Correlation of Membrane Binding and Hydrophobicity to the Chaperone-Like Activity of PDC-109, the Major Protein of Bovine Seminal Plasma

The Major Protein of Bovine Seminal Plasma, PDC-109, Is a Molecular Chaperone

(2010) Rajeshwer Singh Sankhala et al.   BIOCHEMISTRY

Interaction of Mammalian Seminal Plasma Protein PDC-109 with Cholesterol: Implications for a Putative CRAC Domain

(2010) Silvia Scolari et al.   BIOCHEMISTRY

31P NMR and AFM studies on the destabilization of cell and model membranes by the major bovine seminal plasma protein, PDC-109

(2010) Rajani S. Damai et al.   IUBMB LIFE

Hsp12 Is an Intrinsically Unstructured Stress Protein that Folds upon Membrane Association and Modulates Membrane Function

(2010) Sylvia Welker et al.   MOLECULAR CELL

Binding Regions of Outer Membrane Protein A in Complexes with the Periplasmic Chaperone Skp. A Site-Directed Fluorescence Study

(2009) Jian Qu et al.   BIOCHEMISTRY

Fluorescence studies on the interaction of choline-binding domain B of the major bovine seminal plasma protein, PDC-109 with phospholipid membranes

(2009) Rajani S. Damai et al.   BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS

Interaction of the major protein from bovine seminal plasma, PDC-109 with phospholipid membranes and soluble ligands investigated by fluorescence approaches

(2008) V. Anbazhagan et al.   BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS

Fluorescence studies on the interaction of hydrophobic ligands with Momordica charantia (bitter gourd) seed lectin

(2008) Mannem Kavitha et al.   JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY B-BIOLOGY

Interaction of C-Terminal Truncated Human αA-Crystallins with Target Proteins

(2008) Anbarasu Kumarasamy et al.   PLoS One

Binding of bovine seminal plasma protein BSP-A1/-A2 to model membranes: Lipid specificity and effect of the temperature

(2007) Danny Lassiseraye et al.   BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES