95 (show DLG4 Proteins) and GABARAP were analyzed using zebrafish embryos with morpholino knockdown system as a model organism.
Cells that lacked GABARAPs and mice that lacked Gate-16 (show GABARAPL2 Proteins) alone were defective in the IFN-gamma-induced (show SAMHD1 Proteins) clearance of vacuolar pathogens such as Toxoplasma. GABARAPs are uniquely required for antimicrobial host defense through cytosolic distribution of interferon (show IFNA Proteins)-inducible GTPases.
Ablation of GABARAP inhibits tumor initiation and progression through enhancement of both antitumor immunity and cell death signaling.
Lipidation of the LC3 (show MAP1LC3A Proteins)/GABARAP family of autophagy proteins relies on a membrane-curvature-sensing domain in Atg3 (show ATG3 Proteins).
These results support the regulatory role of Bcl-2 (show BCL2 Proteins) in autophagy and define GABARAP as a novel interaction partner involved in this intricate connection.
Results indicate that, compared with LC3 (show MAP1LC3A Proteins), GABARAP is enriched in the axonal initial segments (AIS (show AR Proteins)).
Gabarap functions in the immune system. It is involved in mitochondrial quality control in macrophages, and thus it influences Nlrp3 (show NLRP3 Proteins) inflammasome-dependent inflammatory responses.
ATG8 (show MAP1LC3B Proteins)-like proteins (MAP1LC3B (show MAP1LC3B Proteins), GABARAP and GABARAPL1 (show GABARAPL1 Proteins)) are novel interactors of MAPK15/ERK8 (show MAPK15 Proteins), a MAP kinase (show MAPK1 Proteins) involved in cell proliferation and transformation.
GABARAP/p62 complex is responsible for impairment of glomerular function and that it retards recovery from the effects of doxorubicin.
because of its stronger binding for hKOPR, GEC1 (show GABARAPL1 Proteins) 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.
Gamma-aminobutyric acid A receptors
GABA(A) receptor-associated protein
, gaba(a) receptor-associated protein
, gamma-aminobutyric acid receptor-associated protein
, gamma-aminobutyric acid receptor associated protein
, cerebelluar GABA-A receptor-associated protein
, GABA(A) receptor associated protein
, GABA-A receptor-associated protein
, gamma-aminobutyric acid reseptor associated protein