Motion coordination and programmable teleoperation between two industrial robots

Tasks for two coordinated industrial robots always bring the robots in contact with a same object. The motion coordination among the robots and the object must be maintained all the time. To plan the coordinated tasks, only one robot's motion is planned according to the required motion of the object. The motion of the second robot is to follow the first one as specified by a set of holonomic equality constraints at every time instant. If any modification of the object's motion is needed in real-time, only the first robot's motion has to be modified accordingly in real-time. The modification for the second robot is done implicitly through the constraint conditions. Thus the operation is simplified. If the object is physically removed, the second robot still continually follows the first one through the constraint conditions. If the first robot is maneuvered through either the teach pendant or the keyboard, the second one moves accordingly to form the teleoperation which is linked through the software programming. Obviously, the second robot does not need to duplicate the first robot's motion. The programming of the constraints specifies their relative motions

SUMO Modification Stabilizes Enterovirus 71 Polymerase 3D To Facilitate Viral Replication.

Accumulating evidence suggests that viruses hijack cellular proteins to circumvent the host immune system. Ubiquitination and SUMOylation are extensively studied posttranslational modifications (PTMs) that play critical roles in diverse biological processes. Cross talk between ubiquitination and SUMOylation of both host and viral proteins has been reported to result in distinct functional consequences. Enterovirus 71 (EV71), an RNA virus belonging to the family Picornaviridae, is a common cause of hand, foot, and mouth disease. Little is known concerning how host PTM systems interact with enteroviruses. Here, we demonstrate that the 3D protein, an RNA-dependent RNA polymerase (RdRp) of EV71, is modified by small ubiquitin-like modifier 1 (SUMO-1) both during infection and in vitro Residues K159 and L150/D151/L152 were responsible for 3D SUMOylation as determined by bioinformatics prediction combined with site-directed mutagenesis. Also, primer-dependent polymerase assays indicated that mutation of SUMOylation sites impaired 3D polymerase activity and virus replication. Moreover, 3D is ubiquitinated in a SUMO-dependent manner, and SUMOylation is crucial for 3D stability, which may be due to the interplay between the two PTMs. Importantly, increasing the level of SUMO-1 in EV71-infected cells augmented the SUMOylation and ubiquitination levels of 3D, leading to enhanced replication of EV71. These results together suggested that SUMO and ubiquitin cooperatively regulated EV71 infection, either by SUMO-ubiquitin hybrid chains or by ubiquitin conjugating to the exposed lysine residue through SUMOylation. Our study provides new insight into how a virus utilizes cellular pathways to facilitate its replication. IMPORTANCE: Infection with enterovirus 71 (EV71) often causes neurological diseases in children, and EV71 is responsible for the majority of fatalities. Based on a better understanding of interplay between virus and host cell, antiviral drugs against enteroviruses may be developed. As a dynamic cellular process of posttranslational modification, SUMOylation regulates global cellular protein localization, interaction, stability, and enzymatic activity. However, little is known concerning how SUMOylation directly influences virus replication by targeting viral polymerase. Here, we found that EV71 polymerase 3D was SUMOylated during EV71 infection and in vitro Moreover, the SUMOylation sites were determined, and in vitro polymerase assays indicated that mutations at SUMOylation sites could impair polymerase synthesis. Importantly, 3D is ubiquitinated in a SUMOylation-dependent manner that enhances the stability of the viral polymerase. Our findings indicate that the two modifications likely cooperatively enhance virus replication. Our study may offer a new therapeutic strategy against virus replication

Field-Induced Ferromagnetic Order and Colossal Magnetoresistance in La_{1.2}Sr_{1.8}Mn_2O_7: a ^{139}La NMR study

In order to gain insights into the origin of colossal magneto-resistance (CMR) in manganese oxides, we performed a ^{139}La NMR study in the double-layered compound La_{1.2}Sr_{1.8}Mn_2O_7. We find that above the Curie temperature T_C=126 K, applying a magnetic field induces a long-range ferromagnetic order that persists up to T=330 K. The critical field at which the induced magnetic moment is saturated coincides with the field at which the CMR effect reaches to a maximum. Our results therefore indicate that the CMR observed above T_C in this compound is due to the field-induced ferromagnetism that produces a metallic state via the double exchange interaction