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Lis1 has two opposing modes of regulating dynein, being capable of inducing both low and high affinity for the microtubule; study shows that these opposing modes depend on the stoichiometry of Lis1 binding to dynein and that this stoichiometry is regulated by the nucleotide state of dynein's AAA3 domain.
genetic variants in LIS1 may contribute to AML (show RUNX1 Proteins) risk in Chinese population.
Val279Phe gene polymorphisms in PAF-AH (show Lp-PLA2 Proteins) are associated with PAF-AH (show Lp-PLA2 Proteins) activity and PAF (show KIAA0101 Proteins) and GMP-140 (show SELP Proteins) levels and may be a risk factor for Henoch-Schonlein purpura with gastrointestinal bleeding
There were no significant associations between R92H and A379V variants of PAF-AH (show Lp-PLA2 Proteins) gene and risk of polycystic ovary syndrome in Chinese women.
results indicate that the NAGK-dynein interaction with the involvements of Lis1 and NudE1 plays an important role in prophase nuclear envelope breakdown (NEB) and metaphase MT-KT attachment during eukaryotic cell division.
Results showed that miR (show MLXIP Proteins)-144 was reduced in cholangiocarcinoma tissues and suggested that miR (show MLXIP Proteins)-144 may be an essential suppresser of cholangiocarcinoma cell proliferation and invasion through targeting LIS1.
LIS1 and TSNAX genes are not associated with susceptibility to bipolar I disorder in Chinese Han population.
Identify a key role for Lis1 in hematopoietic stem cells and mark its directed control of asymmetric division as a critical regulator of normal and malignant hematopoietic development
LIS1 gene duplication is associated with developmental, behavioral and brain abnormalities.
LIS1 is required for dynein-mediated transport induced by membrane tethering of BICD2-N and LIS1 contributes to dynein accumulation at microtubule plus ends and BICD2-positive cellular structures.
Nudel (show NDEL1 Proteins)/NudE and Lis1 promote dynein and dynactin (show DCTN1 Proteins) interaction in the context of spindle morphogenesis.
Full rescue by the coiled-coil domain requires LIS1 binding, and increasing LIS1 concentration partly rescues aster formation
PAFAH Ib phospholipase A2 (show YWHAZ Proteins) subunits have distinct roles in maintaining Golgi structure and function.
Results suggest that LIS1 is essential to mediate genomic union in a process that involves the dynein-dynactin (show DCTN1 Proteins) complex.
findings suggest that Lis1 is required for germinal center (GC) B (show NPR2 Proteins) cell expansion, affinity maturation, and maintaining functional intact GC response, thus ensuring both the quantity and quality of Ab response
Lis1 plays an important role in T cell homeostasis and the generation of memory T lymphocytes.
This study demonstrated that LIS-1 regulate the septohippocampal cholinergic projection developmental.
Lis1 is required for the expansion of FL-HSCs by ensuring their genomic stability and therefore promoting their survival.
Results show that LIS1 acts via the LIS1-NDEL1 (show NDEL1 Proteins)-dynein complex to regulate astral microtubule MT plus-ends dynamics and establish proper contacts of MTs (show NEU2 Proteins) with the cell cortex to ensure precise cell division.
Conditional deletion of Lis1 in the hematopoietic system led to a severe bloodless phenotype, depletion of the stem cell pool and embryonic lethality.
Rab6a mediates LIS1 release from a LIS1-dynein complex followed by dynein activation.
LIS1 plays prominently in filopodia dynamics and dendritic spine turnover.
Nde1 and Lis1 regulate central nervous system development by interpreting midline signals differentially.
Lis1 mediates planar polarity of auditory hair cells through regulation of microtubule organization.
This locus was identified as encoding a gene that when mutated or lost caused the lissencephaly associated with Miller-Dieker lissencephaly syndrome. This gene encodes the non-catalytic alpha subunit of the intracellular Ib isoform of platelet-activating factor acteylhydrolase, a heterotrimeric enzyme that specifically catalyzes the removal of the acetyl group at the SN-2 position of platelet-activating factor (identified as 1-O-alkyl-2-acetyl-sn-glyceryl-3-phosphorylcholine). Two other isoforms of intracellular platelet-activating factor acetylhydrolase exist: one composed of multiple subunits, the other, a single subunit. In addition, a single-subunit isoform of this enzyme is found in serum.
, PAF acetylhydrolase 45 kDa subunit
, PAF-AH 45 kDa subunit
, PAF-AH alpha
, PAF-AH beta
, PAFAH alpha
, lissencephaly-1 protein
, platelet-activating factor acetylhydrolase IB subunit alpha
, platelet-activating factor acetylhydrolase beta subunit (PAF-AH beta)
, platelet-activating factor acetylhydrolase, isoform 1b, subunit 1
, platelet-activating factor acetylhydrolase, isoform Ib, alpha subunit 45kDa
, lissencephaly 1 protein
, platelet-activating factor acetylhydrolase, isoform Ib, alpha subunit (45kD)
, platelet-activating factor acetylhydrolase, isoform Ib, subunit 1 (45kDa)
, lissencephaly-1 homolog
, lissencephaly-1 homolog B
, platelet-activating factor acetylhydrolase Ib-alpha subunit
, Miller-Dieker syndrome chromosome region
, Lissencephaly-1 protein
, platelet-activating factor acetylhydrolase isoform Ib alpha subunit
, platelet-activating factor acetylhydrolase 1b, regulatory subunit 1
, platelet-activating factor acetylhydrolase, isoform 1b, beta1 subunit