Warning: Undefined array key "mm" in /www/wwwroot/www.ai-bt.com/si.php on line 10 Deprecated: trim(): Passing null to parameter #1 ($string) of type string is deprecated in /www/wwwroot/www.ai-bt.com/si.php on line 10 Membrane binding of intrinsically disordered proteins: Critical importance of an appropriate membrane model.

Literature DB >> 21487515

Membrane binding of intrinsically disordered proteins: Critical importance of an appropriate membrane model.

Alexander B Sigalov¹.

Abstract

Entities: Disease

Year: 2010 PMID： 21487515 PMCID： PMC3065671 DOI： 10.4161/self.1.2.11547

Source DB: PubMed Journal: Self Nonself ISSN： 1938-2030

× No keyword cloud information.

8 in total

1. Phosphorylation of T cell receptor zeta is regulated by a lipid dependent folding transition.

Authors: D Aivazian; L J Stern
Journal: Nat Struct Biol Date: 2000-11

2. Structure induction of the T-cell receptor zeta-chain upon lipid binding investigated by NMR spectroscopy.

Authors: Elke Duchardt; Alexander B Sigalov; Dikran Aivazian; Lawrence J Stern; Harald Schwalbe
Journal: Chembiochem Date: 2007-05-07 Impact factor: 3.164

3. Lipid-binding activity of intrinsically unstructured cytoplasmic domains of multichain immune recognition receptor signaling subunits.

Authors: Alexander B Sigalov; Dikran A Aivazian; Vladimir N Uversky; Lawrence J Stern
Journal: Biochemistry Date: 2006-12-19 Impact factor: 3.162

4. Conformational effect of phosphorylation on T cell receptor/CD3 zeta-chain sequences.

Authors: I Laczkó; M Hollósi; E Vass; Z Hegedüs; E Monostori; G K Tóth
Journal: Biochem Biophys Res Commun Date: 1998-01-26 Impact factor: 3.575

5. Membrane binding mode of intrinsically disordered cytoplasmic domains of T cell receptor signaling subunits depends on lipid composition.

Authors: Alexander B Sigalov; Gregory M Hendricks
Journal: Biochem Biophys Res Commun Date: 2009-09-04 Impact factor: 3.575

6. Phosphorylated T cell receptor zeta-chain and ZAP70 tandem SH2 domains form a 1:3 complex in vitro.

Authors: W Weissenhorn; M J Eck; S C Harrison; D C Wiley
Journal: Eur J Biochem Date: 1996-06-01

7. Regulation of T cell receptor activation by dynamic membrane binding of the CD3epsilon cytoplasmic tyrosine-based motif.

Authors: Chenqi Xu; Etienne Gagnon; Matthew E Call; Jason R Schnell; Charles D Schwieters; Christopher V Carman; James J Chou; Kai W Wucherpfennig
Journal: Cell Date: 2008-11-14 Impact factor: 41.582

8. The safety on the TCR trigger.

Authors: Michael S Kuhns; Mark M Davis
Journal: Cell Date: 2008-11-14 Impact factor: 41.582

8 in total

7 in total

7. Protocol for Investigating the Interactions Between Intrinsically Disordered Proteins and Membranes by Neutron Reflectometry.

Authors: Alessandra Luchini; Lise Arleth
Journal: Methods Mol Biol Date: 2020

7 in total

Membrane binding of intrinsically disordered proteins: Critical importance of an appropriate membrane model.

1. Phosphorylation of T cell receptor zeta is regulated by a lipid dependent folding transition.

2. Structure induction of the T-cell receptor zeta-chain upon lipid binding investigated by NMR spectroscopy.

3. Lipid-binding activity of intrinsically unstructured cytoplasmic domains of multichain immune recognition receptor signaling subunits.

4. Conformational effect of phosphorylation on T cell receptor/CD3 zeta-chain sequences.

5. Membrane binding mode of intrinsically disordered cytoplasmic domains of T cell receptor signaling subunits depends on lipid composition.

6. Phosphorylated T cell receptor zeta-chain and ZAP70 tandem SH2 domains form a 1:3 complex in vitro.

7. Regulation of T cell receptor activation by dynamic membrane binding of the CD3epsilon cytoplasmic tyrosine-based motif.

8. The safety on the TCR trigger.

1. Unusual biophysics of immune signaling-related intrinsically disordered proteins.

Review 2. The Structural and Functional Diversity of Intrinsically Disordered Regions in Transmembrane Proteins.

3. Membrane-mediated regulation of the intrinsically disordered CD3ϵ cytoplasmic tail of the TCR.

Review 4. Functions of intrinsic disorder in transmembrane proteins.

5. Insights into the Function of the Unstructured N-Terminal Domain of Proteins 4.1R and 4.1G in Erythropoiesis.

Review 6. Recent Advances in Computational Protocols Addressing Intrinsically Disordered Proteins.

7. Protocol for Investigating the Interactions Between Intrinsically Disordered Proteins and Membranes by Neutron Reflectometry.