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An isolated, surface-expressed I domain of the integrin αLβ2 is sufficient for strong adhesive function when locked in the open conformation with a disulfide bond

We introduced disulfide bonds to lock the integrin αLβ2 I domain in predicted open, ligand binding or closed, nonbinding conformations. Transfectants expressing αLβ2 heterodimers containing locked-open but not locked-closed or wild-type I domains constitutively adhered to intercellular adhesion mole...

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Hlavní autoři: Lu, Chafen, Shimaoka, Motomu, Ferzly, Mazen, Oxvig, Claus, Takagi, Junichi, Springer, Timothy A.
Médium: Artigo
Jazyk:Inglês
Vydáno: The National Academy of Sciences 2001
Témata:
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC30148/
https://ncbi.nlm.nih.gov/pubmed/11226249
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.041606398
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