| Year |
Citation |
Score |
| 2011 |
Schmidt A, Teeter M, Weckert E, Lamzin VS. Crystal structure of small protein crambin at 0.48 Å resolution. Acta Crystallographica Section F-Structural Biology and Crystallization Communications. 67: 424-428. PMID 21505232 DOI: 10.1107/S1744309110052607 |
0.448 |
|
| 2005 |
Johnson KA, Kim E, Teeter MM, Suh SW, Stec B. Crystal structure of alpha-hordothionin at 1.9 Angstrom resolution. Febs Letters. 579: 2301-6. PMID 15848162 DOI: 10.1016/J.Febslet.2004.12.100 |
0.359 |
|
| 2005 |
Stec B, Markman O, Rao U, Heffron G, Henderson S, Vernon LP, Brumfeld V, Teeter MM. Proposal for molecular mechanism of thionins deduced from physico-chemical studies of plant toxins. The Journal of Peptide Research : Official Journal of the American Peptide Society. 64: 210-24. PMID 15613085 DOI: 10.1111/J.1399-3011.2004.00187.X |
0.654 |
|
| 2005 |
Rao U, Stec B, Teeter MM. Refinement of purothionins reveals solute particles important for lattice formation and toxicity. Part 1: alpha1-purothionin revisited. Acta Crystallographica. Section D, Biological Crystallography. 51: 904-13. PMID 15299760 DOI: 10.1107/S0907444995002964 |
0.307 |
|
| 2004 |
Teeter MM. Myoglobin cavities provide interior ligand pathway. Protein Science : a Publication of the Protein Society. 13: 313-8. PMID 14739317 DOI: 10.1110/ps.03334304 |
0.367 |
|
| 2001 |
Teeter MM, Yamano A, Stec B, Mohanty U. On the nature of a glassy state of matter in a hydrated protein: Relation to protein function. Proceedings of the National Academy of Sciences of the United States of America. 98: 11242-7. PMID 11572978 DOI: 10.1073/Pnas.201404398 |
0.373 |
|
| 2001 |
Neve KA, Cumbay MG, Thompson KR, Yang R, Buck DC, Watts VJ, DuRand CJ, Teeter MM. Modeling and mutational analysis of a putative sodium-binding pocket on the dopamine D2 receptor. Molecular Pharmacology. 60: 373-81. PMID 11455025 DOI: 10.1124/Mol.60.2.373 |
0.338 |
|
| 2000 |
Jelsch C, Teeter MM, Lamzin V, Pichon-Pesme V, Blessing RH, Lecomte C. Accurate protein crystallography at ultra-high resolution: valence electron distribution in crambin. Proceedings of the National Academy of Sciences of the United States of America. 97: 3171-3176. PMID 10737790 DOI: 10.1073/Pnas.97.7.3171 |
0.386 |
|
| 1999 |
Lamzin VS, Morris RJ, Dauter Z, Wilson KS, Teeter MM. Experimental observation of bonding electrons in proteins Journal of Biological Chemistry. 274: 20753-20755. PMID 10409612 DOI: 10.1074/Jbc.274.30.20753 |
0.436 |
|
| 1999 |
Stec B, Troxler RF, Teeter MM. Crystal structure of C-phycocyanin from Cyanidium caldarium provides a new perspective on phycobilisome assembly. Biophysical Journal. 76: 2912-2921. PMID 10354419 DOI: 10.1016/S0006-3495(99)77446-1 |
0.471 |
|
| 1997 |
Stec B, Yamano A, Whitlow M, Teeter MM. Structure of human plasminogen kringle 4 at 1.68 a and 277 K. A possible structural role of disordered residues. Acta Crystallographica Section D-Biological Crystallography. 53: 169-178. PMID 15299951 DOI: 10.1107/S0907444996012267 |
0.455 |
|
| 1997 |
Yamano A, Heo NH, Teeter MM. Crystal structure of Ser-22/Ile-25 form crambin confirms solvent, side chain substate correlations Journal of Biological Chemistry. 272: 9597-9600. PMID 9092482 DOI: 10.1074/Jbc.272.15.9597 |
0.698 |
|
| 1996 |
Lobb L, Stec B, Kantrowitz EK, Yamano A, Stojanoff V, Markman O, Teeter MM. Expression, purification and characterization of recombinant crambin. Protein Engineering. 9: 1233-9. PMID 9010938 DOI: 10.1093/Protein/9.12.1233 |
0.641 |
|
| 1996 |
Markman O, Roh C, Roberts MF, Teeter MM. Designed additives for controlled growth of crystals of phospholipid interacting proteins: Short chain phospholipids Journal of Crystal Growth. 160: 382-388. DOI: 10.1016/0022-0248(95)00745-8 |
0.675 |
|
| 1995 |
Stec B, Zhou R, Teeter MM. Full-matrix refinement of the protein crambin at 0.83 A and 130 K. Acta Crystallographica Section D-Biological Crystallography. 51: 663-681. PMID 15299796 DOI: 10.1107/S0907444994014484 |
0.425 |
|
| 1995 |
Stec B, Rao U, Teeter MM. Refinement of purothionins reveals solute particles important for lattice formation and toxicity. Part 2: structure of beta-purothionin at 1.7 A resolution. Acta Crystallographica Section D-Biological Crystallography. 51: 914-924. PMID 15299761 DOI: 10.1107/S0907444995002976 |
0.369 |
|
| 1994 |
Teeter MM, Froimowitz M, Stec B, DuRand CJ. Homology modeling of the dopamine D2 receptor and its testing by docking of agonists and tricyclic antagonists. Journal of Medicinal Chemistry. 37: 2874-2888. PMID 7915325 DOI: 10.1021/Jm00044A008 |
0.355 |
|
| 1994 |
Yamano A, Teeter MM. Correlated disorder of the pure Pro22/Leu25 form of crambin at 150 K refined to 1.05-A resolution. Journal of Biological Chemistry. 269: 13956-13965. DOI: 10.2210/Pdb1Cnr/Pdb |
0.696 |
|
| 1993 |
Teeter MM, Roe SM, Heo NH. Atomic resolution (0.83 A) crystal structure of the hydrophobic protein crambin at 130 K. Journal of Molecular Biology. 230: 292-311. PMID 8450543 DOI: 10.1006/Jmbi.1993.1143 |
0.499 |
|
| 1993 |
Roe SM, Teeter MM. Patterns for prediction of hydration around polar residues in proteins. Journal of Molecular Biology. 229: 419-27. PMID 8381492 DOI: 10.1006/Jmbi.1993.1043 |
0.386 |
|
| 1992 |
Rao U, Teeter MM, Erickson-Viitanen S, DeGrado WF. Calmodulin binding to alpha 1-purothionin: solution binding and modeling of the complex. Proteins. 14: 127-38. PMID 1409564 DOI: 10.1002/Prot.340140202 |
0.344 |
|
| 1992 |
Kim T, Kwon S, Kim Y, Ho Heo N, Teeter MM, Yamano A. Synthesis and characterization of various coordination modes of 1,1′-bis(diphenylphosphino)ferrocene in iron carbonyl complexes. X-Ray crystal structures of (η-BPPF)Fe(CO)4, (μ,η 2-BPPF)(Fe(CO)4)2, and (μ,η2-BPPF)Fe3(CO)10 Journal of Organometallic Chemistry. 426: 71-86. DOI: 10.1016/0022-328X(92)83162-B |
0.629 |
|
| 1990 |
Teeter MM, Ma X, Rao U, Whitlow M. Crystal structure of a protein-toxin alpha 1-purothionin at 2.5A and a comparison with predicted models. Proteins. 8: 118-132. PMID 2235992 DOI: 10.1002/Prot.340080203 |
0.377 |
|
| 1989 |
Lii J, Gallion S, Bender C, Wikström H, Allinger NL, Flurchick KM, Teeter MM. Molecular mechanics (MM2) calculations on peptides and on the protein Crambin using the CYBER 205 Journal of Computational Chemistry. 10: 503-513. DOI: 10.1002/Jcc.540100408 |
0.433 |
|
| 1988 |
Teeter MM, Whitlow M. Test of circular dichroism (CD) methods for crambin and CD-assisted secondary structure prediction of its homologous toxins Proteins. 4: 262-273. PMID 3253736 DOI: 10.1002/Prot.340040405 |
0.386 |
|
| 1988 |
Loechler EL, Teeter MM, Whitlow MD. Mapping the binding site of aflatoxin b1 in dna: Molecular modeling of the binding sites for the n(7)-guanine adduct of aflatoxinb1 in different dna sequences Journal of Biomolecular Structure and Dynamics. 5: 1237-1257. PMID 3152159 DOI: 10.1080/07391102.1988.10506467 |
0.327 |
|
| 1987 |
Brünger AT, Campbell RL, Clore GM, Gronenborn AM, Karplus M, Petsko GA, Teeter MM. Solution of a protein crystal structure with a model obtained from NMR interproton distance restraints. Science (New York, N.Y.). 235: 1049-53. PMID 17782253 DOI: 10.1126/Science.235.4792.1049 |
0.445 |
|
| 1987 |
Clore GM, Sukumaran DK, Gronenborn AM, Teeter MM, Whitlow M, Jones BL. Nuclear magnetic resonance study of the solution structure of alpha 1-purothionin. Sequential resonance assignment, secondary structure and low resolution tertiary structure. Journal of Molecular Biology. 193: 571-8. PMID 3586031 DOI: 10.1016/0022-2836(87)90267-1 |
0.337 |
|
| 1986 |
Teeter MM, Hope H. Progress in the Water Structure of the Protein Crambin by X-Ray Diffraction at 140 Ka Annals of the New York Academy of Sciences. 482: 163-165. DOI: 10.1111/J.1749-6632.1986.Tb20947.X |
0.4 |
|
| 1986 |
Whitlow M, Teeter MM. An empirical examination of potential energy minimization using the well-determined structure of the protein crambin Journal of the American Chemical Society. 108: 7163-7172. DOI: 10.1021/Ja00283A005 |
0.373 |
|
| 1985 |
Whitlow M, Teeter MM. Energy Minimization for Tertiary Structure Prediction of Homologous Proteins: α1-purothionin and Viscotoxin A3 Models from Crambin Journal of Biomolecular Structure & Dynamics. 2: 831-848. PMID 3917120 DOI: 10.1080/07391102.1985.10506327 |
0.446 |
|
| 1984 |
Wallace BA, Kohl N, Teeter MM. Crambin in phospholipid vesicles: Circular dichroism analysis of crystal structure relevance Proceedings of the National Academy of Sciences of the United States of America. 81: 1406-1410. PMID 16593429 DOI: 10.1073/Pnas.81.5.1406 |
0.544 |
|
| 1984 |
Williams RW, Teeter MM. Raman spectroscopy of homologous plant toxins: Crambin and α1 and β-purothionin secondary structures, disulfide conformation, and tyrosine environment Biochemistry. 23: 6796-6802. PMID 6549379 DOI: 10.1021/Bi00321A080 |
0.402 |
|
| 1984 |
Teeter MM. Structural analysis of the protein crambin from X-ray diffraction studies at 0.945 Å Acta Crystallographica Section a Foundations of Crystallography. 40: C55-C55. DOI: 10.1107/S0108767384098111 |
0.331 |
|
| 1981 |
Hendrickson WA, Teeter MM. Structure of the hydrophobic protein crambin determined directly from the anomalous scattering of sulphur. Nature. 290: 107-113. PMID 28769131 DOI: 10.1038/290107A0 |
0.65 |
|
| 1981 |
Teeter MM. Water structure of a hydrophobic protein at atomic resolution: Pentagon rings of water molecules in crystals of crambin. Proceedings of the National Academy of Sciences of the United States of America. 81: 6014-6018. PMID 16593516 DOI: 10.1073/Pnas.81.19.6014 |
0.395 |
|
| 1981 |
Teeter MM, Mazer JA, L'Italien JJ. Primary structure of the hydrophobic plant protein crambin. Biochemistry. 20: 5437-43. PMID 6895315 DOI: 10.1021/Bi00522A013 |
0.46 |
|
| 1979 |
Teeter MM, Hendrickson WA. Highly ordered crystals of the plant seed protein crambin. Journal of Molecular Biology. 127: 219-223. PMID 430565 DOI: 10.1016/0022-2836(79)90242-0 |
0.644 |
|
| 1979 |
Rich A, Quigley GJ, Teeter MM, Ducruix A, Woo N. Recent Progress in tRNA Structural Analysis Cold Spring Harbor Monograph Archive. 101-113. DOI: 10.1101/087969128.9A.101 |
0.535 |
|
| 1978 |
Quigley GJ, Teeter MM, Rich A. Structural analysis of spermine and magnesium ion binding to yeast phenylalanine transfer RNA. Proceedings of the National Academy of Sciences of the United States of America. 75: 64-8. PMID 343112 DOI: 10.1073/Pnas.75.1.64 |
0.5 |
|
| 1976 |
Allcock HR, Allen RW, Bissell EC, Smeltz LA, Teeter M. Phosphorus-nitrogen compounds. 26. Molecular motion and molecular separations in cyclophosphazene clathrates Journal of the American Chemical Society. 98: 5120-5125. DOI: 10.1021/Ja00433A012 |
0.334 |
|
| 1976 |
ALLCOCK HR, ALLEN RW, BISSELL EC, SMELTZ LA, TEETER M. ChemInform Abstract: PHOSPHORUS-NITROGEN COMPOUNDS. 26. MOLECULAR MOTION AND MOLECULAR SEPARATIONS S IN CYCLOPHOSPHAZENE CLATHRATES Chemischer Informationsdienst. 7: no-no. DOI: 10.1002/chin.197646285 |
0.336 |
|
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