New Approaches to Exciting Exergame-Experiences for People with Motor Function Impairments

Eckert, M.; Gómez-Martinho, I.; Meneses, J.; Martínez, J.-F.; Sensors 2017, 17, 354. doi:10.3390/s17020354             
OPEN ACCESS

The work presented here suggests new ways to tackle exergames for physical rehabilitation and to improve the players’ immersion and involvement. The primary (but not exclusive) purpose is to increase the motivation of children and adolescents with severe physical impairments, for doing their required exercises while playing. The proposed gaming environment is based on the Kinect sensor and the Blender Game Engine. A middleware has been implemented that efficiently transmits the data from the sensor to the game. Inside the game, different newly proposed mechanisms have been developed to distinguish pure exercise-gestures from other movements used to control the game (e.g., opening a menu). The main contribution is the amplification of weak movements, which allows the physically impaired to have similar gaming experiences as the average population. To test the feasibility of the proposed methods, four mini-games were implemented and tested by a group of 11 volunteers with different disabilities, most of them bound to a wheelchair. Their performance has also been compared to that of a healthy control group. Results are generally positive and motivating, although there is much to do to improve the functionalities. There is a major demand for applications that help to include disabled people in society and to improve their life conditions. This work will contribute towards providing them with more fun during exercise.

ISCU(M108I) and ISCU(D39V) differ from wild type ISCU in their failure to form cysteine desulfurase complexes containing both frataxin and ferredoxin

Kai Cai, Ronnie O. Frederick, Marco Tonelli, and John L. Markley; Biochemistry, Just Accepted Manuscript DOI: 10.1021/acs.biochem.7b01234

Whereas iron-sulfur (Fe-S) cluster assembly on the wild-type scaffold protein ISCU, as catalyzed by the human cysteine desulfurase complex (SDA), exhibits a requirement for frataxin (FXN), assembly on variant ISCU(M108I) has been shown to bypass the FXN requirement. Wild-type ISCU populates two interconverting conformational states: one structured and one dynamically disordered. We show here that ISCU(M108I) populates only the structured state as does another variant ISCU(D39V). We have compared the properties ISCU, ISCU(M108I), and ISCU(D39V), with and without FXN, in both the cysteine desulfurase step of Fe-S cluster assembly and in the overall Fe-S cluster assembly reaction. In the cysteine desulfurase step with DTT as the reductant, FXN was found to stimulate cluster assembly with both the wild-type and structured variants, although the effect was less prominent with ISCU(D39V) than with wild-type or ISCU(M108I). In overall Fe-S cluster assembly, frataxin was found to stimulate cluster assembly with both the wild-type and structured variants when the reductant was DTT; however, with the physiological reductant, reduced ferredoxin 2 (rdFDX2), frataxin stimulated the reaction with wild-type ISCU but not with the fully-structured variants. Through NMR titration experiments, we discovered that, wild-type ISCU, frataxin, and rdFDX2 all bind to SDA. However, when ISCU was replaced by the fully-structured variant ISCU(M108I), the addition of rdFDX2 to the SDA-ISCU(M108I)-FXN complex led to the release of FXN. Thus, the displacement of FXN by rdFDX2 explains the failure of FXN to stimulate Fe-S cluster assembly on ISCU(M108I).