Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP.

BiP and zein binding domains within the delta zein protein

A phaseolin domain involved directly in trimer assembly is a determinant for binding by the chaperone BiP.

The In Vivo Association of BiP with Newly Synthesized Proteins Is Dependent on the Rate and Stability of Folding and Not Simply on the Presence of Sequences That Can Bind to BiP

Interaction between BiP and Sec63p is required for the completion of protein translocation into the ER of Saccharomyces cerevisiae

Interaction between BiP and Sec63p is required for the completion of protein translocation into the ER of Saccharomyces cerevisiae.

Differential Transit Peptide Recognition during Preprotein Binding and Translocation into Flowering Plant PlastidsW

Differential transit peptide recognition during preprotein binding and translocation into flowering plant plastids.

Lectin chaperones help direct the maturation of glycoproteins in the endoplasmic reticulum.

The messenger and the message: gp96 (GRP94)-peptide interactions in cellular immunity.

Production of bioactive recombinant human Eb-peptide of pro-IGF-I and identification of binding components from the plasma membrane of human breast cancer cells (MDA-MB-231).

Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP.

BiP and zein binding domains within the delta zein protein

A phaseolin domain involved directly in trimer assembly is a determinant for binding by the chaperone BiP.

The In Vivo Association of BiP with Newly Synthesized Proteins Is Dependent on the Rate and Stability of Folding and Not Simply on the Presence of Sequences That Can Bind to BiP

Interaction between BiP and Sec63p is required for the completion of protein translocation into the ER of Saccharomyces cerevisiae

Interaction between BiP and Sec63p is required for the completion of protein translocation into the ER of Saccharomyces cerevisiae.

Differential Transit Peptide Recognition during Preprotein Binding and Translocation into Flowering Plant PlastidsW

Differential transit peptide recognition during preprotein binding and translocation into flowering plant plastids.

Lectin chaperones help direct the maturation of glycoproteins in the endoplasmic reticulum.

The messenger and the message: gp96 (GRP94)-peptide interactions in cellular immunity.

Production of bioactive recombinant human Eb-peptide of pro-IGF-I and identification of binding components from the plasma membrane of human breast cancer cells (MDA-MB-231).

Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP.

BiP and zein binding domains within the delta zein protein

A phaseolin domain involved directly in trimer assembly is a determinant for binding by the chaperone BiP.

The In Vivo Association of BiP with Newly Synthesized Proteins Is Dependent on the Rate and Stability of Folding and Not Simply on the Presence of Sequences That Can Bind to BiP

Interaction between BiP and Sec63p is required for the completion of protein translocation into the ER of Saccharomyces cerevisiae

Interaction between BiP and Sec63p is required for the completion of protein translocation into the ER of Saccharomyces cerevisiae.

Differential Transit Peptide Recognition during Preprotein Binding and Translocation into Flowering Plant PlastidsW

Differential transit peptide recognition during preprotein binding and translocation into flowering plant plastids.

Lectin chaperones help direct the maturation of glycoproteins in the endoplasmic reticulum.

The messenger and the message: gp96 (GRP94)-peptide interactions in cellular immunity.

Production of bioactive recombinant human Eb-peptide of pro-IGF-I and identification of binding components from the plasma membrane of human breast cancer cells (MDA-MB-231).