Leonardo de Castro Palmieri

Instituição:

Universidade Federal do Rio de Janeiro

Centro:

Campus de Xerém

Unidade:

Campus de Xerém

Departamento:

Direção Geral do Campus de Xerém

ORCID:

não disponível no Lattes


Formação:

  • Faculdade de Farmácia - UFRJ

    | Pós-Doutorado | 2010 - Agora

  • Universidade Federal do Rio de Janeiro

    | Pós-Doutorado | 2009 - 2010

  • Universidade Federal do Rio de Janeiro

    Química Biológica | Doutorado | 2005 - 2009

  • Universidade Federal do Rio de Janeiro

    Química Biológica | Mestrado | 2003 - 2005

  • Universidade Federal do Estado do Rio de Janeiro

    Biomedicina | Graduação | 1999 - 2003
Laboratórios:
Nenhum laboratório cadastrado
Nuvens de Palavras:
Artigos:

(100.00% artigos com DOI)

Titulo DOI Ano
Polymorphic distribution of proteins in solution by mass spectrometry: The analysis of insulin analogues 10.1016/j.biologicals.2016.09.011 2016
Assignment of polymorphic species of insulin analogues in ion mobility mass spectroscopy 10.1016/j.dib.2016.12.020 2016
Regulation of the assembly and amyloid aggregation of murine amylin by zinc 10.1016/j.bpc.2016.09.008 2016
A T3R3 hexamer of the human insulin variant B28Asp 10.1016/j.bpc.2013.01.003 2013
Structural meta-analysis of regular human insulin in pharmaceutical formulations 10.1016/j.ejpb.2013.05.005 2013
Stepwise oligomerization of murine amylin and assembly of amyloid fibrils 10.1016/j.bpc.2013.07.013 2013
Structure and Behavior of Human α-Thrombin upon Ligand Recognition: Thermodynamic and Molecular Dynamics Studies 10.1371/journal.pone.0024735 2011
Identification of a novel ligand binding motif in the transthyretin channel 10.1016/j.bmc.2009.11.025 2010
Novel Zn2+-binding Sites in Human Transthyretin: IMPLICATIONS FOR AMYLOIDOGENESIS AND RETINOL-BINDING PROTEIN RECOGNITION 10.1074/jbc.m110.157206 2010
Conformational differences between the wild type and V30M mutant transthyretin modulate its binding to genistein: Implications to tetramer stability and ligand-binding 10.1016/j.jsb.2010.03.002 2010
Hydration and Packing are Crucial to Amyloidogenesis as Revealed by Pressure Studies on Transthyretin Variants that Either Protect or Worsen Amyloid Disease 10.1016/S0022-2836(03)00368-1 2003
Dissociation of amyloid fibrils of a-synuclein and transthyretin by pressure reveals their reversible nature and the formation of water-excluded cavities 10.1073/pnas.1734009100 2003
Eventos:

(0.00% eventos com DOI)

Titulo DOI Ano
Structural alterations in the most unstable transthyretin tetramer favor its aggregation in physiological conditions 2011
Folding and stability studies of wild type (WT) and mutant transthyretin using pressure-induced denaturation: Implications for aggregation. 2001
Publicações:
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