Year |
Citation |
Score |
1981 |
Dieter H, Koberstein R, Sund H. Studies of glutamate dehydrogenase. The interaction of ADP, GTP, and NADPH in complexes with glutamate dehydrogenase. European Journal of Biochemistry. 115: 217-226. PMID 7227367 DOI: 10.1111/J.1432-1033.1981.Tb06219.X |
0.306 |
|
1977 |
Rasched IR, Bohn A, Sund H. Studies of glutamate dehydrogenase. Analysis of quaternary structure and contact areas between the polypeptide chains European Journal of Biochemistry. 74: 365-377. PMID 558096 DOI: 10.1111/J.1432-1033.1977.Tb11401.X |
0.318 |
|
1977 |
David M, Rasched IR, Sund H. Studies of glutamate dehydrogenase. Methionine 169: the preferentially carboxymethylated residue European Journal of Biochemistry. 74: 379-385. PMID 15838 DOI: 10.1111/J.1432-1033.1977.Tb11402.X |
0.343 |
|
1976 |
Neumann P, Markau K, Sund H. Studies of glutamate dehydrogenase. Regulation of glutamate dehydrogenase from Candida utilis by a pH and temperature dependent conformational transition European Journal of Biochemistry. 65: 465-472. PMID 7452 DOI: 10.1111/J.1432-1033.1976.Tb10362.X |
0.31 |
|
1975 |
Hucho F, Muellner H, Sund H. Investigation of the symmetry of oligomeric enzymes with bifunctional reagents European Journal of Biochemistry. 59: 79-87. PMID 1204620 DOI: 10.1111/J.1432-1033.1975.Tb02427.X |
0.633 |
|
1975 |
Hucho F, Rasched I, Sund H. Studies of glutamate dehydrogenase: analysis of functional areas and functional groups European Journal of Biochemistry. 52: 221-230. PMID 240678 DOI: 10.1111/J.1432-1033.1975.Tb03990.X |
0.669 |
|
1975 |
Ifflaender U, Markau K, Sund H. Quantitative analysis of mixed association between different protein molecules. Physico chemical and enzymatic properties of rat liver glutamate dehydrogenase European Journal of Biochemistry. 52: 211-220. PMID 240677 DOI: 10.1111/J.1432-1033.1975.Tb03989.X |
0.317 |
|
1974 |
Witzemann V, Koberstein R, Sund H, Rasched I, Jörnvall H, Noack K. Studies of glutamate dehydrogenase: chemical modification and quantitative determination of tryptophan residues. European Journal of Biochemistry / Febs. 43: 319-25. PMID 4365183 DOI: 10.1111/J.1432-1033.1974.Tb03415.X |
0.362 |
|
1973 |
Deppert W, Hucho F, Sund H. Studies of glutamate dehydrogenase. Modification with 5-diazo-1H-tetrazole and glyoxal. Importance of two different amino groups for the binding of 2-oxoglutarate and NADH. European Journal of Biochemistry. 32: 76-82. PMID 4347090 DOI: 10.1111/J.1432-1033.1973.Tb02581.X |
0.64 |
|
1973 |
Hucho F, Markau U, Sund H. Studies of glutamate dehydrogenase. Characterization of histidine residues involved in the activity and association. Photoactivated labelling with pyridoxal 5'-phosphate. European Journal of Biochemistry. 32: 69-75. PMID 4347089 DOI: 10.1111/J.1432-1033.1973.Tb02580.X |
0.646 |
|
1972 |
Hucho F, Deppert W, Sund H. Analysis of functional groups of bovine liver glutamate-dehydrogenase through chemical modification | Analyse von funktionellen Gruppen der Rinderleber-Glutamat-Dehydrogenase durch chemische Modifikation. Hoppe-Seyler's Zeitschrift Fur Physiologische Chemie. 353: 717. PMID 4341660 |
0.612 |
|
1971 |
Markau K, Schneider J, Sund H. Studies of glutamate dehydrogenase. The mechanism of the association-dissociation equilibrium of beef-liver glutamate dehydrogenase. European Journal of Biochemistry. 24: 393-400. PMID 4333603 DOI: 10.1111/J.1432-1033.1971.Tb19698.X |
0.321 |
|
1964 |
WEBER K, SUND H, WALLENFELS K. [ON THE NATURE OF THE BINDING BETWEEN SUBUNITS IN THE MOLECULE OF BETA-GALACTOSIDASE FROM E. COLI]. Biochemische Zeitschrift. 339: 498-500. PMID 14243756 |
0.652 |
|
1964 |
SUND H, DIEKMANN H, WALLENFELS K. [HYDROGEN TRANSFER WITH PYRIDINE NUCLEOTIDES]. Advances in Enzymology and Related Areas of Molecular Biology. 26: 115-91. PMID 14150644 |
0.612 |
|
1963 |
WALLENFELS K, SUND H, WEBER K. [THE SUBUNITS OF BETA-GALACTOSIDASE FROM E. COLI]. Biochemische Zeitschrift. 338: 714-27. PMID 14087336 |
0.647 |
|
1963 |
ARENS A, SUND H, WALLENFELS K. [On the mechanism of hydrogen transfer with pyridine nucleotides. XXI. On the problem of terminal-N groups and zinc content of yeast alcohol dehydrogenase]. Biochemische Zeitschrift. 337: 1-23. PMID 14013696 |
0.639 |
|
1963 |
Webber K, Sund H, Wallenfels K. The Subunits of theβ-Galactosidase from Escherichia coli Angewandte Chemie International Edition in English. 2: 481-481. DOI: 10.1002/Anie.196304812 |
0.624 |
|
1962 |
WALLENFELS K, SUND H, BURCHARD W. [On the effect of BZ 55 on the aggregation of insulin in the presence of zinc ions]. Biochemische Zeitschrift. 335: 315-24. PMID 14004682 |
0.578 |
|
1961 |
KRAINICK HG, MUELLER-HILL B, STRUWE FE, SUND H, WALLENFELS K. [Zinc in the urine in juvenile diabetes mellitus and in ketonemia]. Klinische Wochenschrift. 39: 1132-7. PMID 14459243 DOI: 10.1007/Bf01481829 |
0.592 |
|
1961 |
Krainick HG, Müller-Hill B, Struwe FE, Sund H, Wallenfels K. Zink im Harn bei juvenilem Diabetes mellitus und bei Ketonämie Klinische Wochenschrift. 39: 1132-1137. DOI: 10.1007/BF01481829 |
0.583 |
|
1959 |
WALLENFELS K, SUND H. [The mechanism of action of 3,5-dioxo-1,2-diphenyl-4-n-butyl-pyrazolidine; complex forming ability of this compound and effects on diphosphopyridine nucleotide-dependent zinc enzymes]. Arzneimittel-Forschung. 9: 81-9. PMID 13638188 |
0.634 |
|
1958 |
WALLENFELS K, KERP L, SUND H. [Histamine formation in serum of normal & allergic subjects]. Klinische Wochenschrift. 36: 772-3. PMID 13576764 DOI: 10.1007/Bf01482859 |
0.574 |
|
1958 |
Wallenfels K, Kerp L, Sund H. Über die Histaminbindung im Serum von Normalen und Allergikern - Vorläufige Mitteilung Klinische Wochenschrift. 36: 772-773. DOI: 10.1007/BF01482859 |
0.578 |
|
1957 |
WALLENFELS K, SUND H. [Mechanism of action of butazolidin: inhibition of DPN-dependent zinc enzyme]. Naunyn-Schmiedebergs Archiv FüR Experimentelle Pathologie Und Pharmakologie. 232: 338-40. PMID 13526886 |
0.636 |
|
1957 |
WALLENFELS K, SUND H. [Mechanism of hydrogen transport with pyridine nucleotides. V. Diphosphopyridine nucleotide ion binding abilities of alcohol dehydrogenase and its zinc complex]. Biochemische Zeitschrift. 329: 59-74. PMID 13436414 |
0.648 |
|
1957 |
WALLENFELS K, SUND H. [Mechanism of hydrogen transport with pyridine nucleoides. IV. Inhibitors of diphosphopyridine nucleotide dependent zinc enzymes]. Biochemische Zeitschrift. 329: 48-58. PMID 13436413 |
0.666 |
|
1957 |
WALLENFELS K, SUND H. [Mechanism of hydrogen transport with pyridine nucleotides. III. Binary and tertiary zinc complexes as model substances for the enzyme-coenzyme bonding]. Biochemische Zeitschrift. 329: 41-7. PMID 13436412 |
0.658 |
|
1957 |
WALLENFELS K, SUND H, FAESSLER A, BURCHARD W. [Mechanism of hydrogen transport with pyridine nucleotides. II. The minimal and maximal zinc content of crystallized yeast alcohol dehydrogenase]. Biochemische Zeitschrift. 329: 31-40. PMID 13436411 |
0.639 |
|
1957 |
WALLENFELS K, SUND H. [Mechanism of hydrogen transport with pyridine nucleotides. I. Free sulfhydryl groups and activity of yeast alcohol dehydrogenase]. Biochemische Zeitschrift. 329: 17-30. PMID 13436410 |
0.651 |
|
1957 |
Wallenfels K, Sund H. Zum Wirkungsmechanismus des Butazolidins: Hemmung DPN-abhängiger Zinkenzyme Naunyn-Schmiedebergs Archiv FüR Experimentelle Pathologie Und Pharmakologie. 232: 338-340. DOI: 10.1007/BF00259910 |
0.573 |
|
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