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Osteopontin is a small integrin-binding ligand N-linked glycoprotein (SIBLING) that binds to cell surface receptors including integrins and CD44.
Chordin then binds to cell surface anchored components such as BMP-binding endothelial cell precursor-derived regulator (BMPER) [ 15], integrins [ 16] and collagen IV [ 17], localizing captive BMP to a specific tissue for subsequent release by tolloids or promoting chordin endocytosis.
It has been shown that HBP binds to cell surface proteoglycans, but the importance of this binding for permeability increases has not been investigated [3, 4].
Arnberg, N. et al. Adenovirus type 37 binds to cell surface sialic acid through a charge-dependent interaction.
Their C-terminal domain binds to cell surface receptors and is thereby responsible for cell anchorage and the initiation of specific outside-in and inside-out signals.
When α2M is "activated" (α2M*) by interacting with a proteinase, it binds to cell surface receptors which rapidly remove the complexes from the external environment.
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Fibronectin is normally a tangled protein, but when it binds to cell surfaces, it gets stretched out into long bundles.
Alpha2M* binds to cell surface-associated glucose-regulated protein 78 (GRP78), which activates downstream signaling events.
Receptor-recognized α₂-macroglobulin binds to cell surface-associated GRP78 and activates mTORC1 and mTORC2 signaling in prostate cancer cells.
Polybrene is a small, positively charged molecule that binds to cell surfaces and neutralizes surface charge and has been shown to enhance cell transduction by retroviruses [ 35].
These molecules bind to cell surface receptors and are subsequently internalized by endocytosis, resulting in cell death.
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