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Purification of a bone sialoprotein-binding protein from Staphylococcus aureus.
Yacoub A, Lindahl P, Rubin K, Wendel M, Heinegård D, Rydén C. Yacoub A, et al. Among authors: heinegard d. Eur J Biochem. 1994 Jun 15;222(3):919-25. doi: 10.1111/j.1432-1033.1994.tb18940.x. Eur J Biochem. 1994. PMID: 8026501 Free article.
Bone sialoprotein (BSP) is selectively bound by Staphylococcus aureus cells isolated from patients suffering from infections of bone and joint tissues [Ryden C., Maxe, I., Franzen, A., Ljungh, A., Heinegard, D. & Rubin, K. (1987) Lancet II, 515]. We now report o …
Bone sialoprotein (BSP) is selectively bound by Staphylococcus aureus cells isolated from patients suffering from infections of bone and joi …
Specific binding of bone sialoprotein to Staphylococcus aureus isolated from patients with osteomyelitis.
Rydén C, Yacoub AI, Maxe I, Heinegård D, Oldberg A, Franzén A, Ljungh A, Rubin K. Rydén C, et al. Among authors: heinegard d. Eur J Biochem. 1989 Sep 15;184(2):331-6. doi: 10.1111/j.1432-1033.1989.tb15023.x. Eur J Biochem. 1989. PMID: 2792103 Free article.
Bone sialoprotein is selectively bound by Staphylococcus aureus cells isolated from patients suffering from infections of bone tissue [Ryden, C., Maxe, I., Franzen, A., Ljungh, A., Heinegard, D. & Rubin, K. (1987) Lancet II, 514]. In the present communication th …
Bone sialoprotein is selectively bound by Staphylococcus aureus cells isolated from patients suffering from infections of bone tissue [Ryden …
Dephosphorylation of osteopontin and bone sialoprotein by osteoclastic tartrate-resistant acid phosphatase. Modulation of osteoclast adhesion in vitro.
Ek-Rylander B, Flores M, Wendel M, Heinegård D, Andersson G. Ek-Rylander B, et al. Among authors: heinegard d. J Biol Chem. 1994 May 27;269(21):14853-6. J Biol Chem. 1994. PMID: 8195113 Free article.
TRAP also partially dephosphorylated metabolically [32P]PO4-labeled OPN as well as BSP, whereas comparable amounts of either alkaline phosphatase or prostatic acid phosphatase, at their respective pH optima, were ineffective, indicating a certain preference of TRAP for these phos …
TRAP also partially dephosphorylated metabolically [32P]PO4-labeled OPN as well as BSP, whereas comparable amounts of either alkaline phosph …
Macromolecules in bone matrix.
Heinegård D, Hultenby K, Oldberg A, Reinholt F, Wendel M. Heinegård D, et al. Connect Tissue Res. 1989;21(1-4):3-11; discussion 12-4. doi: 10.3109/03008208909049990. Connect Tissue Res. 1989. PMID: 2691197 Review. No abstract available.
331 results