Results 51 to 60 of about 2,100 (181)
HIV-1 requires capsid remodelling at the nuclear pore for nuclear entry and integration.
PLoS Pathogens, 2021 The capsid (CA) lattice of the HIV-1 core plays a key role during infection. From the moment the core is released into the cytoplasm, it interacts with a range of cellular factors that, ultimately, direct the pre-integration complex to the integration ...
Anabel Guedán +5 more
doaj +1 more source
, 2023 (A) NCOM temperature coefficient Q10 in CPSF6 knockdown versus wild-type cells. Significantly differential responses in PAS selection (i.e., NCOM shifts) upon temperature changes between wild-type and CPSF6 knockdown cells are depicted by orange dots. (B)
Stella Koutsouli (16462758) +10 more
core +1 more source
Cytopmasic CPSF6 and Cyclophilin A Modulate HIV-1 Trafficking [PDF]
, 2020 Human immunodeficiency virus type 1 (HIV-1) capsid binds to multiple host cell proteins after entry into a cell, including cyclophilin A (CypA) and cleavage and polyadenylation specificity factor 6 (CPSF6), which is expressed predominantly in the nucleus.
Zhong, Zhou
core
Differential role for phosphorylation in alternative polyadenylation function versus nuclear import of SR-like protein CPSF6 [PDF]
, 2019 Cleavage factor I mammalian (CFIm) complex, composed of cleavage and polyadenylation specificity factor 5 (CPSF5) and serine/arginine-like protein CPSF6, regulates alternative polyadenylation (APA).
Parmit K Singh (8128404) +7 more
core +2 more sources
mBio, 2022 The relationship between spatiotemporal distribution of HIV-1 proviruses and their transcriptional activity is not well understood. To elucidate the intranuclear positions of transcriptionally active HIV-1 proviruses, we utilized an RNA fluorescence in ...
Ryan C. Burdick +5 more
doaj +1 more source
Depletion of CPSF6 induces a global shift towards shorter 3′ UTRs.
, 2023 (A) Histogram of the center of read distribution along the 3′ UTR, normalized to the length of the isoform’s 3′ UTR (NCOM), in control (blue) and CPSF6-depleted (red) cells.
Stella Koutsouli (16462758) +10 more
core +1 more source
Proteins showing a significantly altered abundance in wild-type and CPSF6 knockdown cells at 37°C.
, 2023 Information about all 1,683 peptides showing a significantly different abundance after CPSF6 knockdown at 37°C is deposited in the table. Column A depicts the corresponding gene symbol.
Stella Koutsouli (16462758) +10 more
core +1 more source
Frontiers in Oncology, 2022 Retinoic acid receptor gamma (RARG) gene rearrangement has been reported in several acute myeloid leukemia (AML) patients. They resemble classical acute promyelocytic leukemia (APL) patients in clinical features, morphology, and immunophenotype but do ...
Junmei Zhao +7 more
doaj +1 more source
CPSF6 binds diverse lentiviral capsids.
, 2012 Isothermal titration calorimetry (ITC) of CPSF6313–327 against CAN domains of lentiviral capsids. CPSF6313–327 binding to HIV-1 is specific (A), being abolished by CA mutation N74D (B). CPSF6313–327 also binds to diverse primate lentiviral capsids, HIV-2,
Vineet N. KewalRamani (138643) +8 more
core +1 more source
CPSF6 deficiency promotes IFN-I signalling activation.
(A, B) The heatmap shows the mRNA abundance of IFNB and ISGs in WT, Cpsf6-/-L929PLVX and Cpsf6-/- L929CPSF6 L929 cells infected with VSV-eGFP (A) or stimulated with poly (I:C) or Poly (dA:dT) (B) at indicated time points.
Rong Chen (29176) +12 more
core +2 more sources