CD45 protein tyrosine phosphatase: Determination of minimal peptide length for substrate recognition and synthesis of some tyrosine-based electrophiles as potential active-site directed irreversible inhibitors

Mark Bobko; Henry R. Wolfe; Ashis Saha; Roland E. Dolle; Diana K. Fisher; Terry J. Higgins

doi:10.1016/0960-894X(95)00034-Q

CD45 protein tyrosine phosphatase: Determination of minimal peptide length for substrate recognition and synthesis of some tyrosine-based electrophiles as potential active-site directed irreversible inhibitors

Mark Bobko, Henry R. Wolfe, Ashis Saha, Roland E. Dolle, Diana K. Fisher, Terry J. Higgins

Center for Drug Discovery

Research output: Contribution to journal › Article › peer-review

9 Scopus citations

Abstract

Using fyn PTK as a template, a series of phosphopeptides 1-11 spanning in length from 1-14 amino acids was prepared. Kinetic evaluation of 1-11 suggest that CD45 does not have a strong preference for its N- or C-terminal amino acids and that extended phosphopeptides are not required for efficient substrate turnover.

Original language	English
Pages (from-to)	353-356
Number of pages	4
Journal	Bioorganic and Medicinal Chemistry Letters
Volume	5
Issue number	4
DOIs	https://doi.org/10.1016/0960-894X(95)00034-Q
State	Published - Feb 16 1995

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Bobko, M., Wolfe, H. R., Saha, A., Dolle, R. E., Fisher, D. K., & Higgins, T. J. (1995). CD45 protein tyrosine phosphatase: Determination of minimal peptide length for substrate recognition and synthesis of some tyrosine-based electrophiles as potential active-site directed irreversible inhibitors. Bioorganic and Medicinal Chemistry Letters, 5(4), 353-356. https://doi.org/10.1016/0960-894X(95)00034-Q

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abstract = "Using fyn PTK as a template, a series of phosphopeptides 1-11 spanning in length from 1-14 amino acids was prepared. Kinetic evaluation of 1-11 suggest that CD45 does not have a strong preference for its N- or C-terminal amino acids and that extended phosphopeptides are not required for efficient substrate turnover.",

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Bobko, M, Wolfe, HR, Saha, A, Dolle, RE, Fisher, DK & Higgins, TJ 1995, 'CD45 protein tyrosine phosphatase: Determination of minimal peptide length for substrate recognition and synthesis of some tyrosine-based electrophiles as potential active-site directed irreversible inhibitors', Bioorganic and Medicinal Chemistry Letters, vol. 5, no. 4, pp. 353-356. https://doi.org/10.1016/0960-894X(95)00034-Q

CD45 protein tyrosine phosphatase : Determination of minimal peptide length for substrate recognition and synthesis of some tyrosine-based electrophiles as potential active-site directed irreversible inhibitors. / Bobko, Mark; Wolfe, Henry R.; Saha, Ashis et al.

In: Bioorganic and Medicinal Chemistry Letters, Vol. 5, No. 4, 16.02.1995, p. 353-356.

Research output: Contribution to journal › Article › peer-review

TY - JOUR

T1 - CD45 protein tyrosine phosphatase

T2 - Determination of minimal peptide length for substrate recognition and synthesis of some tyrosine-based electrophiles as potential active-site directed irreversible inhibitors

AU - Bobko, Mark

AU - Wolfe, Henry R.

AU - Saha, Ashis

AU - Dolle, Roland E.

AU - Fisher, Diana K.

AU - Higgins, Terry J.

PY - 1995/2/16

Y1 - 1995/2/16

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AB - Using fyn PTK as a template, a series of phosphopeptides 1-11 spanning in length from 1-14 amino acids was prepared. Kinetic evaluation of 1-11 suggest that CD45 does not have a strong preference for its N- or C-terminal amino acids and that extended phosphopeptides are not required for efficient substrate turnover.

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SN - 0960-894X

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JO - Bioorganic and Medicinal Chemistry Letters

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Bobko M, Wolfe HR, Saha A, Dolle RE, Fisher DK, Higgins TJ. CD45 protein tyrosine phosphatase: Determination of minimal peptide length for substrate recognition and synthesis of some tyrosine-based electrophiles as potential active-site directed irreversible inhibitors. Bioorganic and Medicinal Chemistry Letters. 1995 Feb 16;5(4):353-356. doi: 10.1016/0960-894X(95)00034-Q

CD45 protein tyrosine phosphatase: Determination of minimal peptide length for substrate recognition and synthesis of some tyrosine-based electrophiles as potential active-site directed irreversible inhibitors

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