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Human heat shock cognate protein (HSC70/HSPA8) interacts with negatively charged phospholipids by a different mechanism than other HSP70s and brings HSP90 into membranes
Human heat shock cognate protein (HSC70/HSPA8) interacts with negatively charged phospholipids by a different mechanism than other HSP70s and brings HSP90 into membranes
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Human heat shock cognate protein (HSC70/HSPA8) interacts with negatively charged phospholipids by a different mechanism than other HSP70s and brings HSP90 into membranes

Paulo Roberto Dores-Silva David M Cauvi; Amanda L. S Coto; Noeli Soares Melo da Silva; Julio Cesar Borges; Antonio De Maio

Cell Stress & Chaperones Dordrecht: Springer Netherlands p. 26, n. 4, p. 671-684, 2021

Dordrecht 2021

Localização: IQSC - Inst. Química de São Carlos    (P19386 )(Acessar)

2
Proteomic data from human cell cultures refine mechanisms of chaperone-mediated protein homeostasis
Proteomic data from human cell cultures refine mechanisms of chaperone-mediated protein homeostasis
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Proteomic data from human cell cultures refine mechanisms of chaperone-mediated protein homeostasis

Finka, Andrija ; Goloubinoff, Pierre

Cell stress & chaperones, 2013-09, Vol.18 (5), p.591-605 [Periódico revisado por pares]

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3
Structure-function relationship of H2A-H2B specific plant histone chaperones
Structure-function relationship of H2A-H2B specific plant histone chaperones
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Structure-function relationship of H2A-H2B specific plant histone chaperones

Kumar, Ashish ; Vasudevan, Dileep

Cell stress & chaperones, 2020-01, Vol.25 (1), p.1-17 [Periódico revisado por pares]

Dordrecht: Springer Science + Business Media

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4
Lipid chaperones and associated diseases: a group of chaperonopathies defining a new nosological entity with implications for medical research and practice
Lipid chaperones and associated diseases: a group of chaperonopathies defining a new nosological entity with implications for medical research and practice
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Lipid chaperones and associated diseases: a group of chaperonopathies defining a new nosological entity with implications for medical research and practice

D’Anneo, Antonella ; Bavisotto, Celeste Caruso ; Gammazza, Antonella Marino ; Paladino, Letizia ; Carlisi, Daniela ; Cappello, Francesco ; de Macario, Everly Conway ; Macario, Alberto J. L. ; Lauricella, Marianna

Cell stress & chaperones, 2020-11, Vol.25 (6), p.805-820 [Periódico revisado por pares]

Dordrecht: Springer Science + Business Media

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5
Small heat-shock proteins and their role in mechanical stress
Small heat-shock proteins and their role in mechanical stress
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Small heat-shock proteins and their role in mechanical stress

Collier, Miranda P. ; Benesch, Justin L.P.

Cell stress & chaperones, 2020-07, Vol.25 (4), p.601-613 [Periódico revisado por pares]

Dordrecht: Springer Science + Business Media

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6
Novel insights into the post-translational modifications of Ydj1/DNAJA1 co-chaperones
Novel insights into the post-translational modifications of Ydj1/DNAJA1 co-chaperones
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Novel insights into the post-translational modifications of Ydj1/DNAJA1 co-chaperones

Mitchem, Megan M. ; Shrader, Courtney ; Abedi, Elizabeth ; Truman, Andrew W.

Cell stress & chaperones, 2024-02, Vol.29 (1), p.1-9 [Periódico revisado por pares]

Netherlands: Elsevier

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7
Protein quality control: from molecular mechanisms to therapeutic intervention—EMBO workshop, May 21–26 2023, Srebreno, Croatia
Protein quality control: from molecular mechanisms to therapeutic intervention—EMBO workshop, May 21–26 2023, Srebreno, Croatia
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Protein quality control: from molecular mechanisms to therapeutic intervention—EMBO workshop, May 21–26 2023, Srebreno, Croatia

Münch, Christian ; Kirstein, Janine

Cell stress & chaperones, 2023-11, Vol.28 (6), p.631-640 [Periódico revisado por pares]

Dordrecht: Springer Science + Business Media

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8
Exported plasmodial J domain protein, PFE0055c, and PfHsp70-x form a specific co-chaperone-chaperone partnership
Exported plasmodial J domain protein, PFE0055c, and PfHsp70-x form a specific co-chaperone-chaperone partnership
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Exported plasmodial J domain protein, PFE0055c, and PfHsp70-x form a specific co-chaperone-chaperone partnership

Dutta, Tanima ; Singh, Harpreet ; Gestwicki, Jason E. ; Blatch, Gregory L.

Cell stress & chaperones, 2021-03, Vol.26 (2), p.355-366 [Periódico revisado por pares]

Dordrecht: Springer Science + Business Media

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9
Human Hsp90 cochaperones: perspectives on tissue-specific expression and identification of cochaperones with similar in vivo functions
Human Hsp90 cochaperones: perspectives on tissue-specific expression and identification of cochaperones with similar in vivo functions
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Human Hsp90 cochaperones: perspectives on tissue-specific expression and identification of cochaperones with similar in vivo functions

Dean, Marissa E. ; Johnson, Jill L.

Cell stress & chaperones, 2021-01, Vol.26 (1), p.3-13 [Periódico revisado por pares]

Dordrecht: Springer Science + Business Media

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10
Increased expression and retention of the secretory chaperone proSAAS following cell stress
Increased expression and retention of the secretory chaperone proSAAS following cell stress
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Increased expression and retention of the secretory chaperone proSAAS following cell stress

Shakya, Manita ; Yildirim, Taha ; Lindberg, Iris

Cell stress & chaperones, 2020-11, Vol.25 (6), p.929-943 [Periódico revisado por pares]

Dordrecht: Springer Science + Business Media

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Deste Autor:

  1. Silva, N
  2. Borges, J
  3. De Maio, A
  4. Dores-Silva, P
  5. Coto, A

Neste Assunto:

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

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

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