Tony A. Klink - Publications

Affiliations: 
2000 Department of Biochemistry University of Wisconsin, Madison, Madison, WI 

7 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2001 Park C, Kelemen BR, Klink TA, Sweeney RY, Behlke MA, Eubanks SR, Raines RT. Fast, facile, hypersensitive assays for ribonucleolytic activity. Methods in Enzymology. 341: 81-94. PMID 11582813 DOI: 10.1016/S0076-6879(01)41146-3  0.591
2001 Klink TA, Vicentini AM, Hofsteenge J, Raines RT. High-level soluble production and characterization of porcine ribonuclease inhibitor. Protein Expression and Purification. 22: 174-9. PMID 11437592 DOI: 10.1006/Prep.2001.1422  0.492
2000 Ruoppolo M, Vinci F, Klink TA, Raines RT, Marino G. Contribution of individual disulfide bonds to the oxidative folding of ribonuclease A. Biochemistry. 39: 12033-42. PMID 11009618 DOI: 10.1021/Bi001044N  0.417
2000 Klink TA, Raines RT. Conformational stability is a determinant of ribonuclease A cytotoxicity. The Journal of Biological Chemistry. 275: 17463-7. PMID 10747991 DOI: 10.1074/Jbc.M001132200  0.459
2000 Klink TA, Woycechowsky KJ, Taylor KM, Raines RT. Contribution of disulfide bonds to the conformational stability and catalytic activity of ribonuclease A. European Journal of Biochemistry / Febs. 267: 566-72. PMID 10632727 DOI: 10.1046/J.1432-1327.2000.01037.X  0.63
1999 Kelemen BR, Klink TA, Behlke MA, Eubanks SR, Leland PA, Raines RT. Hypersensitive substrate for ribonucleases. Nucleic Acids Research. 27: 3696-701. PMID 10471739 DOI: 10.1093/Nar/27.18.3696  0.472
1998 Schultz LW, Hargraves SR, Klink TA, Raines RT. Structure and stability of the P93G variant of ribonuclease A. Protein Science : a Publication of the Protein Society. 7: 1620-5. PMID 9684895 DOI: 10.1002/Pro.5560070716  0.56
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