A
Alessandro Paiardini
Researcher at Sapienza University of Rome
Publications - 126
Citations - 3190
Alessandro Paiardini is an academic researcher from Sapienza University of Rome. The author has contributed to research in topics: Serine hydroxymethyltransferase & Active site. The author has an hindex of 29, co-authored 108 publications receiving 2452 citations.
Papers
More filters
Journal ArticleDOI
PyMod 2.0: improvements in protein sequence-structure analysis and homology modeling within PyMOL
TL;DR: A number of new MODELLER functionalities have also been implemented, including SALIGN, modeling of quaternary structures, DOPE scores, disulfide bond modeling and choice of heteroatoms to be included in the final model.
Journal ArticleDOI
Structural adaptation of extreme halophilic proteins through decrease of conserved hydrophobic contact surface
TL;DR: The results suggest that haloadaptation strategy in the presence of molar salt concentration, but not of osmolytes, necessitates a weakening of the hydrophobic interactions, in particular at the level of conservedHydrophobic contacts.
Journal ArticleDOI
PyMod: sequence similarity searches, multiple sequence-structure alignments, and homology modeling within PyMOL
TL;DR: A simple and intuitive interface, PyMod has been developed, to show how the integration of the individual steps required for homology modeling and sequence/structure analysis within the PyMOL framework can hugely simplify these tasks.
Journal ArticleDOI
Glucose Metabolism in the Progression of Prostate Cancer.
Francesca Cutruzzolà,Giorgio Giardina,Marina Marani,Alberto Macone,Alessandro Paiardini,Serena Rinaldo,Alessio Paone +6 more
TL;DR: The metabolic transformations occurring in the prostate from the normal cell to the metastasis are recapitulate, highlighting the role of the microenvironment and summarizing what is known on the molecular mechanisms involved in the process.
Journal ArticleDOI
Open conformation of human DOPA decarboxylase reveals the mechanism of PLP addition to Group II decarboxylases
Giorgio Giardina,Riccardo Montioli,Stefano Gianni,Barbara Cellini,Alessandro Paiardini,Carla Borri Voltattorni,Francesca Cutruzzolà +6 more
TL;DR: Analysis of three-dimensional data coupled to a kinetic study allows to identify the structural determinants of the open/close conformational change occurring upon PLP binding and thereby propose a model for the preferential degradation of the apoenzymes of Group II decarboxylases.