l242  (ATCC)

Journal: The Journal of Investigative Dermatology

Article Title: Notch-Mediated Generation of Monocyte-Derived Langerhans Cells: Phenotype and Function

doi: 10.1016/j.jid.2020.05.098

Figure Lengend Snippet: Fluorophore-Labeled Antibodies Used for Flow Cytometry

Article Snippet: HLA-DR , L242 , BioLegend.

Techniques:

Journal: International Journal of Molecular Sciences

Article Title: Molecular Basis of the Pathogenic Mechanism Induced by the m.9191T>C Mutation in Mitochondrial ATP6 Gene

doi: 10.3390/ijms21145083

Figure Lengend Snippet: Evolutionary conservation and topology of a L242 and a L242S/T residues. ( A ) Amino-acid alignment of the C-terminal ΔΨ-helix ( a H6) of subunits a from various mitochondrial origins: Saccharomyces cerevisiae ( S.c. ), Schizosaccharomyces pombe ( S.p. ), Yarrowia lipolytica ( Y.l. ), Arabidopsis thaliana ( A.t. ), Polytomella sp ( P.sp. ), Bos taurus ( B.t. ), Sus scrofa ( S.s. ), and Homo sapiens ( H.s. ). At the top and bottom, are numbered the residues in S.c. mature protein (i.e., without the first ten residues that are moved during assembly) and in the H.s. protein, respectively. Strictly conserved residues are in white on a red background while similar residues are in red on a white background with blue frames. The secondary structures of the S.c. protein marked above the alignment are according to . Top view from the matrix ( B ) and side view ( C ) of the c 10 -ring and subunit a and the pathway along which protons are transported from the intermembrane space (IMS) to the mitochondrial matrix. The side chains of the two residues essential to this transfer ( a R176 and c E59), and of residues presumed to be important for this transfer, in the n-side cleft ( a H185, a E223) and in the p-side cleft ( a E162, a D244), and of a L242 are drawn as ball and stick. ( D ) The wild type a L242 residue is within a 4-helix bundle ( a H2, a H3, a H4 and a H6) in proximity to a I77, a Y85, a M88 and a N129. This bundle is disrupted with a L242P and fully preserved with a L242S and a L242T, which presumably involves the formation of a hydrogen bond between the hydroxyl group of a S242 or a T242 and the amide group of a N129 as depicted ( E ). The partial impairment of ATP synthase function with a S242 or a T242 is possibly caused by a local disturbance at the level of a D244 as indicated by the double arrowed curved trait (see Text). ( F ) In a L242A (green) and a L242Q (cyan) a cavity or clashes between neighboring helices preclude the helix bundle stability. ( G ) Schematic top view showing the probable bend of a H6 due to the a S240P mutation that should deepen the n -side pocket. The a H6 helix axis is drawn as a continuous (S240) and dashed (P240) line. For sake of clarity, only relevant side chains are depicted.

Article Snippet: In S. cerevisiae cryo-EM structure (Pdb_id:6b8h, 3.4 Å resolution [6), a L242 is located near the C-terminus of a H6, at the heart of the 4-helix bundle, quite far away from the a / c interface (Pdb_id:6b8h, 3.4 Å resolution) ( D).

Techniques: Mutagenesis

Journal: British journal of haematology

Article Title: Targeting Oncogenic Interleukin-7 Receptor Signalling with N-acetylcysteine in T-cell acute lymphoblastic leukaemia

doi: 10.1111/bjh.13115

Figure Lengend Snippet: Sanger sequencing results for IL7R exon 6 from 21 T-ALL cell lines together with STAT5 phosphorylation status.

Article Snippet: Cell viability was tested using the Cell Titer Glo assay after 48 h of NAC treatment. table ft1 table-wrap mode="anchored" t5 caption a7 T-ALL cell line IL7R exon 6 Phospho-STAT5 status * (Y964) IC 50 to NAC (μM) ALL-SIL WT + Be13 WT 91.2 CCRF-CEM WT − 61.7 DND-41 L242_L243 ins LSRC ++ 74.1 HPB-ALL WT − >300 H-SB2 WT + JURKAT WT − 177.8 K3P WT KOPT-K1 WT ++ 257.0 LOUCY WT − MOLT-3 WT MOLT-4 WT − MOLT-16 WT − >300 P12-ICHIKAWA WT − PEER WT + PF382 WT − RPMI-8402 WT − >300 SKW-3/KE-37 WT − SUP-T1 WT SUP-T11 WT − SUP-T13 WT + 141.3 T-ALL1 WT 162.2 Open in a separate window * As determined by Western blot.

Techniques: Sequencing