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1
Crystal structure of a soluble decoy receptor IL-22BP bound to interleukin-22
Crystal structure of a soluble decoy receptor IL-22BP bound to interleukin-22
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Crystal structure of a soluble decoy receptor IL-22BP bound to interleukin-22

Patricia Ribeiro Moura Leandra Watanabe; Lucas Bleicher; Didier Colau; Laure Dumoutier; Muriel M Lemaire; Jean Christophe Renauld; Igor Polikarpov

FEBS Letters Amsterdam v. 583, n. 7, p. 1072-1077, Apr. 2009

Amsterdam 2009

Localização: IFSC - Inst. Física de São Carlos    (PROD015774 )(Acessar)

2
Crystal structure of a soluble decoy receptor IL-22BP bound to interleukin-22
Crystal structure of a soluble decoy receptor IL-22BP bound to interleukin-22
Material Type:
Artigo 		Adicionar ao Meu Espaço

Crystal structure of a soluble decoy receptor IL-22BP bound to interleukin-22

Patricia Ribeiro Moura Leandra Watanabe; Lucas Bleicher; Didier Colau; Laure Dumoutier; Muriel M Lemaire; Jean Christophe Renauld; Igor Polikarpov

FEBS Letters Amsterdam v. 583, n. 7, p. 1072-1077, Apr. 2009

Amsterdam 2009

Localização: IFSC - Inst. Física de São Carlos    (PROD015774 )(Acessar)

3
Crystal structure of a soluble decoy receptor IL-22BP bound to interleukin-22
Crystal structure of a soluble decoy receptor IL-22BP bound to interleukin-22
Material Type:
Artigo 		Adicionar ao Meu Espaço

Crystal structure of a soluble decoy receptor IL-22BP bound to interleukin-22

de Moura, Patricia Ribeiro ; Watanabe, Leandra ; Bleicher, Lucas ; Colau, Didier ; Dumoutier, Laure ; Lemaire, Muriel M. ; Renauld, Jean-Christophe ; Polikarpov, Igor

FEBS letters, 2009-04, Vol.583 (7), p.1072-1077 [Periódico revisado por pares]

England: Elsevier B.V

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4
Is the cytoplasmic loop of MerT, the mercuric ion transport protein, involved in mercury transfer to the mercuric reductase?
Is the cytoplasmic loop of MerT, the mercuric ion transport protein, involved in mercury transfer to the mercuric reductase?
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Is the cytoplasmic loop of MerT, the mercuric ion transport protein, involved in mercury transfer to the mercuric reductase?

Rossy, Emmanuel ; Sénèque, Olivier ; Lascoux, David ; Lemaire, David ; Crouzy, Serge ; Delangle, Pascale ; Covès, Jacques

FEBS letters, 2004-09, Vol.575 (1), p.86-90 [Periódico revisado por pares]

England: Elsevier B.V

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5
Cysteine-153 is required for redox regulation of pea chloroplast fructose-1,6-bisphosphatase
Cysteine-153 is required for redox regulation of pea chloroplast fructose-1,6-bisphosphatase
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Cysteine-153 is required for redox regulation of pea chloroplast fructose-1,6-bisphosphatase

Jacquot, Jean-Pierre ; Lopez-Jaramillo, Javier ; Miginiac-Maslow, Myroslawa ; Lemaire, Stéphane ; Cherfils, Jacqueline ; Chueca, Ana ; Lopez-Gorge, Julio

FEBS letters, 1997-01, Vol.401 (2), p.143-147 [Periódico revisado por pares]

England: Elsevier B.V

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6
The internal Cys-207 of sorghum leaf NADP-malate dehydrogenase can form mixed disulphides with thioredoxin
The internal Cys-207 of sorghum leaf NADP-malate dehydrogenase can form mixed disulphides with thioredoxin
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The internal Cys-207 of sorghum leaf NADP-malate dehydrogenase can form mixed disulphides with thioredoxin

Goyer, Aymeric ; Decottignies, Paulette ; Lemaire, Stephane ; Ruelland, Eric ; Issakidis-Bourguet, Emmanuelle ; Jacquot, Jean-Pierre ; Miginiac-Maslow, Myroslawa

FEBS letters, 1999-02, Vol.444 (2), p.165-169 [Periódico revisado por pares]

England: Elsevier B.V

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7
Inhibition of Bcl-2-dependent cell survival by a caspase inhibitor: a possible new pathway for Bcl-2 to regulate cell death
Inhibition of Bcl-2-dependent cell survival by a caspase inhibitor: a possible new pathway for Bcl-2 to regulate cell death
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Inhibition of Bcl-2-dependent cell survival by a caspase inhibitor: a possible new pathway for Bcl-2 to regulate cell death

Rincheval, V ; Renaud, F ; Lemaire, C ; Mignotte, B ; Vayssière, J.L

FEBS letters, 1999-10, Vol.460 (2), p.203-206 [Periódico revisado por pares]

England: Elsevier B.V

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8
Direct evidence for the different roles of the N- and C-terminal regulatory disulfides of sorghum leaf NADP-malate dehydrogenase in its activation by reduced thioredoxin
Direct evidence for the different roles of the N- and C-terminal regulatory disulfides of sorghum leaf NADP-malate dehydrogenase in its activation by reduced thioredoxin
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Direct evidence for the different roles of the N- and C-terminal regulatory disulfides of sorghum leaf NADP-malate dehydrogenase in its activation by reduced thioredoxin

Issakidis, Emmanuelle ; Lemaire, Martine ; Decottignies, Paulette ; Jacquot, Jean-Pierre ; Miginiac-Maslow, Myroslawa

FEBS letters, 1996-08, Vol.392 (2), p.121-124 [Periódico revisado por pares]

England: Elsevier B.V

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9
Expression of the sarcoplasmic reticulum Ca2+‐ATPase in yeast
Expression of the sarcoplasmic reticulum Ca2+‐ATPase in yeast
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Expression of the sarcoplasmic reticulum Ca2+‐ATPase in yeast

Centeno, Francisco ; Deschamps, Stéphane ; Lompré, Anne-Marie ; Anger, Marielle ; Moutin, Marie-Jo ; Dupont, Yves ; Palmgren, Michael Gjedde ; Villalba, Jose Manuel ; Møller, Jesper Vuust ; Falson, Pierre ; le Maire, Marc

FEBS letters, 1994-10, Vol.354 (1), p.117-122 [Periódico revisado por pares]

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10
mRNP3 and mRNP4 are phosphorylatable by casein kinase II in Xenopus oocytes, but phosphorylation does not modify RNA-binding affinity
mRNP3 and mRNP4 are phosphorylatable by casein kinase II in Xenopus oocytes, but phosphorylation does not modify RNA-binding affinity
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mRNP3 and mRNP4 are phosphorylatable by casein kinase II in Xenopus oocytes, but phosphorylation does not modify RNA-binding affinity

Deschamps, Stéphane ; Jacquemin-Sablon, Hélène ; Triqueneaux, Gérard ; Mulner-Lorillon, Odile ; Potier, Michel ; Le Caer, Jean-Pierre ; Dautry, François ; le Maire, Marc

FEBS letters, 1997-08, Vol.412 (3), p.495-500 [Periódico revisado por pares]

England: Elsevier B.V

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Deste Autor:

  1. Colau, D
  2. Watanabe, L
  3. Lemaire, M
  4. Polikarpov, I
  5. Dumoutier, L

Neste Assunto:

  1. Cell Biology
  2. Biophysics
  3. Biochemistry & Molecular Biology
  4. Life Sciences & Biomedicine
  5. Science & Technology

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

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