[HTML][HTML] SPARC, a matricellular protein that functions in cellular differentiation and tissue response to injury
AD Bradshaw, EH Sage - The Journal of clinical …, 2001 - Am Soc Clin Investig
AD Bradshaw, EH Sage
The Journal of clinical investigation, 2001•Am Soc Clin InvestigStructure of SPARC protein. A ribbon diagram derived from crystallographic data shows the
three modular domains of SPARC. Representative activities attributed to each domain are
shown beneath the designated amino acids. The follistatin-like domain contains the peptide
2.1 (see ref. 1) shown in green and the (K) GHK angiogenic peptide (amino acids 114–130)
shown in black. The EC domain contains the amino acids 255–274 (peptide 4.2) shown in
yellow. Modified from Hohenester et al.(29) and the Brookhaven Protein Database …
three modular domains of SPARC. Representative activities attributed to each domain are
shown beneath the designated amino acids. The follistatin-like domain contains the peptide
2.1 (see ref. 1) shown in green and the (K) GHK angiogenic peptide (amino acids 114–130)
shown in black. The EC domain contains the amino acids 255–274 (peptide 4.2) shown in
yellow. Modified from Hohenester et al.(29) and the Brookhaven Protein Database …
Structure of SPARC protein. A ribbon diagram derived from crystallographic data shows the three modular domains of SPARC. Representative activities attributed to each domain are shown beneath the designated amino acids. The follistatin-like domain contains the peptide 2.1 (see ref. 1) shown in green and the (K) GHK angiogenic peptide (amino acids 114–130) shown in black. The EC domain contains the amino acids 255–274 (peptide 4.2) shown in yellow. Modified from Hohenester et al.(29) and the Brookhaven Protein Database, accession no. 1BM0 from Ref. 1, with permission.
The Journal of Clinical Investigation