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Items: 1 to 50 of 125

1.

Detection of phosphorylation by immunological techniques.

Sefton BM.

Curr Protoc Protein Sci. 2001 May;Chapter 13:Unit13.4. doi: 10.1002/0471140864.ps1304s00.

PMID:
18429116
2.

Phosphoamino acid analysis.

Sefton BM.

Curr Protoc Protein Sci. 2001 May;Chapter 13:Unit13.3. doi: 10.1002/0471140864.ps1303s04.

PMID:
18429115
3.

Labeling cultured cells with 32P(i) and preparing cell lysates for immunoprecipitation.

Sefton BM.

Curr Protoc Protein Sci. 2001 May;Chapter 13:Unit13.2. doi: 10.1002/0471140864.ps1302s10.

PMID:
18429114
4.

Overview of protein phosphorylation.

Sefton BM, Shenolikar S.

Curr Protoc Protein Sci. 2001 May;Chapter 13:Unit13.1. doi: 10.1002/0471140864.ps1301s00. Review.

PMID:
18429113
5.

Analysis of phosphorylation of unlabeled proteins.

Sefton BM.

Curr Protoc Mol Biol. 2001 May;Chapter 18:Unit 18.4. doi: 10.1002/0471142727.mb1804s40.

PMID:
18265169
6.

Phosphoamino acid analysis.

Sefton BM.

Curr Protoc Mol Biol. 2001 May;Chapter 18:Unit 18.3. doi: 10.1002/0471142727.mb1803s40.

PMID:
18265168
7.

Labeling cultured cells with 32P(i) and preparing cell lysates for immunoprecipitation.

Sefton BM.

Curr Protoc Mol Biol. 2001 May;Chapter 18:Unit 18.2. doi: 10.1002/0471142727.mb1802s40.

PMID:
18265167
8.

Overview of protein phosphorylation.

Sefton BM, Shenolikar S.

Curr Protoc Mol Biol. 2001 May;Chapter 18:Unit 18.1. doi: 10.1002/0471142727.mb1801s33.

PMID:
18265166
9.

Phosphoamino acid analysis.

Sefton BM.

Curr Protoc Cell Biol. 2001 May;Chapter 14:Unit 14.5. doi: 10.1002/0471143030.cb1405s03.

PMID:
18228327
10.

Labeling cultured cells with 32Pi and preparing cell lysates for immunoprecipitation.

Sefton BM.

Curr Protoc Cell Biol. 2001 May;Chapter 14:Unit 14.4. doi: 10.1002/0471143030.cb1404s03.

PMID:
18228326
11.

Overview of protein phosphorylation.

Sefton BM.

Curr Protoc Cell Biol. 2001 May;Chapter 14:Unit 14.1. doi: 10.1002/0471143030.cb1401s00. Review.

PMID:
18228324
12.

Functional characterization and conformational analysis of the Herpesvirus saimiri Tip-C484 protein.

Mitchell JL, Trible RP, Emert-Sedlak LA, Weis DD, Lerner EC, Applen JJ, Sefton BM, Smithgall TE, Engen JR.

J Mol Biol. 2007 Mar 2;366(4):1282-93. Epub 2006 Dec 16.

13.

Altered dynamics in Lck SH3 upon binding to the LBD1 domain of Herpesvirus saimiri Tip.

Weis DD, Kjellen P, Sefton BM, Engen JR.

Protein Sci. 2006 Oct;15(10):2402-10.

14.

Relative contributions of desolvation, inter- and intramolecular interactions to binding affinity in protein kinase systems.

Sims PA, Wong CF, Vuga D, McCammon JA, Sefton BM.

J Comput Chem. 2005 May;26(7):668-81.

PMID:
15754303
15.
16.

The herpesvirus saimiri tip484 and tip488 proteins both stimulate lck tyrosine protein kinase activity in vivo and in vitro.

Kjellen P, Amdjadi K, Lund TC, Medveczky PG, Sefton BM.

Virology. 2002 Jun 5;297(2):281-8.

17.
18.

Activation of the Lck tyrosine protein kinase by the Herpesvirus saimiri tip protein involves two binding interactions.

Hartley DA, Amdjadi K, Hurley TR, Lund TC, Medveczky PG, Sefton BM.

Virology. 2000 Oct 25;276(2):339-48.

20.
21.

The Src-family kinase Lck can induce STAT3 phosphorylation and DNA binding activity.

Lund TC, Coleman C, Horvath E, Sefton BM, Jove R, Medveczky MM, Medveczky PG.

Cell Signal. 1999 Nov;11(11):789-96.

PMID:
10617281
22.

Activation of the lck tyrosine-protein kinase by the binding of the tip protein of herpesvirus saimiri in the absence of regulatory tyrosine phosphorylation.

Hartley DA, Hurley TR, Hardwick JS, Lund TC, Medveczky PG, Sefton BM.

J Biol Chem. 1999 Jul 16;274(29):20056-9.

23.

Growth-related changes in phosphorylation of yeast RNA polymerase II.

Patturajan M, Schulte RJ, Sefton BM, Berezney R, Vincent M, Bensaude O, Warren SL, Corden JL.

J Biol Chem. 1998 Feb 20;273(8):4689-94.

25.

Stimulation of phosphorylation of Tyr394 by hydrogen peroxide reactivates biologically inactive, non-membrane-bound forms of Lck.

Yurchak LK, Hardwick JS, Amrein K, Pierno K, Sefton BM.

J Biol Chem. 1996 May 24;271(21):12549-54.

26.
27.
29.

Role of tyrosine kinases in lymphocyte activation.

Sefton BM, Taddie JA.

Curr Opin Immunol. 1994 Jun;6(3):372-9. Review.

PMID:
7917104
30.

Activation of B- and T-cells by the cytoplasmic domains of the B-cell antigen receptor proteins Ig-alpha and Ig-beta.

Taddie JA, Hurley TR, Hardwick BS, Sefton BM.

J Biol Chem. 1994 May 6;269(18):13529-35.

31.
32.

B-cell activation by wild type and mutant Ig-beta cytoplasmic domains.

Taddie JA, Hurley TR, Sefton BM.

Adv Exp Med Biol. 1994;365:23-34.

PMID:
7887308
34.

Correlation between Src family member regulation by the protein-tyrosine-phosphatase CD45 and transmembrane signaling through the T-cell receptor.

Cahir McFarland ED, Hurley TR, Pingel JT, Sefton BM, Shaw A, Thomas ML.

Proc Natl Acad Sci U S A. 1993 Feb 15;90(4):1402-6.

35.

Tyrosine phosphorylation of actin in Dictyostelium associated with cell-shape changes.

Howard PK, Sefton BM, Firtel RA.

Science. 1993 Jan 8;259(5092):241-4.

PMID:
7678470
36.
38.

Tyrosine phosphorylation of CD22 during B cell activation.

Schulte RJ, Campbell MA, Fischer WH, Sefton BM.

Science. 1992 Nov 6;258(5084):1001-4.

PMID:
1279802
39.

Functional analysis of the SH2 and SH3 domains of the lck tyrosine protein kinase.

Reynolds PJ, Hurley TR, Sefton BM.

Oncogene. 1992 Oct;7(10):1949-55.

PMID:
1408136
40.
41.
43.

The lck tyrosine protein kinase.

Sefton BM.

Oncogene. 1991 May;6(5):683-6. Review. No abstract available.

PMID:
1905004
44.

Measurement of stoichiometry of protein phosphorylation by biosynthetic labeling.

Sefton BM.

Methods Enzymol. 1991;201:245-51. No abstract available.

PMID:
1943767
45.

Cyanogen bromide cleavage and proteolytic peptide mapping of proteins immobilized to membranes.

Luo KX, Hurley TR, Sefton BM.

Methods Enzymol. 1991;201:149-52. No abstract available.

PMID:
1943761
46.

The role of tyrosine protein phosphorylation in lymphocyte activation.

Sefton BM, Campbell MA.

Annu Rev Cell Biol. 1991;7:257-74. Review. No abstract available.

PMID:
1667083
48.

Changes in the relative abundance of type I and type II lck mRNA transcripts suggest differential promoter usage during T-cell development.

Reynolds PJ, Lesley J, Trotter J, Schulte R, Hyman R, Sefton BM.

Mol Cell Biol. 1990 Aug;10(8):4266-70.

50.

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