Cargando…

The structure and oxidation of the eye lens chaperone αA-crystallin

The small heat shock protein (sHsp) αA-crystallin is a molecular chaperone important for the optical properties of the vertebrate eye lens. It forms heterogeneous oligomeric ensembles. We determined the structures of human αA-crystallin oligomers combining cryo-electron microscopy, cross-linking/mas...

Descripción completa

Detalles Bibliográficos
Autores principales:	Kaiser, Christoph J. O., Peters, Carsten, Schmid, Philipp W. N., Stavropoulou, Maria, Zou, Juan, Dahiya, Vinay, Mymrikov, Evgeny V., Rockel, Beate, Asami, Sam, Haslbeck, Martin, Rappsilber, Juri, Reif, Bernd, Zacharias, Martin, Buchner, Johannes, Weinkauf, Sevil
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	2019
Materias:	Article
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7115824/ https://www.ncbi.nlm.nih.gov/pubmed/31792453 http://dx.doi.org/10.1038/s41594-019-0332-9

Ejemplares similares

The permanently chaperone-active small heat shock protein Hsp17 from Caenorhabditis elegans exhibits topological separation of its N-terminal regions
por: Strauch, Annika, et al.
Publicado: (2022)

Phosphorylation activates the yeast small heat shock protein Hsp26 by weakening domain contacts in the oligomer ensemble
por: Mühlhofer, Moritz, et al.
Publicado: (2021)

In Vivo Substrates of the Lens Molecular Chaperones αA-Crystallin and αB-Crystallin
por: Andley, Usha P., et al.
Publicado: (2014)

Correction: In Vivo Substrates of the Lens Molecular Chaperones αA-Crystallin and αB-Crystallin
Publicado: (2014)

Disordered region encodes α-crystallin chaperone activity toward lens client γD-crystallin
por: Woods, Christopher N., et al.
Publicado: (2023)

α-Crystallin chaperone mimetic drugs inhibit lens γ-crystallin aggregation: Potential role for cataract prevention
por: Islam, Sidra, et al.
Publicado: (2022)

The Crystalline Lens
por: Macnamara, C.
Publicado: (1866)

Active unfolding of the glucocorticoid receptor by the Hsp70/Hsp40 chaperone system in single-molecule mechanical experiments
por: Moessmer, Patrick, et al.
Publicado: (2022)

Reprodution of the Crystalline Lens
Publicado: (1867)

Functional Amyloid Protection in the Eye Lens: Retention of α-Crystallin Molecular Chaperone Activity after Modification into Amyloid Fibrils
por: Garvey, Megan, et al.
Publicado: (2017)

The Molecular Chaperone α-Crystallin as an Excipient in an Insulin Formulation
por: Rasmussen, Tue, et al.
Publicado: (2010)

DNAJC9 integrates heat shock molecular chaperones into the histone chaperone network
por: Hammond, Colin M., et al.
Publicado: (2021)

Spontaneous Lens Absorption Initially Misdiagnosed as Crystalline Lens Luxation
por: Gönül, Şaban, et al.
Publicado: (2018)

PAX8 Expression in the Crystalline Lens and Lens-Derived Lesions
por: Milman, Tatyana, et al.
Publicado: (2021)

In vivo human crystalline lens topography
por: Ortiz, Sergio, et al.
Publicado: (2012)

Inadvertent steroid injection into the crystalline lens
por: Alam, Md. Shahid, et al.
Publicado: (2017)

Loss of Crystalline Lens by Blow on Eyeball
por: Kenan, Thomas H.
Publicado: (1876)

Crystallin genes: lens specificity of the murine alpha A-crystallin gene.
por: Chepelinsky, A B, et al.
Publicado: (1987)

Structural basis for centromere maintenance by Drosophila CENP‐A chaperone CAL1
por: Medina‐Pritchard, Bethan, et al.
Publicado: (2020)

The molecular basis of chaperone-mediated interleukin 23 assembly control
por: Meier, Susanne, et al.
Publicado: (2019)

Peripheral Defocus of the Monkey Crystalline Lens With Accommodation in a Lens Stretcher
por: Maceo Heilman, Bianca, et al.
Publicado: (2018)

Subunit Mobility and the Chaperone Activity of Recombinant αB-Crystallin
por: Krushelnitsky, A, et al.
Publicado: (2008)

Entrapment of intravitreal triamcinolone behind the crystalline lens
por: Salman, Amjad, et al.
Publicado: (2009)

In Vivo Brillouin Analysis of the Aging Crystalline Lens
por: Besner, Sebastien, et al.
Publicado: (2016)

Mode of Discovering the Proper Capsule of the Crystalline Lens
Publicado: (1815)

A native chemical chaperone in the human eye lens
por: Serebryany, Eugene, et al.
Publicado: (2022)

Molecular Mechanism of the Chaperone Function of Mini-α-Crystallin, a 19-Residue Peptide of Human α-Crystallin
por: Banerjee, Priya R., et al.
Publicado: (2014)

Refolding Increases the Chaperone-like Activity of α(H)-Crystallin and Reduces Its Hydrodynamic Diameter to That of α-Crystallin
por: Muranov, Konstantin O., et al.
Publicado: (2023)

Management of endophthalmitis while preserving the uninvolved crystalline lens
por: Townsend, Justin, et al.
Publicado: (2012)

Connexins, Cell Proliferation and Second Messengers in the Crystalline Lens
por: White, Thomas W
Publicado: (2012)

A medieval fallacy: the crystalline lens in the center of the eye
por: Leffler, Christopher T, et al.
Publicado: (2016)

A Case of Mineral or Calcareous Degeneration of the Crystalline Lens
por: Chatterjee, H.
Publicado: (1892)

Crystalline lens dislocation secondary to bacterial endogenous endophthalmitis
por: Sangave, Amit, et al.
Publicado: (2017)

Crystalline Lens Resorption Caused by Ciliary Body Melanoma
por: Carrera, William M., et al.
Publicado: (2020)

Hop/Sti1 phosphorylation inhibits its co-chaperone function
por: Röhl, Alina, et al.
Publicado: (2015)

Age-dependent association of γ-crystallins with aged α-crystallins from old bovine lens
por: Takemoto, Larry, et al.
Publicado: (2008)

αA-Crystallin Peptide (66) SDRDKFVIFLDVKHF (80) Accumulating in Aging Lens Impairs the Function of α-Crystallin and Induces Lens Protein Aggregation
por: Santhoshkumar, Puttur, et al.
Publicado: (2011)

Addition of αA-Crystallin Sequence 164–173 to a Mini-Chaperone DFVIFLDVKHFSPEDLT Alters the Conformation but Not the Chaperone-like Activity
por: Raju, Murugesan, et al.
Publicado: (2014)

αA-Crystallin–Derived Mini-Chaperone Modulates Stability and Function of Cataract Causing αAG98R-Crystallin
por: Raju, Murugesan, et al.
Publicado: (2012)

The mechanism for thermal-enhanced chaperone-like activity of α-crystallin against UV irradiation-induced aggregation of γD-crystallin
por: Li, Hao, et al.
Publicado: (2022)

Cannot write session to /tmp/vufind_sessions/sess_gruc6a0uqi0qipbknr0nbegoo9