Expression, purification, and crystallization of the RGS-like domain from the Rho nucleotide exchange factor, PDZ-RhoGEF, using the surface entropy reduction approach

Protein Expression and Purification

Volumn 21, Issue 3, 2001, Pages 412-416

  Garrard, Sarah M ^a   Longenecker, Kenton L ^a   Lewis, Mary E ^a   Sheffield, Peter J ^a   Derewenda, Zygmunt S ^a  

^a UNIVERSITY OF VIRGINIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EUKARYOTA;

EID: 0035717549     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.2001.1392     Document Type: Article

References (19)

1. Signalling mechanisms in the regulation of vascular cell migration
2. Rho GTPases and the actin cytoskeleton
3. Rho GTPases
4. The small GTPase Rho: Cellular functions and signal transduction
5. Rho effectors and reorganization of actin cytoskeleton
6. The small Gtp-binding proteins, Rac and Rho, regulate cytoskeletal organization and exocytosis in mast cells by parallel pathways
7. An essential role for Rho, Rac, and Cdc42 GTPases in cell cycle progression through G1
8. The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors
9. Signal transduction and regulation in smooth muscle
10. The Rho family GTPases RhoA, Rac1, and CDC42Hs regulate transcriptional activation by SRF
11. Proteins regulating Ras and its relatives
12. Dbl family proteins
13. The DH protein family, exchange factors for Rho-like GTPases
14. Structure and mutagenesis of the Dbl homology domain
15. A novel PDZ domain containing guanine nucleotide exchange factor links heterotrimeric G proteins to Rho
16. Overcoming expression and purification problems of RhoGDI using a family of “Parallel” expression vectors
17. Processing of X-ray diffraction data collected in oscillation mode
18. Measures of residue density in protein structures
19. Role of main-chain electrostatics, hydrophobic effect and side-chain conformational entropy in determining the secondary structure of proteins