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.
The 64 checked references that resolve
resolves10.1073/pnas.69.6.1408Purification of Biologically Active Globin Messenger RNA by Chromatography on Oligothymidylic acid-Cellulose
resolves10.1021/bi00591a005Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease
resolves10.1093/nar/16.8.3580A rapid and convenient method for the preparation and storage of competent bacterial cells
resolves10.1073/pnas.80.1.21The tac promoter: a functional hybrid derived from the trp and lac promoters.
resolves10.1139/m86-009Secretion of α-amylase and multiple forms of glucoamylase by the yeast <i>Trichosporon pullulans</i>
resolves10.1016/0378-1119(88)90044-3Sequence and organization of pobA, the gene coding for p-hydroxybenzoate hydroxylase, an inducible enzyme from Pseudomonas aeruginosa
resolves10.1016/0014-5793(90)80843-8Engineering of microheterogeneity‐resistant <i>p</i>‐hydroxybenzoate hydroxylase from <i>Pseudomonas fluorescens</i>
resolves10.1007/BF00527072Induction of phenol-metabolizing enzymes in Trichosporon cutaneum
resolves10.1007/BF00404904DNA base composition and DNA relatedness among species of Trichosporon Behrend
resolves10.1093/nar/14.21.8615Efficient construction of cDNA libraries in plasmid expression vectors using an adaptor strategy
resolves10.1002/bit.260241115Growth of <i>Trichosporon cutaneum</i> under oxygen limitation: Kinetics of oxygen uptake
resolves10.1128/JB.172.8.4624-4630.1990Molecular cloning, characterization, and regulation of a Pseudomonas pickettii PKO1 gene encoding phenol hydroxylase and expression of the gene in Pseudomonas aeruginosa PAO1c
resolves10.1038/227680a0Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
resolves10.1007/BF00286325Degradation of phenol by a mixed culture of Pseudomonas putida and Cryptococcus elinovii adsorbed on activated carbon
resolves10.1021/bi00410a038Thiol- and pH-modulated slow conformational changes and cooperativity of phenol-binding sites in phenol hydroxylase
resolves10.1021/bi00563a005Phenol hydroxylase from yeast: a lysyl residue essential for binding of reduced nicotinamide adenine dinucleotide phosphate
resolves10.1016/0378-1119(91)90531-FSequence of the gene (pheA) encoding phenol monooxygenase from Pseudomonas sp. EST1001: expression in Escherichia coli and Pseudomonas putida
resolves10.1111/j.1432-1033.1976.tb10019.xBacterial Metabolism of Resorcinylic Compounds:. Purification and Properties of Orcinol Hydroxylase and Resorcinol Hydroxylase from Pseudomonas putida ORC
resolves10.1128/JB.172.5.2351-2359.1990Organization and sequence analysis of the 2,4-dichlorophenol hydroxylase and dichlorocatechol oxidative operons of plasmid pJP4
resolves10.1126/science.2999980Enzymatic Amplification of β-Globin Genomic Sequences and Restriction Site Analysis for Diagnosis of Sickle Cell Anemia
resolves10.1007/BF01024654Arginyl residues in the NADPH-binding sites of phenol hydroxylase
resolves10.1093/nar/16.15.7583λ ZAP: a bacteriophage λ expression vector with<i>in vivo</i>excision properties
resolves10.1002/bit.260290409Growth and enzyme synthesis during continuous culture of <i>Trichosporon cutaneum</i> on phenol
resolves10.1016/0003-2697(87)90367-8Construction of cDNA libraries by blunt-end ligation: High-frequency cloning of long cDNAs from filamentous fungi
resolves10.1007/BF01378246Isolation from soil of phenol-utilizing organisms and metabolic studies on the pathways of phenol degradation
resolves10.1007/BF00413025Physiological role of microbodies in the yeast Trichosporon cutaneum during growth on ethylamine as the source of energy, carbon and nitrogen
resolves10.1021/bi00327a012Interaction of pyrophosphate moieties with .alpha.-helixes in dinucleotide-binding proteins
resolves10.1016/0022-2836(86)90409-2Prediction of the occurrence of the ADP-binding βαβ-fold in proteins, using an amino acid sequence fingerprint
resolves10.1021/bi00220a028Nucleotide sequence analysis of the Pseudomonas putida PpG7 salicylate hydroxylase gene (nahG) and its 3'-flanking region
The 13 references without a DOI — listed, not checked
no DOI — not checkedBallou D. 1982. Flavoprotein monooxygenases p. 301-310. In V. Massey and C. H. Williams (ed.) Flavin and flavoproteins. Elsevier/North Holland Publishing Co. New York.
no DOI — not checkedBayty R. C. and M. G. Barbour. 1984. The degradation of aromatic compounds by the meta and gentisate pathways: biochemistry and regulation p. 253-294. In D. T. Gibson (ed.) Microbial degradation of organic compounds. Marcel Dekker Inc. New York.
no DOI — not checkedBullock , W. O. , J. M. Fernandez , and J. M. Short . 1987 . XL1-Blue: a high efficiency plasmid transforming recA Escherichia coli strain with beta-galactosidase selection . BioTechniques 5 : 376 - 379 .
no DOI — not checkedEggink , G. , H. Engel , G. Vriend , P. Terpstra , and B. Witholt . 1990 . Rubredoxin reductase of Pseudomonas oleovorans. Structural relationship to other flavoprotein oxidoreductases based on one NAD and two FAD fingerprints . J. Mol. Biol. 212 : 135 - 142 .
no DOI — not checkedEschrich , K. , W. J. H. van Berkel , A. H. Westphal , A. de Kok , A. Mattevi , G. Obmolova , K. H. Kalk , and W. G. J. Hol . 1990 . Engineering of microheterogeneity-resistant p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens . FEBS Lett. 278 : 287 . (Erratum.)
no DOI — not checkedKukor J. J. and R. H. Olsen (University of Michigan Ann Arbor). 1992. Personal communication.
no DOI — not checkedManiatis T. E. F. Fritsch and J. Sambrook 1982. Molecular cloning: a laboratory manual. Cold Spring Harbor Laboratory Cold Spring Harbor N.Y.
no DOI — not checkedSakai , T. , and M. Okushima . 1982 . Purification and crystallization of a protopectin-solubilizing enzyme from Tnchosporon penicilatum . Agric. Biol. Chem. 46 : 667 - 676 .
no DOI — not checkedSambrook J. E. F. Fritsch and T. Maniatis. 1989. Molecular cloning: a laboratory manual 2nd ed. Cold Spring Harbor Laboratory Cold Spring Harbor N.Y.
no DOI — not checkedSejlitz T. and H. Y. Neijahr. Unpublished data.
no DOI — not checkedSejlitz , T. , C. Wernstedt , U. Hellman , and H. Y. Neujahr . 1991 . The N-terminal amino acid sequence of phenol hydroxylase contains an ADP-binding sequence motif . Protein Sequences Data Anal. 4 : 21 - 23 .
no DOI — not checkedSuter M. Unpublished data.
no DOI — not checkedZimmermann M. and C. C. Emeis. 1989. Extracellular polysaccharidases from Trichosporon beigelii abstr. S131. Proc. Seventh Int. Symp. Yeasts. John Wiley & Sons Chichester United Kingdom.
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