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11
DNA converts cellular prion protein into the beta-sheet conformation and inhibits prion peptide aggregation
DNA converts cellular prion protein into the beta-sheet conformation and inhibits prion peptide aggregation
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DNA converts cellular prion protein into the beta-sheet conformation and inhibits prion peptide aggregation

Yraima Cordeiro Filipe Machado; Luiz Juliano; Maria Aparecida Juliano; Débora Foguel; Jerson L Silva; Ricardo R Brentani

The Journal of Biological Chemistry Bethesda v. 276, n. 52, p. 49400-49409, December, 2002

Bethesda 2002

Item não circula. Consulte sua biblioteca.(Acessar)

12
Identification of a novel ligand binding motif in the transthyretin channel
Identification of a novel ligand binding motif in the transthyretin channel
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Identification of a novel ligand binding motif in the transthyretin channel

Luis Mauricio T. R. Lima Vivian de Almeida Silva; Leonardo de Castro Palmieri; Maria Clara B. R Oliveira; Débora Foguel; Igor Polikarpov

Bioorganic and Medicinal Chemistry Oxford : Pergamon v. 18, n. 1, p. 100-110, Jan. 2010

Oxford 2010

Localização: IFSC - Inst. Física de São Carlos    (PROD016743 )(Acessar)

13
An intermediate structure in the thermal unfolding of the GTPase domain of human septin 4 (SEPT4/Bradeion-'beta') forms amyloid-like filaments in vitro
An intermediate structure in the thermal unfolding of the GTPase domain of human septin 4 (SEPT4/Bradeion-'beta') forms amyloid-like filaments in vitro
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An intermediate structure in the thermal unfolding of the GTPase domain of human septin 4 (SEPT4/Bradeion-'beta') forms amyloid-like filaments in vitro

Wanius Garcia Ana Paula Ulian de Araújo; Flávio Lara; Débora Foguel; Manami Tanaka; Tomoo Tanaka; Richard Charles Garratt

Biochemistry Washington v. 46, n. 39, p. 11101-11109, Oct. 2007

Washington 2007

Localização: IFSC - Inst. Física de São Carlos    (PROD013876 )(Acessar)

14
Novel 'Zn IND.2+'-binding sites in human transthyretin implications for amyloidogenesis and retinol binding protein recognition
Novel 'Zn IND.2+'-binding sites in human transthyretin implications for amyloidogenesis and retinol binding protein recognition
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Novel 'Zn IND.2+'-binding sites in human transthyretin implications for amyloidogenesis and retinol binding protein recognition

Leonardo C. Palmieri Luis Mauricio T. R Lima; Juliana B. B Freire; Lucas Bleicher; Igor Polikarpov; Fabio C. L Almeida; Débora Foguel

Journal of Biological Chemistry Bethesda : American Society of Biochemistry and Molecular Biology v. 285, n. 41, p. 31731-31741, Oct. 2010

Bethesda 2010

Localização: IFSC - Inst. Física de São Carlos    (PROD017451 )(Acessar)

15
Dissecting the structure, thermodynamic stability, and aggregation properties of the A25T transthyretin (A25T-TTR) variant involved in leptomeningeal amyloidosis identifying protein partners that co-aggregate during A25T-TTR fibrillogenesis in cerebrospinal fluid
Dissecting the structure, thermodynamic stability, and aggregation properties of the A25T transthyretin (A25T-TTR) variant involved in leptomeningeal amyloidosis identifying protein partners that co-aggregate during A25T-TTR fibrillogenesis in cerebrospinal fluid
Material Type:
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Dissecting the structure, thermodynamic stability, and aggregation properties of the A25T transthyretin (A25T-TTR) variant involved in leptomeningeal amyloidosis identifying protein partners that co-aggregate during A25T-TTR fibrillogenesis in cerebrospinal fluid

Estefania P. C. Azevedo Humberto D'Muniz Pereira; Richard Charles Garratt; Jeffery W Kelly; Debora Foguel; Fernando L Palhano

Biochemistry Washington, DC : American Chemical Society - ACS v. 50, n. 51, p. 11070-11083, Dec. 2011

Washington, DC 2011

Localização: IFSC - Inst. Física de São Carlos    (PROD019201 )(Acessar)

16
An intermediate structure in the thermal unfolding of the GTPase domain of human septin 4 (SEPT4/Bradeion-'beta') forms amyloid-like filaments in vitro
An intermediate structure in the thermal unfolding of the GTPase domain of human septin 4 (SEPT4/Bradeion-'beta') forms amyloid-like filaments in vitro
Material Type:
Artigo 		Adicionar ao Meu Espaço

An intermediate structure in the thermal unfolding of the GTPase domain of human septin 4 (SEPT4/Bradeion-'beta') forms amyloid-like filaments in vitro

Wanius Garcia Ana Paula Ulian de Araújo; Flávio Lara; Débora Foguel; Manami Tanaka; Tomoo Tanaka; Richard Charles Garratt

Biochemistry Washington v. 46, n. 39, p. 11101-11109, Oct. 2007

Washington 2007

Localização: IFSC - Inst. Física de São Carlos    (PROD013876 )(Acessar)

17
Dissecting the structure, thermodynamic stability, and aggregation properties of the A25T transthyretin (A25T-TTR) variant involved in leptomeningeal amyloidosis identifying protein partners that co-aggregate during A25T-TTR fibrillogenesis in cerebrospinal fluid
Dissecting the structure, thermodynamic stability, and aggregation properties of the A25T transthyretin (A25T-TTR) variant involved in leptomeningeal amyloidosis identifying protein partners that co-aggregate during A25T-TTR fibrillogenesis in cerebrospinal fluid
Material Type:
Artigo 		Adicionar ao Meu Espaço

Dissecting the structure, thermodynamic stability, and aggregation properties of the A25T transthyretin (A25T-TTR) variant involved in leptomeningeal amyloidosis identifying protein partners that co-aggregate during A25T-TTR fibrillogenesis in cerebrospinal fluid

Estefania P. C. Azevedo Humberto D'Muniz Pereira; Richard Charles Garratt; Jeffery W Kelly; Debora Foguel; Fernando L Palhano

Biochemistry Washington, DC : American Chemical Society - ACS v. 50, n. 51, p. 11070-11083, Dec. 2011

Washington, DC 2011

Localização: IFSC - Inst. Física de São Carlos    (PROD019201 )(Acessar)

18
Conformational differences between the wild type and V30M mutant transthyretin modulate its binding to genistein implications to tetramer stability and ligand-binding
Conformational differences between the wild type and V30M mutant transthyretin modulate its binding to genistein implications to tetramer stability and ligand-binding
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Conformational differences between the wild type and V30M mutant transthyretin modulate its binding to genistein implications to tetramer stability and ligand-binding

Daniela B. B. Trivella Lucas Bleicher; Leonardo de Castro Palmieri; Helton José Wiggers; Carlos Alberto Montanari; Jeffery W Kelly; Luis Maurício T. R Lima; Débora Foguel; Igor Polikarpov

Journal of Structural Biology Maryland Heights : Academic Press v. 170, n. 3, p. 522-531, June 2010

Maryland Heights 2010

Localização: IFSC - Inst. Física de São Carlos    (PROD011663 ) e outros locais(Acessar)

19
Identification of archaeal proteins that affect the exosome function in vitro
Identification of archaeal proteins that affect the exosome function in vitro
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Identification of archaeal proteins that affect the exosome function in vitro

Juliana Silva da Luz Celso Raúl Romero Ramos; Márcia C. T Santos; Patricia Pereira Coltri; Fernando L Palhano; Débora Foguel; Nilson Ivo Tonin Zanchin; Carla Columbano de Oliveira

BMC Biochemistry London v. 9, art. 22 p. 1-14, 2010

London 2010

Acesso online

20
Conformational changes in human Hsp70 induced by high hydrostatic pressure produce oligomers with ATPase activity but without chaperone activity
Conformational changes in human Hsp70 induced by high hydrostatic pressure produce oligomers with ATPase activity but without chaperone activity
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Conformational changes in human Hsp70 induced by high hydrostatic pressure produce oligomers with ATPase activity but without chaperone activity

Thaís L. S. Araujo Julio Cesar Borges; Carlos Henrique Inacio Ramos; José Roberto Meyer-Fernandes; Reinaldo S Oliveira Júnior; Pedro Geraldo Pascutti; Debora Foguel; Fernando L Palhano

Biochemistry v. 53, n. 18, p. 2884-2889, 2014

Washington 2014

Localização: IQSC - Inst. Química de São Carlos    (P15047 )(Acessar)

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Deste Autor:

  1. Foguel, D
  2. Polikarpov, I
  3. Lima, L
  4. Palmieri, L
  5. Trivella, D

Neste Assunto:

  1. Science & Technology
  2. Life Sciences & Biomedicine
  3. Biochemistry & Molecular Biology
  4. Humans
  5. Animals

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

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