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1
Structural basis for the function and inhibition of dihydroorotate dehydrogenase from Schistosoma mansoni
Structural basis for the function and inhibition of dihydroorotate dehydrogenase from Schistosoma mansoni
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Structural basis for the function and inhibition of dihydroorotate dehydrogenase from Schistosoma mansoni

Renan Minin de Mori Mariana Araújo Ajalla Aleixo; Luana Carlos Campisano Zapata; Felipe A Calil; Flavio da Silva Emery; Maria Cristina Nonato

The FEBS Journal West Sussex v. 288, n. 3, p. 930-944, 2021

West Sussex 2021

Localização: FCFRP - Fac. Ciên. Farm. Ribeirão Preto    (pcd 3130256 Acervo Digital )(Acessar)

2
Tolcapone, a potent aggregation inhibitor for the treatment of familial leptomeningeal amyloidosis
Tolcapone, a potent aggregation inhibitor for the treatment of familial leptomeningeal amyloidosis
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Tolcapone, a potent aggregation inhibitor for the treatment of familial leptomeningeal amyloidosis

Pinheiro, Francisca ; Varejão, Nathalia ; Esperante, Sebastian ; Santos, Jaime ; Velázquez‐Campoy, Adrián ; Reverter, David ; Pallarès, Irantzu ; Ventura, Salvador

The FEBS journal, 2021-01, Vol.288 (1), p.310-324 [Periódico revisado por pares]

England: Blackwell Publishing Ltd

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3
Structural insights into the multiple binding modes of Dimethyl Fumarate (DMF) and its analogs to the Kelch domain of Keap1
Structural insights into the multiple binding modes of Dimethyl Fumarate (DMF) and its analogs to the Kelch domain of Keap1
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Structural insights into the multiple binding modes of Dimethyl Fumarate (DMF) and its analogs to the Kelch domain of Keap1

Unni, Sruthi ; Deshmukh, Prashant ; Krishnappa, Gopinatha ; Kommu, Padmini ; Padmanabhan, Balasundaram

The FEBS journal, 2021-03, Vol.288 (5), p.1599-1613 [Periódico revisado por pares]

England: Blackwell Publishing Ltd

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4
Crystal structure of Mycobacterium tuberculosis ketol‐acid reductoisomerase at 1.0 Å resolution – a potential target for anti‐tuberculosis drug discovery
Crystal structure of Mycobacterium tuberculosis ketol‐acid reductoisomerase at 1.0 Å resolution – a potential target for anti‐tuberculosis drug discovery
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Crystal structure of Mycobacterium tuberculosis ketol‐acid reductoisomerase at 1.0 Å resolution – a potential target for anti‐tuberculosis drug discovery

Lv, You ; Kandale, Ajit ; Wun, Shun Jie ; McGeary, Ross P. ; Williams, Simon J. ; Kobe, Bostjan ; Sieber, Volker ; Schembri, Mark A. ; Schenk, Gerhard ; Guddat, Luke W.

The FEBS journal, 2016-04, Vol.283 (7), p.1184-1196 [Periódico revisado por pares]

England: Blackwell Publishing Ltd

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5
Comparative study of two GH19 chitinase‐like proteins from Hevea brasiliensis, one exhibiting a novel carbohydrate‐binding domain
Comparative study of two GH19 chitinase‐like proteins from Hevea brasiliensis, one exhibiting a novel carbohydrate‐binding domain
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Comparative study of two GH19 chitinase‐like proteins from Hevea brasiliensis, one exhibiting a novel carbohydrate‐binding domain

Martínez‐Caballero, Siseth ; Cano‐Sánchez, Patricia ; Mares‐Mejía, Israel ; Díaz‐Sánchez, Angel G. ; Macías‐Rubalcava, Martha L. ; Hermoso, Juan A. ; Rodríguez‐Romero, Adela

The FEBS journal, 2014-10, Vol.281 (19), p.4535-4554 [Periódico revisado por pares]

England: Blackwell Publishing Ltd

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6
Crystal structure of mouse mu‐crystallin complexed with NADPH and the T3 thyroid hormone
Crystal structure of mouse mu‐crystallin complexed with NADPH and the T3 thyroid hormone
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Crystal structure of mouse mu‐crystallin complexed with NADPH and the T3 thyroid hormone

Borel, Franck ; Hachi, Isma ; Palencia, Andres ; Gaillard, Marie‐Claude ; Ferrer, Jean‐Luc

The FEBS journal, 2014-03, Vol.281 (6), p.1598-1612 [Periódico revisado por pares]

England: Blackwell Publishing Ltd

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7
Crystal structure of yeast xylose reductase in complex with a novel NADP‐DTT adduct provides insights into substrate recognition and catalysis
Crystal structure of yeast xylose reductase in complex with a novel NADP‐DTT adduct provides insights into substrate recognition and catalysis
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Crystal structure of yeast xylose reductase in complex with a novel NADP‐DTT adduct provides insights into substrate recognition and catalysis

Paidimuddala, Bhaskar ; Mohapatra, Samar B. ; Gummadi, Sathyanarayana N. ; Manoj, Narayanan

The FEBS journal, 2018-12, Vol.285 (23), p.4445-4464 [Periódico revisado por pares]

England: Blackwell Publishing Ltd

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8
Correcting the record of structural publications requires joint effort of the community and journal editors
Correcting the record of structural publications requires joint effort of the community and journal editors
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Correcting the record of structural publications requires joint effort of the community and journal editors

Rupp, Bernhard ; Wlodawer, Alexander ; Minor, Wladek ; Helliwell, John R. ; Jaskolski, Mariusz

The FEBS journal, 2016-12, Vol.283 (24), p.4452-4457 [Periódico revisado por pares]

England: Blackwell Publishing Ltd

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9
Structural basis for substrate recognition by Erwinia chrysanthemi GH30 glucuronoxylanase
Structural basis for substrate recognition by Erwinia chrysanthemi GH30 glucuronoxylanase
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Structural basis for substrate recognition by Erwinia chrysanthemi GH30 glucuronoxylanase

Urbániková, Ľubica ; Vršanská, Mária ; Mørkeberg Krogh, Kristian B.R ; Hoff, Tine ; Biely, Peter

The FEBS journal, 2011-06, Vol.278 (12), p.2105-2116 [Periódico revisado por pares]

Oxford, UK: Blackwell Publishing Ltd

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10
Evidence that phosphorylation of threonine in the GT motif triggers activation of PknA, a eukaryotic‐type serine/threonine kinase from Mycobacterium tuberculosis
Evidence that phosphorylation of threonine in the GT motif triggers activation of PknA, a eukaryotic‐type serine/threonine kinase from Mycobacterium tuberculosis
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Evidence that phosphorylation of threonine in the GT motif triggers activation of PknA, a eukaryotic‐type serine/threonine kinase from Mycobacterium tuberculosis

Ravala, Sandeep K ; Singh, Suruchi ; Yadav, Ghanshyam S ; Kumar, Sanjay ; Karthikeyan, Subramanian ; Chakraborti, Pradip K

The FEBS journal, 2015-04, Vol.282 (8), p.1419-1431 [Periódico revisado por pares]

England: Published by Blackwell Pub. on behalf of the Federation of European Biochemical Societies

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