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Your search keyword '"Turk, Benjamin E."' showing total 7 results
Start Over Author "Turk, Benjamin E." Journal biochemistry
7 results on '"Turk, Benjamin E."'

3. MMP-20 is predominately a tooth-specific enzyme with a deep catalytic pocket that hydrolyzes type V collagen

Author

Turk, Benjamin E., Lee, Daniel H., Yamakoshi, Yasuo, Klingenhoff, Andreas, Reichenberger, Ernst, Wright, J. Timothy, Simmer, James P., Komisarof, Justin A., Cantley, Lewis C., and Bartlett, John D.

Subjects
Collagen -- Properties, Proteolysis -- Analysis, Rats as laboratory animals -- Physiological aspects, Rats as laboratory animals -- Research, Biological sciences, Chemistry
Abstract

A systematic mouse tissue expression screen is performed, to identify other tissues that might express matrix metalloproteinase-20 (MMP-20). On the basis of the matrices derived from the peptide library data, it was identified and then confirmed that type V collagen is an MMP-20 substrate.

Published
2006

4. In SilicoDesign and in VitroCharacterization of Universal Tyrosine Kinase Peptide Substrates

Author

Marholz, Laura J., Zeringo, Nicholas A., Lou, Hua Jane, Turk, Benjamin E., and Parker, Laurie L.

Abstract

A majority of the 90 human protein tyrosine kinases (PTKs) are understudied “orphan” enzymes with few or no known substrates. Designing experiments aimed at assaying the catalytic activity of these PTKs has been a long-running problem. In the past, researchers have used polypeptides with a randomized 4:1 molar ratio of glutamic acid to tyrosine as general PTK substrates. However, these substrates are inefficient and perform poorly for many applications. In this work, we apply the KINATEST-ID pipeline for artificial kinase substrate discovery to design a set of candidate “universal” PTK peptide substrate sequences. We identified two unique peptide sequences from this set that had robust activity with a panel of 15 PTKs tested in an initial screen. Kinetic characterization with seven receptor and nonreceptor PTKs confirmed these peptides to be efficient and general PTK substrates. The broad scope of these artificial substrates demonstrates that they should be useful as tools for probing understudied PTK activity.

Published
2024
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6. Defining the Substrate Specificity Determinants Recognized by the Active Site of C-Terminal Src Kinase-Homologous Kinase (CHK) and Identification of β-Synuclein as a Potential CHK Physiological Substrate

Author

Ia, Kim K., primary, Jeschke, Grace R., additional, Deng, Yang, additional, Kamaruddin, Mohd Aizuddin, additional, Williamson, Nicholas A., additional, Scanlon, Denis B., additional, Culvenor, Janetta G., additional, Hossain, Mohammed Iqbal, additional, Purcell, Anthony W., additional, Liu, Sheng, additional, Zhu, Hong-Jian, additional, Catimel, Bruno, additional, Turk, Benjamin E., additional, and Cheng, Heung-Chin, additional

Published
2011
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