Brenner C - Search Results

1

Hint, Fhit, and GalT: function, structure, evolution, and mechanism of three branches of the histidine triad superfamily of nucleotide hydrolases and transferases.

Brenner C. Brenner C. Biochemistry. 2002 Jul 23;41(29):9003-14. doi: 10.1021/bi025942q. Biochemistry. 2002. PMID: 12119013 Free PMC article.

2

Crystal structures of HINT demonstrate that histidine triad proteins are GalT-related nucleotide-binding proteins.

Brenner C, Garrison P, Gilmour J, Peisach D, Ringe D, Petsko GA, Lowenstein JM. Brenner C, et al. Nat Struct Biol. 1997 Mar;4(3):231-8. doi: 10.1038/nsb0397-231. Nat Struct Biol. 1997. PMID: 9164465 Free PMC article.

3

The histidine triad superfamily of nucleotide-binding proteins.

Brenner C, Bieganowski P, Pace HC, Huebner K. Brenner C, et al. J Cell Physiol. 1999 Nov;181(2):179-87. doi: 10.1002/(SICI)1097-4652(199911)181:2<179::AID-JCP1>3.0.CO;2-8. J Cell Physiol. 1999. PMID: 10497298 Free PMC article. Review.

4

Designed FHIT alleles establish that Fhit-induced apoptosis in cancer cells is limited by substrate binding.

Trapasso F, Krakowiak A, Cesari R, Arkles J, Yendamuri S, Ishii H, Vecchione A, Kuroki T, Bieganowski P, Pace HC, Huebner K, Croce CM, Brenner C. Trapasso F, et al. Among authors: brenner c. Proc Natl Acad Sci U S A. 2003 Feb 18;100(4):1592-7. doi: 10.1073/pnas.0437915100. Epub 2003 Feb 6. Proc Natl Acad Sci U S A. 2003. PMID: 12574506 Free PMC article.

5

Scaffolding functions of arrestin-2 revealed by crystal structure and mutagenesis.

Milano SK, Pace HC, Kim YM, Brenner C, Benovic JL. Milano SK, et al. Among authors: brenner c. Biochemistry. 2002 Mar 12;41(10):3321-8. doi: 10.1021/bi015905j. Biochemistry. 2002. PMID: 11876640

6

Fhit-nucleotide specificity probed with novel fluorescent and fluorogenic substrates.

Draganescu A, Hodawadekar SC, Gee KR, Brenner C. Draganescu A, et al. Among authors: brenner c. J Biol Chem. 2000 Feb 18;275(7):4555-60. doi: 10.1074/jbc.275.7.4555. J Biol Chem. 2000. PMID: 10671479 Free PMC article.

7

Crystal structure of the worm NitFhit Rosetta Stone protein reveals a Nit tetramer binding two Fhit dimers.

Pace HC, Hodawadekar SC, Draganescu A, Huang J, Bieganowski P, Pekarsky Y, Croce CM, Brenner C. Pace HC, et al. Among authors: brenner c. Curr Biol. 2000 Jul 27-Aug 10;10(15):907-17. doi: 10.1016/s0960-9822(00)00621-7. Curr Biol. 2000. PMID: 10959838 Free article.

8

The nitrilase superfamily: classification, structure and function.

Pace HC, Brenner C. Pace HC, et al. Among authors: brenner c. Genome Biol. 2001;2(1):REVIEWS0001. doi: 10.1186/gb-2001-2-1-reviews0001. Epub 2001 Jan 15. Genome Biol. 2001. PMID: 11380987 Free PMC article. Review.

9

Purification and crystallization of complexes modeling the active state of the fragile histidine triad protein.

Brenner C, Pace HC, Garrison PN, Robinson AK, Rosler A, Liu XH, Blackburn GM, Croce CM, Huebner K, Barnes LD. Brenner C, et al. Protein Eng. 1997 Dec;10(12):1461-3. doi: 10.1093/protein/10.12.1461. Protein Eng. 1997. PMID: 9543008 Free PMC article.

10

Genetic, biochemical, and crystallographic characterization of Fhit-substrate complexes as the active signaling form of Fhit.

Pace HC, Garrison PN, Robinson AK, Barnes LD, Draganescu A, Rösler A, Blackburn GM, Siprashvili Z, Croce CM, Huebner K, Brenner C. Pace HC, et al. Among authors: brenner c. Proc Natl Acad Sci U S A. 1998 May 12;95(10):5484-9. doi: 10.1073/pnas.95.10.5484. Proc Natl Acad Sci U S A. 1998. PMID: 9576908 Free PMC article.

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