Reference health
The probable conformation of substrates recognized by dipeptidyl-peptidase IV and some aspects of the catalytic mechanism derived from theoretical investigations
23/23 checkable references clean · checked 2026-08-11
Every reference with a DOI in the deposited reference list resolved to a known work in Crossref or DataCite at the dated check, and none carried a retraction, withdrawal, or removal notice.
13 without a DOI — not checked. A reference deposited without a DOI is never matched by title or guessed at; it stays outside the checked set, and this line discloses that.
The 23 checked references that resolve
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The catalytic mechanism of serine proteases II: The effect of the protein environment in the α-chymotrypsin proton relay system
resolves10.1007/BF00306327
Distribution of a dipeptide naphthylamidase in rat tissues and its localisation by using diazo coupling and labeled antibody techniques
resolves10.1515/bchm2.1967.348.1.1540
Purification and Characterization of an Aminopeptidase Hydrolyzing Glycyl-Proline-Naphthylamide
resolves10.1111/j.1432-1033.1978.tb12628.x
An Amphiphilic Form of Dipeptidyl Peptidase IV from Pig Small-Intestinal Brush-Border Membrane. Purification by Immunoadsorbent Chromatography and Some Properties
resolves10.1016/0378-1119(80)90137-7
The nucleotide sequence of a cloned human leukocyte Interferon cDNA
resolves10.1016/S0006-3495(84)84073-4
Stereoelectronic control in peptide bond formation. Ab initio calculations and speculations on the mechanism of action of serine proteases
resolves10.1007/978-94-015-6918-7_7
Recent Quantum/Statistical Mechanical Studies on Enzyme Activityx Serine Proteases and Alcohol Dehydrogenases
resolves10.1016/0166-1280(85)80192-5
Modelling active site response towards changes in the protein-core of serine proteases. Aa CNDO/2—INDO SCRF study of subtilisin and thiosubtilisin
resolves10.1063/1.442434
An inhomogeneous self-consistent reaction field theory of protein core effects. Towards a quantum scheme for describing enzyme reactions
resolves10.1002/qua.560220309
Electrostatic effect on catalytic rate enhancement in serine proteinases
resolves10.1002/qua.560230241
Unusually large electrostatic field effect of the buried aspartate in serine proteinases: Source of catalytic power
resolves10.1016/0022-5193(83)90291-6
Comparison of protein electrostatic potential along the catalytic triad of serine proteinases
resolves10.1016/0141-8130(81)90056-8
Easily polarizable proton transfer hydrogen bonds between the side chains of histidine and the carboxylic acid groups of glutamic and aspartic acid residues in proteins
resolves10.1016/0022-2836(85)90283-9
The 1.8 Å structure of the complex between chymostatin and Streptomyces griseus protease A
resolves10.1016/0263-7855(91)85010-V
HAMOG: Molecular graphics program for chemistry 5 biochemistry 5 molecular biology and enzyme research
resolves10.1021/ja00798a002
Estimation of atomic charges by an electronegativity equalization procedure calibrated with core binding energies
resolves10.1021/ic50141a028
Calculation of atomic charges by an electronegativity equalization procedure
resolves10.1111/j.1399-3011.1984.tb00951.x
Backbone conformations, bend structures, helix structures and other tests of an improved conformational energy program for peptides: ECEPP83
resolves10.1016/0167-4838(83)90261-3
The conformation around the peptide bond between the P1- and P2-positions is important for catalytic activity of some proline-specific proteases
resolves10.1073/pnas.84.22.7962
cDNA cloning for a bile canaliculus domain-specific membrane glycoprotein of rat hepatocytes.
The 13 references without a DOI — listed, not checked
no DOI — not checkedMcDonald, J.K., Callahan, P.X., Smith, R.E. and Ellis, S., In Barett, A.J. and Dingle, J.T., (Eds) Tissue Proteinases North-Holland Amsterdam, 1971, pp. 69?107.
no DOI — not checkedBarth, A., Schulz, H. and Neubert, K., Acta Biol. Med. Germ., 32 (1974) 157.
no DOI — not checkedBarth, A. and Schulz, H., Pharmazie, 29 (1974) 137.
no DOI — not checkedWolf, B., Fischer, G. and Barth, A., Acta Biol. Med. Germ., 37 (1978) 409.
no DOI — not checkedFischer, G. and Barth, A., In Öhme, P., Löwe, H. and Gores, E. (Eds.), Beiträge zur Wirkstofforschung, Vol. 11, Akademie-Industrie-Komplex ?Arzneimittelforschung?, Berlin, 1981, pp. 105?133.
no DOI — not checkedBarth, A., Fischer, G., Neubert, K., Heins, J. and Mager, H., Wiss. Z. Leuna-Merseburg, 22 (1980) 352.
no DOI — not checkedBarth, A., Reference 12, pp. 134?151
no DOI — not checkedBarth, A., Wiss. Z. Univ. Halle, 28 (1979) 23.
no DOI — not checkedChuman, H., Momany, F.A. and Schäfer, L., In Hruby, V. and Rich, D.H. (Eds.) Peptides: Structure and Function (Proceedings of the 8th American Peptide Symposium) Pierce Chemical Co., Rockford, IL, 1983, pp. 825?828.
no DOI — not checkedReck, G. and Barth, A., Cryst. Struct. Comm., 10 (1981) 653.
no DOI — not checkedBrandt, W. and Hofmann, T., Biol. Zbl., 107 (1988) 21.
no DOI — not checkedReck, G. and Barth, A., Cryst. Struct. Comm., 10 (1981) 1001.
no DOI — not checkedBrandt, W. and Barth, A., Wiss. Z. Univ. Halle, 38 (1989) 55.
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