| Year |
Citation |
Score |
| 2015 |
Oktaviani NA, Risør MW, Lee YH, Megens RP, de Jong DH, Otten R, Scheek RM, Enghild JJ, Nielsen NC, Ikegami T, Mulder FA. Optimized co-solute paramagnetic relaxation enhancement for the rapid NMR analysis of a highly fibrillogenic peptide. Journal of Biomolecular Nmr. 62: 129-42. PMID 25820763 DOI: 10.1007/S10858-015-9925-8 |
0.324 |
|
| 2013 |
Mulder F, Scheek R. Multidimensional NMR spectroscopy Springer Us. 1637-1646. DOI: 10.1007/9783642167126 |
0.346 |
|
| 2012 |
Oktaviani NA, Pool TJ, Kamikubo H, Slager J, Scheek RM, Kataoka M, Mulder FA. Comprehensive determination of protein tyrosine pKa values for photoactive yellow protein using indirect 13C NMR spectroscopy. Biophysical Journal. 102: 579-86. PMID 22325281 DOI: 10.1016/J.Bpj.2011.12.024 |
0.366 |
|
| 2012 |
Wood K, Paz A, Dijkstra K, Scheek RM, Otten R, Silman I, Sussman JL, Mulder FA. Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3. Biomolecular Nmr Assignments. 6: 15-8. PMID 21647611 DOI: 10.1007/S12104-011-9315-4 |
0.329 |
|
| 2011 |
Mulder FA, Otten R, Scheek RM. Origin and removal of mixed-phase artifacts in gradient sensitivity enhanced heteronuclear single quantum correlation spectra. Journal of Biomolecular Nmr. 51: 199-207. PMID 21947928 DOI: 10.1007/S10858-011-9554-9 |
0.31 |
|
| 2011 |
Oktaviani NA, Otten R, Dijkstra K, Scheek RM, Thulin E, Akke M, Mulder FA. 100% complete assignment of non-labile (1)H, (13)C, and (15)N signals for calcium-loaded Calbindin D(9k) P43G. Biomolecular Nmr Assignments. 5: 79-84. PMID 21069485 DOI: 10.1007/S12104-010-9272-3 |
0.3 |
|
| 2007 |
de Vries B, Kiel JAKW, Scheek R, Veenhuis M, van der Klei IJ. A conserved alpha helical domain at the N-terminus of Pex14p is required for PTS1 and PTS2 protein import in Hansenula polymorpha Febs Letters. 581: 5627-5634. PMID 18023285 DOI: 10.1016/J.Febslet.2007.11.012 |
0.32 |
|
| 2005 |
Haas PJ, de Haas CJ, Poppelier MJ, van Kessel KP, van Strijp JA, Dijkstra K, Scheek RM, Fan H, Kruijtzer JA, Liskamp RM, Kemmink J. The structure of the C5a receptor-blocking domain of chemotaxis inhibitory protein of Staphylococcus aureus is related to a group of immune evasive molecules. Journal of Molecular Biology. 353: 859-72. PMID 16213522 DOI: 10.1016/J.Jmb.2005.09.014 |
0.372 |
|
| 2005 |
Veldhuis G, Broos J, Poolman B, Scheek RM. Stoichiometry and substrate affinity of the mannitol transporter, EnzymeIImtl, from Escherichia coli. Biophysical Journal. 89: 201-10. PMID 15879478 DOI: 10.1529/Biophysj.105.062877 |
0.328 |
|
| 2004 |
Otten R, van Lune FS, Dijkstra K, Scheek RM. 1H, 13C, and 15N resonance assignments of the phosphorylated enzyme IIB of the mannitol-specific phosphoenolpyruvate-dependent phosphotransferase system of Escherichia coli. Journal of Biomolecular Nmr. 30: 461-2. PMID 15630568 DOI: 10.1007/S10858-004-3498-2 |
0.362 |
|
| 2004 |
Brokx RD, Scheek RM, Weljie AM, Vogel HJ. Backbone dynamic properties of the central linker region of calcium-calmodulin in 35% trifluoroethanol. Journal of Structural Biology. 146: 272-80. PMID 15099569 DOI: 10.1016/J.Jsb.2003.12.007 |
0.324 |
|
| 2003 |
Hess B, Scheek RM. Orientation restraints in molecular dynamics simulations using time and ensemble averaging. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 164: 19-27. PMID 12932451 DOI: 10.1016/S1090-7807(03)00178-2 |
0.346 |
|
| 2003 |
Canet D, Lyon CE, Scheek RM, Robillard GT, Dobson CM, Hore PJ, van Nuland NA. Rapid formation of non-native contacts during the folding of HPr revealed by real-time photo-CIDNP NMR and stopped-flow fluorescence experiments. Journal of Molecular Biology. 330: 397-407. PMID 12823977 DOI: 10.1016/S0022-2836(03)00507-2 |
0.374 |
|
| 2003 |
Azuaga AI, Canet D, Smeenk G, Berends R, Titgemeijer F, Duurkens R, Mateo PL, Scheek RM, Robillard GT, Dobson CM, van Nuland NA. Characterization of single-tryptophan mutants of histidine-containing phosphocarrier protein: evidence for local rearrangements during folding from high concentrations of denaturant. Biochemistry. 42: 4883-95. PMID 12718529 DOI: 10.1021/Bi027182P |
0.343 |
|
| 2002 |
Feenstra KA, Peter C, Scheek RM, van Gunsteren WF, Mark AE. A comparison of methods for calculating NMR cross-relaxation rates (NOESY and ROESY intensities) in small peptides. Journal of Biomolecular Nmr. 23: 181-94. PMID 12238590 DOI: 10.1023/A:1019854626147 |
0.326 |
|
| 2002 |
van Lune F, Manning L, Dijkstra K, Berendsen HJ, Scheek RM. Order-parameter tensor description of HPr in a medium of oriented bicelles. Journal of Biomolecular Nmr. 23: 169-79. PMID 12238589 DOI: 10.1023/A:1019877830921 |
0.317 |
|
| 2002 |
Odaert B, Landrieu I, Dijkstra K, Schuurman-Wolters G, Casteels P, Wieruszeski JM, Scheek R, Lippens G. Assignment of the 1H, 13C and 15N resonances and secondary structure of the monomeric p13suc1 protein of Saccharomyces pombe [3] Journal of Biomolecular Nmr. 23: 155-156. PMID 12153042 DOI: 10.1023/A:1016316107468 |
0.39 |
|
| 2002 |
Odaert B, Landrieu I, Dijkstra K, Schuurman-Wolters G, Casteels P, Wieruszeski JM, Inzé D, Scheek R, Lippens G. Solution NMR study of the monomeric form of p13suc1 protein sheds light on the hinge region determining the affinity for a phosphorylated substrate Journal of Biological Chemistry. 277: 12375-12381. PMID 11812792 DOI: 10.1074/Jbc.M111741200 |
0.389 |
|
| 2001 |
Ab E, Schuurman-Wolters GK, Nijlant D, Dijkstra K, Saier MH, Robillard GT, Scheek RM. NMR structure of cysteinyl-phosphorylated enzyme IIB of the N,N'-diacetylchitobiose-specific phosphoenolpyruvate-dependent phosphotransferase system of Escherichia coli. Journal of Molecular Biology. 308: 993-1009. PMID 11352587 DOI: 10.1006/Jmbi.2001.4623 |
0.432 |
|
| 1999 |
Dijkstra K, Karvonen P, Pirneskoski A, Koivunen P, Kivirikko KI, Darby NJ, van Straaten M, Scheek RM, Kemmink J. Assignment of 1H, 13C and 15N resonances of the a' domain of protein disulfide isomerase. Journal of Biomolecular Nmr. 14: 195-6. PMID 10427749 DOI: 10.1023/A:1008331225208 |
0.378 |
|
| 1999 |
Kemmink J, Dijkstra K, Mariani M, Scheek RM, Penka E, Nilges M, Darby NJ. The structure in solution of the b domain of protein disulfide isomerase. Journal of Biomolecular Nmr. 13: 357-68. PMID 10383197 DOI: 10.1023/A:1008341820489 |
0.347 |
|
| 1998 |
Meijberg W, Schuurman-Wolters GK, Boer H, Scheek RM, Robillard GT. The thermal stability and domain interactions of the mannitol permease of Escherichia coli. A differential scanning calorimetry study. The Journal of Biological Chemistry. 273: 20785-94. PMID 9694823 DOI: 10.1074/Jbc.273.33.20785 |
0.344 |
|
| 1998 |
Van Nuland NA, Meijberg W, Warner J, Forge V, Scheek RM, Robillard GT, Dobson CM. Slow cooperative folding of a small globular protein HPr. Biochemistry. 37: 622-37. PMID 9425085 DOI: 10.1021/Bi9717946 |
0.31 |
|
| 1997 |
de Groot BL, van Aalten DM, Scheek RM, Amadei A, Vriend G, Berendsen HJ. Prediction of protein conformational freedom from distance constraints. Proteins. 29: 240-51. PMID 9329088 DOI: 10.1002/(Sici)1097-0134(199710)29:2<240::Aid-Prot11>3.0.Co;2-O |
0.372 |
|
| 1997 |
Dijkstra K, Kroon GJA, Ab E, Scheek RM, Kemmink J. Correlation of the 15N(i + 1), 13Calpha(i), and 1Halpha(i) Backbone Resonances in 13C/15N-Labeled Proteins by the (CO)N(CO)CAH Experiment Journal of Magnetic Resonance (San Diego, Calif. : 1997). 125: 149-52. PMID 9245371 DOI: 10.1006/Jmre.1996.1096 |
0.318 |
|
| 1997 |
Ab E, Schuurman-Wolters G, Reizer J, Saier MH, Dijkstra K, Scheek RM, Robillard GT. The NMR side-chain assignments and solution structure of enzyme IIBcellobiose of the phosphoenolpyruvate-dependent phosphotransferase system of Escherichia coli. Protein Science : a Publication of the Protein Society. 6: 304-14. PMID 9041631 DOI: 10.1002/Pro.5560060205 |
0.42 |
|
| 1996 |
de Groot BL, Amadei A, Scheek RM, van Nuland NA, Berendsen HJ. An extended sampling of the configurational space of HPr from E. coli. Proteins. 26: 314-22. PMID 8953652 DOI: 10.1002/(Sici)1097-0134(199611)26:3<314::Aid-Prot7>3.0.Co;2-D |
0.313 |
|
| 1995 |
Scheek RM, van Nuland NA, de Groot BL, Amadei A. Structure from NMR and molecular dynamics: Distance restraining inhibits motion in the essential subspace. Journal of Biomolecular Nmr. 6: 106-11. PMID 22911579 DOI: 10.1007/Bf00417496 |
0.345 |
|
| 1995 |
Kemmink J, Darby NJ, Dijkstra K, Scheek RM, Creighton TE. Nuclear magnetic resonance characterization of the N-terminal thioredoxin-like domain of protein disulfide isomerase. Protein Science : a Publication of the Protein Society. 4: 2587-93. PMID 8580850 DOI: 10.1002/Pro.5560041216 |
0.388 |
|
| 1995 |
van Nuland NA, Boelens R, Scheek RM, Robillard GT. High-resolution structure of the phosphorylated form of the histidine-containing phosphocarrier protein HPr from Escherichia coli determined by restrained molecular dynamics from NMR-NOE data. Journal of Molecular Biology. 246: 180-93. PMID 7853396 DOI: 10.1006/Jmbi.1994.0075 |
0.426 |
|
| 1995 |
Kemmink J, Scheek RM. Dynamic modelling of a helical peptide in solution using NMR data: multiple conformations and multi-spin effects. Journal of Biomolecular Nmr. 6: 33-40. PMID 7545042 DOI: 10.1007/Bf00417489 |
0.308 |
|
| 1994 |
van Nuland NA, Hangyi IW, van Schaik RC, Berendsen HJ, van Gunsteren WF, Scheek RM, Robillard GT. The high-resolution structure of the histidine-containing phosphocarrier protein HPr from Escherichia coli determined by restrained molecular dynamics from nuclear magnetic resonance nuclear Overhauser effect data. Journal of Molecular Biology. 237: 544-59. PMID 8158637 DOI: 10.1006/Jmbi.1994.1254 |
0.411 |
|
| 1994 |
Ab E, Schuurman-Wolters GK, Saier MH, Reizer J, Jacuinod M, Roepstorff P, Dijkstra K, Scheek RM, Robillard GT. Enzyme IIBcellobiose of the phosphoenol-pyruvate-dependent phosphotransferase system of Escherichia coli: backbone assignment and secondary structure determined by three-dimensional NMR spectroscopy. Protein Science : a Publication of the Protein Society. 3: 282-90. PMID 8003964 DOI: 10.1002/Pro.5560030212 |
0.395 |
|
| 1994 |
Dijkstra K, Kroon GJA, Vannuland NAJ, Scheek RM. The COCAH Experiment to Correlate Intraresidue Carbonyl, Cα, and Hα Resonances in Proteins Journal of Magnetic Resonance, Series A. 107: 102-105. DOI: 10.1006/Jmra.1994.1053 |
0.325 |
|
| 1993 |
van Nuland NA, Kroon GJ, Dijkstra K, Wolters GK, Scheek RM, Robillard GT. The NMR determination of the IIA(mtl) binding site on HPr of the Escherichia coli phosphoenol pyruvate-dependent phosphotransferase system. Febs Letters. 315: 11-5. PMID 8416803 DOI: 10.1016/0014-5793(93)81122-G |
0.381 |
|
| 1993 |
Kroon GJ, Grötzinger J, Dijkstra K, Scheek RM, Robillard GT. Backbone assignments and secondary structure of the Escherichia coli enzyme-II mannitol A domain determined by heteronuclear three-dimensional NMR spectroscopy. Protein Science : a Publication of the Protein Society. 2: 1331-41. PMID 8401218 DOI: 10.1002/Pro.5560020816 |
0.407 |
|
| 1993 |
Kemmink J, van Mierlo CP, Scheek RM, Creighton TE. Local structure due to an aromatic-amide interaction observed by 1H-nuclear magnetic resonance spectroscopy in peptides related to the N terminus of bovine pancreatic trypsin inhibitor. Journal of Molecular Biology. 230: 312-22. PMID 7680725 DOI: 10.1006/Jmbi.1993.1144 |
0.353 |
|
| 1992 |
van Nuland NA, van Dijk AA, Dijkstra K, van Hoesel FH, Scheek RM, Robillard GT. Three-dimensional 15N-1H-1H and 15N-13C-1H nuclear-magnetic resonance studies of HPr a central component of the phosphoenolpyruvate-dependent phosphotransferase system from Escherichia coli. Assignment of backbone resonances. European Journal of Biochemistry / Febs. 203: 483-91. PMID 1735433 DOI: 10.1111/J.1432-1033.1992.Tb16573.X |
0.388 |
|
| 1992 |
van Nuland NA, Grötzinger J, Dijkstra K, Scheek RM, Robillard GT. Determination of the three-dimensional solution structure of the histidine-containing phosphocarrier protein HPr from Escherichia coli using multidimensional NMR spectroscopy. European Journal of Biochemistry / Febs. 210: 881-91. PMID 1483471 DOI: 10.1111/J.1432-1033.1992.Tb17492.X |
0.408 |
|
| 1992 |
Van Dijk AA, Scheek RM, Dijkstra K, Wolters GK, Robillard GT. Characterization of the protonation and hydrogen bonding state of the histidine residues in IIAmtl, a domain of the phosphoenolpyruvate-dependent mannitol-specific transport protein. Biochemistry. 31: 9063-72. PMID 1390693 DOI: 10.1021/Bi00152A050 |
0.353 |
|
| 1990 |
Torda AE, Scheek RM, van Gunsteren WF. Time-averaged nuclear Overhauser effect distance restraints applied to tendamistat. Journal of Molecular Biology. 214: 223-35. PMID 2370663 DOI: 10.1016/0022-2836(90)90157-H |
0.333 |
|
| 1989 |
Ray BD, Scheek RM, Kemple MD, Prendergast FG, Nageswara Rao BD. Photochemically-induced dynamic nuclear polarization proton-NMR of aequorin discharged by calcium-independent light emission. European Journal of Biochemistry / Febs. 178: 705-9. PMID 2912730 DOI: 10.1111/J.1432-1033.1989.Tb14501.X |
0.348 |
|
| 1988 |
Basus VJ, Scheek RM. Structural studies of alpha-bungarotoxin. 2. 1H NMR assignments via an improved relayed coherence transfer nuclear overhauser enhancement experiment. Biochemistry. 27: 2772-5. PMID 3401448 DOI: 10.1021/Bi00408A017 |
0.374 |
|
| 1988 |
Pepermans H, Tourwé D, Van Binst G, Boelens R, Scheek RM, Van Gunsteren WF, Kaptein R. The combined use of NMR, distance geometry, and restrained molecular dynamics for the conformational study of a cyclic somatostatin analogue. Biopolymers. 27: 323-38. PMID 3359005 DOI: 10.1002/Bip.360270211 |
0.366 |
|
| 1988 |
Stob S, Scheek RM, Boelens R, Kaptein R. Photo-CIDNP study of the interaction between lac repressor headpiece and lac operator DNA. Febs Letters. 239: 99-104. PMID 3053247 DOI: 10.1016/0014-5793(88)80553-2 |
0.349 |
|
| 1988 |
de Vlieg J, Scheek RM, van Gunsteren WF, Berendsen HJ, Kaptein R, Thomason J. Combined procedure of distance geometry and restrained molecular dynamics techniques for protein structure determination from nuclear magnetic resonance data: application to the DNA binding domain of lac repressor from Escherichia coli. Proteins. 3: 209-18. PMID 3047742 DOI: 10.1002/Prot.340030402 |
0.394 |
|
| 1988 |
Stob S, Scheek RM, Boelens R, Dukstra K, Kaptein R. Applications of Two-Dimensional1H NMR Methods to Photo-Chemically Induced Dynamic Nuclear Polarisation Spectroscopy Israel Journal of Chemistry. 28: 319-327. DOI: 10.1002/Ijch.198800043 |
0.372 |
|
| 1987 |
Boelens R, Scheek RM, van Boom JH, Kaptein R. Complex of lac repressor headpiece with a 14 base-pair lac operator fragment studied by two-dimensional nuclear magnetic resonance. Journal of Molecular Biology. 193: 213-6. PMID 3586020 DOI: 10.1016/0022-2836(87)90638-3 |
0.365 |
|
| 1986 |
De Vlieg J, Boelens R, Scheek RM, Kaptein R, van Gunsteren WF. Restrained Molecular Dynamics Procedure for Protein Tertiary Structure Determination from NMR Data: ALacRepressor Headpiece Structure Based on Information on J-coupling and from Presence and Absence of NOE's Israel Journal of Chemistry. 27: 181-188. DOI: 10.1002/Ijch.198600027 |
0.337 |
|
| 1985 |
Zuiderweg ER, Scheek RM, Kaptein R. Two-dimensional 1H-nmr studies on the lac repressor DNA binding domain: further resonance assignments and identification of nuclear Overhauser enhancements. Biopolymers. 24: 2257-77. PMID 3912012 DOI: 10.1002/Bip.360241208 |
0.418 |
|
| 1985 |
Zuiderweg ER, Scheek RM, Boelens R, van Gunsteren WF, Kaptein R. Determination of protein structures from nuclear magnetic resonance data using a restrained molecular dynamics approach: the lac repressor DNA binding domain. Biochimie. 67: 707-15. PMID 3910108 DOI: 10.1016/S0300-9084(85)80158-9 |
0.392 |
|
| 1985 |
Kaptein R, Zuiderweg ER, Scheek RM, Boelens R, van Gunsteren WF. A protein structure from nuclear magnetic resonance data. lac repressor headpiece. Journal of Molecular Biology. 182: 179-82. PMID 3889346 DOI: 10.1016/0022-2836(85)90036-1 |
0.401 |
|
| 1985 |
Boelens R, Gros P, Scheek RM, Verpoorte JA, Kaptein R. Hydrogen exchange of individual amide protons in the E. coli lac repressor DNA-binding domain: a nuclear magnetic resonance study. Journal of Biomolecular Structure & Dynamics. 3: 269-80. PMID 2855972 DOI: 10.1080/07391102.1985.10508416 |
0.383 |
|
| 1985 |
Boelens R, Scheek RM, Dijkstra K, Kaptein R. Sequential assignment of imino- and amino-proton resonances in 1H NMR spectra of oligonucleotides by two-dimensional NMR spectroscopy. Application to a lac operator fragment Journal of Magnetic Resonance (1969). 62: 378-386. DOI: 10.1016/0022-2364(85)90207-0 |
0.39 |
|
| 1984 |
Moonen CT, Scheek RM, Boelens R, Müller F. The use of two-dimensional nuclear-magnetic-resonance spectroscopy and two-dimensional difference spectra in the elucidation of the active center of Megasphaera elsdenii flavodoxin. European Journal of Biochemistry / Febs. 141: 323-30. PMID 6734600 DOI: 10.1111/J.1432-1033.1984.Tb08195.X |
0.39 |
|
| 1984 |
Scheek RM, Boelens R, Russo N, van Boom JH, Kaptein R. Sequential resonance assignments in 1H NMR spectra of oligonucleotides by two-dimensional NMR spectroscopy. Biochemistry. 23: 1371-6. PMID 6722097 DOI: 10.1021/Bi00302A006 |
0.354 |
|
| 1984 |
Zuiderweg ER, Billeter M, Boelens R, Scheek RM, Wüthrich K, Kaptein R. Spatial arrangement of the three alpha helices in the solution conformation of E. coli lac repressor DNA-binding domain. Febs Letters. 174: 243-7. PMID 6381097 DOI: 10.1016/0014-5793(84)81166-7 |
0.357 |
|
| 1984 |
Scheek RM, Stob S, Boelens R, Dijkstra K, Kaptein R. Applications of two-dimensional 1H nuclear magnetic resonance methods in photochemically induced dynamic nuclear polarisation spectroscopy Faraday Discussions of the Chemical Society. 78: 245-256. DOI: 10.1039/Dc9847800245 |
0.388 |
|
| 1983 |
Buck F, Hahn KD, Zemann W, Rüterjans H, Sadler JR, Beyreuther K, Kaptein R, Scheek R, Hull WE. NMR study of the interaction between the lac repressor and the lac operator European Journal of Biochemistry. 132: 321-327. PMID 6341060 DOI: 10.1111/J.1432-1033.1983.Tb07365.X |
0.382 |
|
| 1983 |
Scheek RM, Zuiderweg ER, Klappe KJ, van Boom JH, Kaptein R, Rüterjans H, Beyreuther K. lac Repressor headpiece binds specifically to half of the lac operator: a proton nuclear magnetic resonance study. Biochemistry. 22: 228-35. PMID 6338916 DOI: 10.1021/Bi00270A033 |
0.381 |
|
| 1983 |
Scheek RM, Russo N, Boelens R, Kaptein R, Van Boom JH. Sequential resonance assignments in DNA proton NMR spectra by two-dimensional NOE spectroscopy Journal of the American Chemical Society. 105: 2914-2916. DOI: 10.1002/Chin.198332337 |
0.361 |
|
| 1982 |
Scheek RM, Slater EC. Glyceraldehyde-3-phosphate dehydrogenase from rabbit muscle. Methods in Enzymology. 89: 305-9. PMID 7144575 DOI: 10.1016/S0076-6879(82)89055-1 |
0.412 |
|
| 1982 |
Schleich T, Scheek RM, Stob S, Alma NCM, Hilbers CW, Kaptein R. PHOTO-CIDNP STUDY OF ADENYLYL-CONTAINING DEOXY-DINUCLEOTIDES. PAIR SUBSTITUTION EFFECTS DUE TO INTRAMOLECULAR CATION RADICAL DEPROTONATION Photochemistry and Photobiology. 35: 575-577. DOI: 10.1111/J.1751-1097.1982.Tb02612.X |
0.347 |
|
| 1982 |
Hore PJ, Scheek RM, Volbeda A, Kaptein R, van Boom JH. 1H NMR assignments and connectivis of cytosines in lac operator DNA via double quantum coherence Journal of Magnetic Resonance (1969). 50: 328-334. DOI: 10.1016/0022-2364(82)90063-4 |
0.301 |
|
| 1981 |
Zuiderweg ER, Scheek RM, Veeneman G, van Boom JH, Kaptein R, Rüterjans H, Beyreuther K. 1H NMR studies of lac-operator DNA fragments. Nucleic Acids Research. 9: 6553-69. PMID 7322923 DOI: 10.1093/Nar/9.23.6553 |
0.36 |
|
| 1980 |
Scheek RM, Kalkman ML, Berden JA, Slater EC. Subunit interactions in glyceraldehyde-3-phosphate dehydrogenases. Their involvement in nucleotide binding and cooperativity. Biochimica Et Biophysica Acta. 613: 275-91. PMID 7004489 DOI: 10.1016/0005-2744(80)90083-2 |
0.472 |
|
| 1979 |
Scheek RM, Berden JA, Hooghiemstra R, Slater EC. Subunit interactions in rabbit-muscle glyceraldehyde-phosphate dehydrogenase, as measured by NAD+ and NADH binding. Biochimica Et Biophysica Acta. 569: 124-34. PMID 224931 DOI: 10.1016/0005-2744(79)90047-0 |
0.492 |
|
| 1979 |
Scheek RM, Kaptein R, Verhoeven JW. Resolution of specific histidine resonances in the 360 MHz 1H NMR spectrum of glyceraldehyde-3-phosphate dehydrogenase, a 145 000 molecular weight protein, by photo-CIDNP. Febs Letters. 107: 288-90. PMID 41741 DOI: 10.1016/0014-5793(79)80392-0 |
0.316 |
|
| 1978 |
Scheek RM, Slater EC. Preparation and properties of rabbit-muscle glyceraldehyde-phosphate dehydrogenase with equal binding parameters for the third and fourth NAD+ molecules. Biochimica Et Biophysica Acta. 526: 13-24. PMID 210823 DOI: 10.1016/0005-2744(78)90285-1 |
0.481 |
|
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