Heat-shock protein gp96/grp94 is an essential chaperone for the platelet glycoprotein Ib-IX-V complex

Folding of Toll-like receptors by the HSP90 paralogue gp96 requires a substrate-specific cochaperone

(2010) Bei Liu et al.   Nature Communications

gp96, an endoplasmic reticulum master chaperone for integrins and Toll-like receptors, selectively regulates early T and B lymphopoiesis

(2009) M. Staron et al.   BLOOD

Endoplasmic reticulum HSP90b1 (gp96, grp94) optimizes B-cell function via chaperoning integrin and TLR but not immunoglobulin

(2008) B. Liu et al.   BLOOD

The leucine-rich repeat structure

(2008) J. Bella et al.   CELLULAR AND MOLECULAR LIFE SCIENCES

Novel point mutation in a leucine-rich repeat of the GPIb  chain of the platelet von Willebrand factor receptor, GPIb/IX/V, resulting in an inherited dominant form of Bernard-Soulier syndrome affecting two unrelated families: the N41H variant

(2008) S. Vettore et al.   HAEMATOLOGICA

OS-9 and GRP94 deliver mutant α1-antitrypsin to the Hrd1–SEL1L ubiquitin ligase complex for ERAD

(2008) John C. Christianson et al.   NATURE CELL BIOLOGY

The role of Akt in the signaling pathway of the glycoprotein Ib-IX induced platelet activation

(2007) H. Yin et al.   BLOOD