ORCID Profile
0000-0002-4696-461X
Current Organisations
Victoria University of Wellington
,
MZ Minerals Pty Ltd
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Publisher: Elsevier BV
Date: 03-2014
Publisher: Elsevier BV
Date: 06-2014
Publisher: Informa UK Limited
Date: 24-06-2021
Publisher: Elsevier BV
Date: 04-2009
Publisher: Elsevier BV
Date: 06-2015
Publisher: Elsevier BV
Date: 12-2009
Publisher: Elsevier BV
Date: 2015
Publisher: Elsevier BV
Date: 2012
Publisher: Public Library of Science (PLoS)
Date: 09-10-2018
Publisher: Elsevier BV
Date: 03-2015
Publisher: Elsevier BV
Date: 04-2022
Publisher: FapUNIFESP (SciELO)
Date: 06-2012
DOI: 10.1590/S0370-44672012000200017
Abstract: O objetivo desse trabalho é apresentar e discutir a determinação dos parâmetros de dispersão de ar em células mecânicas de flotação, em circuitos industriais brasileiros. Foram investigados os circuitos rougher e scavenger das usinas RPM, Taquari-Vassouras, Copebras e Fosfértil-Catalão (atual Vale Fertilizantes). Nas usinas RPM e Taquari-Vassouras, foram determinados a velocidade superficial do ar (Jg), o hold-up do ar (εg), o diâmetro médio de bolhas (d32) e o fluxo de área superficial de bolhas (Sb). Para as outras usinas, foram determinados somente o Jg e εg. Os resultados mostraram que, com exceção da RPM, todos os circuitos investigados apresentaram baixos valores para os parâmetros de dispersão do ar. Taquari-Vassouras apresentou os mais baixos valores médios para Jg e εg, respectivamente, 0,05 cm/s e 5%. Os maiores valores de Jg foram determinados no circuito rougher da Copebras, 1,17 cm/s, ao passo que a RPM apresentou os maiores valores para o hold-up e tamanho de bolha, respectivamente, 31% e 2,61mm. Os valores obtidos, para Sb, situaram-se abaixo daqueles reportados na literatura.
Publisher: Elsevier BV
Date: 12-2018
Publisher: Wiley
Date: 02-06-2020
Publisher: Elsevier BV
Date: 11-2023
Publisher: Elsevier BV
Date: 2011
Publisher: Elsevier BV
Date: 07-2018
Publisher: International Union of Crystallography (IUCr)
Date: 23-09-2017
DOI: 10.1107/S2053230X17013073
Abstract: Type II NADH:quinone oxidoreductase (NDH-2) is a respiratory enzyme found in the electron-transport chain of many species, with the exception of mammals. It is a 40–70 kDa single-subunit monotopic membrane protein that catalyses the oxidation of NADH and the reduction of quinone molecules via the cofactor FAD. NDH-2 is a promising new target for drug development given its essential role in many bacterial species and intracellular parasites. Only two bacterial NDH-2 structures have been reported and these structures are at moderate resolution (2.3–2.5 Å). In this communication, a new crystallization platform is reported that produced high-quality NDH-2 crystals that diffracted to high resolution (2.15 Å). The high-resolution NDH-2 structure was used for in silico quinone substrate-docking studies to investigate the binding poses of menadione and ubiquinone molecules. These studies revealed that a very limited number of molecular interactions occur at the quinone-binding site of NDH-2. Given that the conformation of the active site is well defined, this high-resolution structure is potentially suitable for in silico inhibitor-compound screening and ligand-docking applications.
Publisher: Elsevier BV
Date: 09-2013
Publisher: Elsevier BV
Date: 07-2013
Publisher: MDPI AG
Date: 14-10-2016
DOI: 10.3390/MIN6040105
Publisher: Elsevier BV
Date: 2015
Publisher: Elsevier BV
Date: 06-2019
Publisher: Elsevier BV
Date: 2024
Publisher: Elsevier BV
Date: 03-2022
Publisher: Elsevier BV
Date: 08-2021
Publisher: Elsevier BV
Date: 12-1997
Publisher: Elsevier BV
Date: 02-2019
Publisher: Elsevier BV
Date: 10-2019
Publisher: Elsevier BV
Date: 11-2019
Publisher: Elsevier BV
Date: 06-2022
Publisher: Elsevier BV
Date: 08-2013
Publisher: Elsevier BV
Date: 02-2015
Publisher: Elsevier BV
Date: 02-2009
Publisher: Elsevier BV
Date: 08-2021
Publisher: Elsevier BV
Date: 03-2011
Publisher: Elsevier BV
Date: 03-2021
Publisher: Elsevier BV
Date: 12-2015
Publisher: Elsevier BV
Date: 2014
Publisher: Elsevier BV
Date: 07-2012
Publisher: Elsevier BV
Date: 07-2012
Publisher: Elsevier BV
Date: 03-2011
Publisher: Elsevier BV
Date: 08-2021
Publisher: Elsevier BV
Date: 05-2015
Publisher: Elsevier BV
Date: 2021
Publisher: Elsevier BV
Date: 09-2021
Publisher: Elsevier BV
Date: 09-2021
Publisher: Elsevier BV
Date: 07-2015
Publisher: Elsevier BV
Date: 11-2014
Publisher: Elsevier BV
Date: 2012
Publisher: Informa UK Limited
Date: 2015
DOI: 10.15834/CIMJ.2015.3
Publisher: Elsevier BV
Date: 05-2022
Publisher: Wiley
Date: 29-04-2022
Abstract: Heparan sulfate (HS) is a highly sulfated natural carbohydrate that plays crucial roles in cancer, inflammation, and angiogenesis. Heparanase (HPSE) is the sole HS degrading endoglycosidase that cleaves HS at structure‐dependent sites along the polysaccharide chain. Overexpression of HPSE by cancer cells correlates with increased tumor size and enhanced metastasis. Previously we have shown that a tetramer HS mimetic is a potent HPSE inhibitor displaying remarkable anticancer activity in vivo . Building on that work, we report the synthesis and testing of a novel library of single entity trimer glycolipid mimetics that effectively inhibit HPSE at low nanomolar concentrations. A lipophilic arm was introduced to assess whether an improvement of pharmacokinetics and plasma residence time would offset the reduction in charge and multivalency. Preclinical tests in a mouse syngeneic model showed effective tumor growth inhibition by the tetramer but not the trimer glycomimetic.
Publisher: Elsevier BV
Date: 06-2000
Publisher: Informa UK Limited
Date: 06-06-2021
Publisher: Informa UK Limited
Date: 10-2013
Publisher: Elsevier BV
Date: 08-2013
Publisher: Elsevier BV
Date: 02-2015
Publisher: Elsevier BV
Date: 02-2022
No related grants have been discovered for Massimiliano Zanin.