Year |
Citation |
Score |
2016 |
Kim JH, Schlebach JP, Lu Z, Peng D, Reasoner KC, Sanders CR. A pH-Mediated Topological Switch within the N-Terminal Domain of Human Caveolin-3. Biophysical Journal. 110: 2475-2485. PMID 27276265 DOI: 10.1016/J.Bpj.2016.05.004 |
0.303 |
|
2015 |
Wu J, Peng D, Zhang Y, Lu Z, Voehler M, Sanders CR, Li J. Biophysical characterization of interactions between the C-termini of peripheral nerve claudins and the PDZ₁ domain of zonula occludens. Biochemical and Biophysical Research Communications. 459: 87-93. PMID 25712527 DOI: 10.1016/J.Bbrc.2015.02.075 |
0.327 |
|
2014 |
Collier SE, Voehler M, Peng D, Ohi R, Gould KL, Reiter NJ, Ohi MD. Structural and functional insights into the N-terminus of Schizosaccharomyces pombe Cdc5. Biochemistry. 53: 6439-51. PMID 25263959 DOI: 10.1021/Bi5008639 |
0.312 |
|
2014 |
Kim JH, Peng D, Schlebach JP, Hadziselimovic A, Sanders CR. Modest effects of lipid modifications on the structure of caveolin-3. Biochemistry. 53: 4320-2. PMID 24960539 DOI: 10.1021/Bi5005238 |
0.353 |
|
2014 |
Peng D, Kim JH, Kroncke BM, Law CL, Xia Y, Droege KD, Van Horn WD, Vanoye CG, Sanders CR. Purification and structural study of the voltage-sensor domain of the human KCNQ1 potassium ion channel. Biochemistry. 53: 2032-42. PMID 24606221 DOI: 10.1021/Bi500102W |
0.338 |
|
2014 |
Collier SE, Peng D, Voehler M, Reiter N, Ohi M. Characterizing the Structure and Function of the N-Terminus of Schizosaccharomyces Pombe Cdc5, a Pre-Mrna Splicing Factor Biophysical Journal. 106: 429a. DOI: 10.1016/J.Bpj.2013.11.2417 |
0.349 |
|
2013 |
Wu J, Peng D, Voehler M, Sanders CR, Li J. Structure and expression of a novel compact myelin protein - small VCP-interacting protein (SVIP). Biochemical and Biophysical Research Communications. 440: 173-8. PMID 24055875 DOI: 10.1016/J.Bbrc.2013.09.056 |
0.31 |
|
2013 |
Schlebach JP, Peng D, Kroncke BM, Mittendorf KF, Narayan M, Carter BD, Sanders CR. Reversible folding of human peripheral myelin protein 22, a tetraspan membrane protein. Biochemistry. 52: 3229-41. PMID 23639031 DOI: 10.1021/Bi301635F |
0.301 |
|
2013 |
Peng D, Ogura H, Ma LH, Evans JP, de Montellano PR, La Mar GN. Solution NMR characterization of magnetic/electronic properties of azide and cyanide-inhibited substrate complexes of human heme oxygenase: implications for steric ligand tilt. Journal of Inorganic Biochemistry. 121: 179-86. PMID 23391487 DOI: 10.1016/J.Jinorgbio.2013.01.004 |
0.575 |
|
2013 |
Barrett PJ, Chen J, Cho MK, Kim JH, Lu Z, Mathew S, Peng D, Song Y, Van Horn WD, Zhuang T, Sönnichsen FD, Sanders CR. The quiet renaissance of protein nuclear magnetic resonance. Biochemistry. 52: 1303-20. PMID 23368985 DOI: 10.1021/Bi4000436 |
0.307 |
|
2012 |
Peng D, Ma LH, Smith KM, Zhang X, Sato M, La Mar GN. Role of propionates in substrate binding to heme oxygenase from Neisseria meningitidis: a nuclear magnetic resonance study. Biochemistry. 51: 7054-63. PMID 22913621 DOI: 10.1021/Bi3007803 |
0.583 |
|
2011 |
Peng D, Satterlee JD, Ma LH, Dallas JL, Smith KM, Zhang X, Sato M, La Mar GN. Influence of substrate modification and C-terminal truncation on the active site structure of substrate-bound heme oxygenase from Neisseriae meningitidis. A 1H NMR study. Biochemistry. 50: 8823-33. PMID 21870860 DOI: 10.1021/Bi200978G |
0.572 |
|
2010 |
Peng D, Ma LH, Ogura H, Yang EC, Zhang X, Yoshida T, La Mar GN. 1H NMR study of the influence of mutation on the interaction of the C-terminus with the active site in heme oxygenase from Neisseria meningitidis: implications for product release. Biochemistry. 49: 5832-40. PMID 20540495 DOI: 10.1021/Bi1000867 |
0.569 |
|
2009 |
Peng D, Ogura H, Zhu W, Ma LH, Evans JP, Ortiz de Montellano PR, La Mar GN. Coupling of the distal hydrogen bond network to the exogenous ligand in substrate-bound, resting state human heme oxygenase. Biochemistry. 48: 11231-42. PMID 19842713 DOI: 10.1021/Bi901216S |
0.538 |
|
2009 |
Ogura H, Evans JP, Peng D, Satterlee JD, Ortiz de Montellano PR, La Mar GN. The orbital ground state of the azide-substrate complex of human heme oxygenase is an indicator of distal H-bonding: implications for the enzyme mechanism. Biochemistry. 48: 3127-37. PMID 19243105 DOI: 10.1021/Bi802360G |
0.547 |
|
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