A
A. De Santis
Researcher at University of Naples Federico II
Publications - 13
Citations - 501
A. De Santis is an academic researcher from University of Naples Federico II. The author has contributed to research in topics: Inverse kinematics & Robot. The author has an hindex of 8, co-authored 13 publications receiving 480 citations.
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Proceedings ArticleDOI
Safe and Dependable Physical Human-Robot Interaction in Anthropic Domains: State of the Art and Challenges
Rachid Alami,A. Albu-Schaeffer,Antonio Bicchi,Rainer Bischoff,Raja Chatila,A. De Luca,A. De Santis,Georges Giralt,Jérémie Guiochet,Gerd Hirzinger,Félix Ingrand,Vincenzo Lippiello,R. Mattone,David Powell,Soumen Sen,Bruno Siciliano,G. Tonietti,Luigi Villani +17 more
TL;DR: The state of the art in the field as surveyed by the PHRIDOM project is presented, as well as it enlightens a number of challenges that will be undertaken within the PHRIENDS project.
Journal ArticleDOI
Transglutaminase-mediated modifications of the rat sperm surface in vitro
TL;DR: Two transglutaminase-mediated modifications of the rat epididymal spermatozoon surface were demonstrated in vitro and a specific physiological role for the enzyme, bringing about modifications ofThe rat sperm surface in the seminal fluid environment, is suggested.
Proceedings ArticleDOI
The skeleton algorithm for self-collision avoidance of a humanoid manipulator
TL;DR: A robust reactive algorithm, named the "skeleton algorithm", is proposed for the real-time generation of self-collision avoidance motions, where only proprioceptive sensory data are needed.
Journal ArticleDOI
Sperm maturation in human semen: role of transglutaminase-mediated reactions.
Raffaele Porta,Cinzia Esposito,A. De Santis,Alfredo Fusco,Michelangelo Iannone,Salvatore Metafora +5 more
TL;DR: Evidence is reported of the ability of several seminal plasma proteins to act as acyl donor substrates for endogenous transglutaminase, whereas human ejaculated spermatozoa have been shown to possess polyamine-binding sites specifically involved in transglUTaminase-catalyzed reactions.