Author

Fernando Pavão

Observed names: F. Pavao, F. Pavão, Pavão, Fernando

Observed institutions: Centre National de la Recherche Scientifique, Université Toulouse III - Paul Sabatier, Universidade de São Paulo, Instituto de Química de São Carlos, Synthèse et Physicochimie de Molécules d'Intérêt Biologique, Instituto de Física de São Carlos

ORCID: 0000-0001-8002-0834

Observed ORCID: 0000-0001-8002-0834

OpenAlex ID: A5043083866

Structure of Trypanosoma cruzi glycosomal glyceraldehyde‐3‐phosphate dehydrogenase complexed with chalepin, a natural product inhibitor, at 1.95 Å resolution

2002 · F. Pavão, M.S. Castilho, et al. · FEBS Letters · 77

Strategies for the isolation and identification of trypanocidal compounds from the Rutales

2001 · Paulo C. Vieira, Jair Mafezoli, et al. · Pure and Applied Chemistry · 51

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Evidence for the Two Phosphate Binding Sites of an Analogue of the Thioacyl Intermediate for theTrypanosoma cruziGlyceraldehyde-3-phosphate Dehydrogenase-Catalyzed Reaction, from Its Crystal Structure

2003 · Marcelo S. Castilho, Fernando Pavão, et al. · Biochemistry · 40

3D QSAR studies on binding affinities of coumarin natural products for glycosomal GAPDH of Trypanosoma cruzi

2003 · Irwin R.A. Menezes, Julio C.D. Lopes, et al. · Journal of Computer-Aided Molecular Design · 39

Synthesis of acylated nucleosides and ribonic-1,4-lactones as inhibitors of trypanosomal glyceraldehyde-3-phosphate dehydrogenase (gGAPDH)

2002 · Marcus M. Sá, Gustavo P. Silveira, et al. · ARKIVOC · 6

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The use of molecular modelling in the understanding of configurational specificity (R or S) in asymmetric reactions catalyzed by Saccharomyces cerevisiae or isolated dehydrogenases

1998 · Ricardo de Souza Pereira, Fernando Pavão, et al. · Molecular and Cellular Biochemistry · 2

Structure of Glycosomal Glyceraldehyde-3-Phosphate Dehydrogenase from Trypanosoma cruzi Complexed with Chalepin, a Coumarin Derivative Inhibitor

2001 · F. Pavao · Worldwide Protein Data Bank · 1

As características anti-imperiais da mensagem de Paulo em Filipenses 3.20-21

2020 · Fernando Pavão, Flávio Schmitt · Reflexus

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Evidences for a flip-flop catalytic mechanism of Trypanosoma cruzi glyceraldehyde-3-phosphate dehydrogenase, from its crystal structure in complex with reacted irreversible inhibitor 2-(2-phosphono-ethyl)-acrylic acid 4-nitro-phenyl ester

2002 · M.S. Castilho, F. Pavao, et al. · Worldwide Protein Data Bank

Estudos cristalográficos e planejamento racional de inibidores específicos da enzima gliceraldeído-3-fosfato desidrogenase glicossomal (gGAPDH) de Trypanosoma cruzi

2001 · Fernando Pavão

Natural products in structure-based drug discovery: coumarin derivatives as specific trypanosomal inhibitors

2000 · Fernando Pavão, Marcelo Santos Castilho, et al.

Structure-based design of specific inhibitors of the glycosomal glyceraldehyde-3-phosphate dehidrogenase from Trypanosoma cruzi

2000 · Fernando Pavão, Marcelo Santos Castilho, et al.

Structure of APO T.cruzi glyceraldehyde-3-phosphate dehydrogenase: implications for drug design

1999 · Glaucius Oliva, B.G. Guimarães, et al. · Abstracts

Drogas antichagásicas tendo como alvo a enzima Gliceraldeído-3-fosfato Desidrogenase (GAPDH) de Trypanosoma cruzi - complexo GAPDH-chalepina

1999 · Fernando Pavão, Maria Cristina Nonato, et al. · Programa e resumos

Desenvolvimento de novas drogas anti-chagásicas: síntese de potenciais inibidores de gliceraldeído-3-fosfato desidrogenase (gGAPDH)

1998 · Glaucius Oliva, Fernando Pavão, et al. · Livro de Resumos

Structure-based design and biodiversity in the search for new antichagasic drugs

1998 · Glaucius Oliva, Dulce H F Souza, et al.

Desenho racional de inibidores da enzima gliceraldeído-3-fosfato desidrogenase glicossomal (gGAPDH) de Trypanosoma cruzi - agente causador da doença de Chagas

1996 · Fernando Pavão

Rational design of inhibitors of glyceraldehyde-3-phosphate dehydrogenase (gGAPDH) from Trypanosoma cruzi - causative agent of Chagas disease

1996 · Pavão, Fernando · LA Referencia (Red Federada de Repositorios Institucionales de Publicaciones Científicas)

Works count: 18

Citation count: 216

H-index: 5

I10-index: 4