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1
Proteolytic cleavage by the inner membrane peptidase (IMP) complex or Oct1 peptidase controls the localization of the yeast peroxiredoxin Prx1 to distinct mitochondrial compartments
Proteolytic cleavage by the inner membrane peptidase (IMP) complex or Oct1 peptidase controls the localization of the yeast peroxiredoxin Prx1 to distinct mitochondrial compartments
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Proteolytic cleavage by the inner membrane peptidase (IMP) complex or Oct1 peptidase controls the localization of the yeast peroxiredoxin Prx1 to distinct mitochondrial compartments

Fernando Gomes Flávio Romero Palma; Mário Henrique de Barros; Eduardo T Tsuchida; Helena G Turano; Thiago G. P Alegria; Marilene Demasi; Luis Eduardo Soares Netto

Journal of Biological Chemistry Bethesda v. 292, n. 41, p. 17011-17024, 2017

Bethesda 2017

Item não circula. Consulte sua biblioteca.(Acessar)

2
Calcium and magnesium ions modulate the oligomeric state and function of mitochondrial 2-Cys peroxiredoxins in Leishmania parasites
Calcium and magnesium ions modulate the oligomeric state and function of mitochondrial 2-Cys peroxiredoxins in Leishmania parasites
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Calcium and magnesium ions modulate the oligomeric state and function of mitochondrial 2-Cys peroxiredoxins in Leishmania parasites

Mariana A. B Morais Priscila O Giuseppe; Tatiana A. C. B Souza; Helena Castro; Rodrigo V Honorato; Paulo S. L Oliveira; Luis Eduardo Soares Netto; Ana M Tomas; Mário T Murakami

Journal of Biological Chemistry Bethesda v. 292, n. 17, p. 7023-7039, 2017

Bethesda 2017

Item não circula. Consulte sua biblioteca.(Acessar)

3
How pH modulates the dimer-decamer interconversion of 2-Cys peroxiredoxins from the Prx1 subfamily
How pH modulates the dimer-decamer interconversion of 2-Cys peroxiredoxins from the Prx1 subfamily
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How pH modulates the dimer-decamer interconversion of 2-Cys peroxiredoxins from the Prx1 subfamily

Mariana A. B Morais Priscila O Giuseppe; Tatiana Arruda Campos Brasil Souza; Thiago Gerônimo Pires Alegria; Marcos A Oliveira; Luis Eduardo Soares Netto; Mário Tyago Murakami

Journal of Biological Chemistry Bethesda v. 290, p. 8582-859, March 27, 2015

Bethesda 2015

Item não circula. Consulte sua biblioteca.(Acessar)

4
Coregulator Control of Androgen Receptor Action by a Novel Nuclear Receptor-binding Motif
Coregulator Control of Androgen Receptor Action by a Novel Nuclear Receptor-binding Motif
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Coregulator Control of Androgen Receptor Action by a Novel Nuclear Receptor-binding Motif

Jehle, Katja ; Cato, Laura ; Neeb, Antje ; Muhle-Goll, Claudia ; Jung, Nicole ; Smith, Emmanuel W. ; Buzon, Victor ; Carbó, Laia R. ; Estébanez-Perpiñá, Eva ; Schmitz, Katja ; Fruk, Ljiljana ; Luy, Burkhard ; Chen, Yu ; Cox, Marc B. ; Bräse, Stefan ; Brown, Myles ; Cato, Andrew C.B.

The Journal of biological chemistry, 2014-03, Vol.289 (13), p.8839-8851 [Periódico revisado por pares]

United States: Elsevier Inc

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5
Control of KirBac3.1 potassium channel gating at the interface between cytoplasmic domains
Control of KirBac3.1 potassium channel gating at the interface between cytoplasmic domains
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Control of KirBac3.1 potassium channel gating at the interface between cytoplasmic domains

Lejla Zubcevic Vassiliy N Bavro; João Renato Carvalho Muniz; Matthias R Schmidt; Shizhen Wang; Rita De Zorzi; Catherine Venien-Bryan; Mark S. P Sansom; Colin G Nichols; Stephen J Tucker

Journal of Biological Chemistry Bethesda : American Society of Biochemistry and Molecular Biology - ASBMB v. 289, n. 1, p. 143-151, Jan. 2014

Bethesda 2014

Localização: IFSC - Inst. Física de São Carlos    (PROD021663 )(Acessar)

6
Aspergillus niger β-glucosidase has a cellulase-like tadpole molecular shape insights into glycoside hydrolase family 3 (gh3) β-glucosidase structure and function
Aspergillus niger β-glucosidase has a cellulase-like tadpole molecular shape insights into glycoside hydrolase family 3 (gh3) β-glucosidase structure and function
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Aspergillus niger β-glucosidase has a cellulase-like tadpole molecular shape insights into glycoside hydrolase family 3 (gh3) β-glucosidase structure and function

Marisa A. Lima Mario Oliveira Neto; Marco Antonio S Kadowaki; Flavio R Rosseto; Erica T Prates; Fabio M Squina; Adriana F. P Leme; Munir S Skaf; Igor Polikarpov

Journal of Biological Chemistry Bethesda : American Society of Biochemistry and Molecular Biology - ASBMB v. 288, n. 46, p. 32991-33005, + supplemental Figs. S1 and S2 and Table S1, Nov. 2013

Bethesda 2013

Localização: IFSC - Inst. Física de São Carlos    (PROD021575 )(Acessar)

7
Characterization of heparin-induced glyceraldehyde 3-phosphate dehydrogenase early amyloid-like oligomers and their implication in `alfa´-synuclein aggregation
Characterization of heparin-induced glyceraldehyde 3-phosphate dehydrogenase early amyloid-like oligomers and their implication in `alfa´-synuclein aggregation
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Characterization of heparin-induced glyceraldehyde 3-phosphate dehydrogenase early amyloid-like oligomers and their implication in `alfa´-synuclein aggregation

Clarisa M Torres-Bugeau César L Ávila; R Raisman-Vozzari; Dulce Papy-Garcia; Rosangela Itri; Leandro Ramos Souza Barbosa; Leonardo M Cortez; Rosana N Chehín

Journal of Biological Chemistry Baltimore v. 287, n. 4, p. 2398–2409, 2012

Baltimore 2012

Acesso online

8
Urate as a physiological substrate for myeloperoxidase implications for hyperuricemia and inflammation
Urate as a physiological substrate for myeloperoxidase implications for hyperuricemia and inflammation
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Urate as a physiological substrate for myeloperoxidase implications for hyperuricemia and inflammation

Flavia Carla Meotti Guy N. L Jameson; Rufus Turner; D. Tim Harwood; Samantha Stockwell; Martin D Rees; Shane R Thomas; Anthony J Kettle

Journal of Biological Chemistry Bethesda v. 286, n. 15, p. 12901-12911, 2011

Bethesda 2011

Item não circula. Consulte sua biblioteca.(Acessar)

9
'CA POT. 2+' binding alters the interdomain flexibility between the two cytoplasmic calcium-binding domains in the 'NA POT. +'/'CA POT. 2+' exchanger
'CA POT. 2+' binding alters the interdomain flexibility between the two cytoplasmic calcium-binding domains in the 'NA POT. +'/'CA POT. 2+' exchanger
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'CA POT. 2+' binding alters the interdomain flexibility between the two cytoplasmic calcium-binding domains in the 'NA POT. +'/'CA POT. 2+' exchanger

Roberto Kopke Salinas Lei Bruschweiler Li; Eric Johnson; Rafael Brüschweiler

Journal of Biological Chemistry Bethesda v. 286, n. 37, p. 32123-32131 : + Supplementary materials (p. S1-S6), 2011

Bethesda 2011

Item não circula. Consulte sua biblioteca.(Acessar)

10
'CA POT. 2+' binding alters the interdomain flexibility between the two cytoplasmic calcium-binding domains in the 'NA POT. +'/'CA POT. 2+' exchanger
'CA POT. 2+' binding alters the interdomain flexibility between the two cytoplasmic calcium-binding domains in the 'NA POT. +'/'CA POT. 2+' exchanger
Material Type:
Artigo 		Adicionar ao Meu Espaço

'CA POT. 2+' binding alters the interdomain flexibility between the two cytoplasmic calcium-binding domains in the 'NA POT. +'/'CA POT. 2+' exchanger

Roberto Kopke Salinas Lei Bruschweiler Li; Eric Johnson; Rafael Brüschweiler

Journal of Biological Chemistry Bethesda v. 286, n. 37, p. 32123-32131 : + Supplementary materials (p. S1-S6), 2011

Bethesda 2011

Item não circula. Consulte sua biblioteca.(Acessar)

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Deste Autor:

  1. Augusto, O
  2. Reinach, F
  3. Farah, C
  4. Fischer, H
  5. Craievich, A

Neste Assunto:

  1. Bioquímica
  2. Cell Biology
  3. Biochemistry
  4. Molecular Biology
  5. Life Sciences & Biomedicine

  • Realização: ABCD-USP USP   Logos de Redes Sociais: Freepik

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