Direction repulsion and attraction as functions of the veridical direction-separation.

<p><b>A.</b> Difference between the perceived direction-separation and the veridical direction- separation at the motion coherence of 60%. <b>B.</b> Difference between the perceived direction-separation and the veridical direction-separation normalized by the veridical direction-separation at the motion coherence of 60%. <b>C.D.</b> The motion coherence was at 100%. Error bars represent Standard Errors.</p

Illustration of visual stimuli and the temporal sequence of an experimental trial.

<p>The test stimuli (T) were spatially-overlapping random-dot patches moving in two directions. Red and black colors are used to illustrate two different sets of random dots, whereas the actual random-dot patches were achromatic and had the same luminance. The comparison stimuli (C) were two static lines forming an angle. Subjects compared the direction separation of the test stimuli with the angle of the comparison stimuli. The order of stimuli appearance was randomized.</p

Perceived direction-separation as a function of motion coherence. A.

<p>The veridical direction-separation of the random-dot stimuli was 30°, indicated by the dash line. <b>B.</b> The veridical direction-separation of the random-dot stimuli was 60°. Error bars represent Standard Errors.</p

Chemical structures of NAD+, ABT-888, AZD2281, XAV939, IWR1, and IWR2 and the binding modes of ABT-888 and XAV939 to PARP2 and TNKS2.

<p>The nicotinamide in NAD+ and the nicotinamide-mimic moieties in ABT-888, AZD2281, and XAV939 are highlighted in red. ABT-888 and XAV939 bind to conserved serine and glycine residues of PARP2 and TNKS2 through three hydrogen bonds. These serine and glycine residues as well as the hydrogen bonds are highlighted in blue.</p

Structure based sequence alignment of TNKS1, TNKS2, and other PARP family members.

<p>Key residues Pro1187 (following deletion of two amino acids) and His1201 of the induced pocket in TNKS1 are highlighted, together with their equivalent residues in other PARP proteins, to illustrate the poor conservation of these amino acids.</p

Structure activity relationship of IWR compounds.

<p>Structure activity relationship of IWR compounds.</p

Crystal Structure of the TNKS1/IWR2 complex.

<p>(A) Surface representation of TNKS1 (colored in wheat) with IWR2 (colored in green) bound. XAV939 (colored in yellow) from the crystal structure of TNKS2/XAV939 is superimposed to illustrate that IWR2 binds to a different pocket other than the nicotinamide pocket. (B) Superposition of crystal structures of TNKS1/IWR2 (colored in wheat and green) and apo TNKS1 (colored in cyan), with residues Phe1188 and His1201 in sticks, to illustrate the opening of the induced pocket in TNKS1 upon IWR2 binding. IWR2 binds to TNKS1 through three highlighted hydrogen bonds. (C) The induced pocket, showing the hydrogen bond and hydrophobic interactions between IWR2 and TNKS1 residues, colored as in (A).</p

Metal-Free Mediated Meerwein-Type Reaction: A Radical Cascade Arylation/Aryl Migration/Desulfonylation of Conjugated Alkenes

A metal-free cascade arylation/aryl migration/desulfonylation of <i>N</i>-phenyl-<i>N</i>-(phenylsulfonyl)­meth­acryl­amide is described. The in situ generated diazonium salts from anilines and <i>t</i>-BuONO are used as aryl precursors. This process provides an efficient strategy for the synthesis of α-all-carbon quaternary stereocenters amides. A radical mechanism was proposed for this transformation

Structural Basis for the Interaction between Casein Kinase 1 Delta and a Potent and Selective Inhibitor

Casein kinase 1 delta (CK1δ) and its closest homologue CK1ε are key regulators of diverse cellular growth and survival processes such as Wnt signaling, DNA repair, and circadian rhythms. We report three crystal structures of the kinase domain of human CK1δ, one apo and two complexed with a potent and selective CK1δ/ε inhibitor PF670462 in two different crystal forms. These structures provide a molecular basis for the strong and specific inhibitor interactions and suggest clues for further development of CK1δ/ε inhibitors

Structural Basis for the Potent and Selective Inhibition of Casein Kinase 1 Epsilon

Casein kinase 1 epsilon (CK1ε) and its closest homologue CK1δ are key regulators of diverse cellular processes. We report two crystal structures of PF4800567, a potent and selective inhibitor of CK1ε, bound to the kinase domains of human CK1ε and CK1δ as well as one apo CK1ε crystal structure. These structures provide a molecular basis for the strong and specific inhibitor interactions with CK1ε and suggest clues for further development of CK1δ inhibitors