Cochran AG - Search Results

1

BAFF/BLyS receptor 3 binds the B cell survival factor BAFF ligand through a discrete surface loop and promotes processing of NF-kappaB2.

Kayagaki N, Yan M, Seshasayee D, Wang H, Lee W, French DM, Grewal IS, Cochran AG, Gordon NC, Yin J, Starovasnik MA, Dixit VM. Kayagaki N, et al. Among authors: cochran ag. Immunity. 2002 Oct;17(4):515-24. doi: 10.1016/s1074-7613(02)00425-9. Immunity. 2002. PMID: 12387744 Free article.

2

Tryptophan zippers: stable, monomeric beta -hairpins.

Cochran AG, Skelton NJ, Starovasnik MA. Cochran AG, et al. Proc Natl Acad Sci U S A. 2001 May 8;98(10):5578-83. doi: 10.1073/pnas.091100898. Epub 2001 May 1. Proc Natl Acad Sci U S A. 2001. PMID: 11331745 Free PMC article.

3

A minimal peptide scaffold for beta-turn display: optimizing a strand position in disulfide-cyclized beta-hairpins.

Cochran AG, Tong RT, Starovasnik MA, Park EJ, McDowell RS, Theaker JE, Skelton NJ. Cochran AG, et al. J Am Chem Soc. 2001 Jan 31;123(4):625-32. doi: 10.1021/ja003369x. J Am Chem Soc. 2001. PMID: 11456574

4

BAFF/BLyS receptor 3 comprises a minimal TNF receptor-like module that encodes a highly focused ligand-binding site.

Gordon NC, Pan B, Hymowitz SG, Yin J, Kelley RF, Cochran AG, Yan M, Dixit VM, Fairbrother WJ, Starovasnik MA. Gordon NC, et al. Among authors: cochran ag. Biochemistry. 2003 May 27;42(20):5977-83. doi: 10.1021/bi034017g. Biochemistry. 2003. PMID: 12755599

5

Phosphorylation-dependent activity of the deubiquitinase DUBA.

Huang OW, Ma X, Yin J, Flinders J, Maurer T, Kayagaki N, Phung Q, Bosanac I, Arnott D, Dixit VM, Hymowitz SG, Starovasnik MA, Cochran AG. Huang OW, et al. Among authors: cochran ag. Nat Struct Mol Biol. 2012 Jan 15;19(2):171-5. doi: 10.1038/nsmb.2206. Nat Struct Mol Biol. 2012. PMID: 22245969

6

Deubiquitinase DUBA is a post-translational brake on interleukin-17 production in T cells.

Rutz S, Kayagaki N, Phung QT, Eidenschenk C, Noubade R, Wang X, Lesch J, Lu R, Newton K, Huang OW, Cochran AG, Vasser M, Fauber BP, DeVoss J, Webster J, Diehl L, Modrusan Z, Kirkpatrick DS, Lill JR, Ouyang W, Dixit VM. Rutz S, et al. Among authors: cochran ag. Nature. 2015 Feb 19;518(7539):417-21. doi: 10.1038/nature13979. Epub 2014 Dec 3. Nature. 2015. PMID: 25470037

7

Novel peptides selected to bind vascular endothelial growth factor target the receptor-binding site.

Fairbrother WJ, Christinger HW, Cochran AG, Fuh G, Keenan CJ, Quan C, Shriver SK, Tom JY, Wells JA, Cunningham BC. Fairbrother WJ, et al. Among authors: cochran ag. Biochemistry. 1998 Dec 22;37(51):17754-64. doi: 10.1021/bi981931e. Biochemistry. 1998. PMID: 9922141

8

Crystal structure of the complex between VEGF and a receptor-blocking peptide.

Wiesmann C, Christinger HW, Cochran AG, Cunningham BC, Fairbrother WJ, Keenan CJ, Meng G, de Vos AM. Wiesmann C, et al. Among authors: cochran ag. Biochemistry. 1998 Dec 22;37(51):17765-72. doi: 10.1021/bi9819327. Biochemistry. 1998. PMID: 9922142

9

Antagonists of protein-protein interactions.

Cochran AG. Cochran AG. Chem Biol. 2000 Apr;7(4):R85-94. doi: 10.1016/s1074-5521(00)00106-x. Chem Biol. 2000. PMID: 10779412 Review.

10

Solution structure of a phage-derived peptide antagonist in complex with vascular endothelial growth factor.

Pan B, Li B, Russell SJ, Tom JY, Cochran AG, Fairbrother WJ. Pan B, et al. Among authors: cochran ag. J Mol Biol. 2002 Feb 22;316(3):769-87. doi: 10.1006/jmbi.2001.5370. J Mol Biol. 2002. PMID: 11866530

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