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141 related items for PubMed ID: 1727645
1. The amino acid sequence and oxygen-binding properties of the single hemoglobin of the cold-adapted Antarctic teleost Gymnodraco acuticeps. Tamburrini M, Brancaccio A, Ippoliti R, di Prisco G. Arch Biochem Biophys; 1992 Jan; 292(1):295-302. PubMed ID: 1727645 [Abstract] [Full Text] [Related]
2. The hemoglobins of the cold-adapted Antarctic teleost Cygnodraco mawsoni. Caruso C, Rutigliano B, Romano M, di Prisco G. Biochim Biophys Acta; 1991 Jun 24; 1078(2):273-82. PubMed ID: 2065095 [Abstract] [Full Text] [Related]
3. The amino acid sequence of the single hemoglobin of the high-antarctic fish Bathydraco marri Norman. Caruso C, Rutigliano B, Riccio A, Kunzmann A, di Prisco G. Comp Biochem Physiol B; 1992 Aug 24; 102(4):941-6. PubMed ID: 1395518 [Abstract] [Full Text] [Related]
4. The hemoglobins of the antarctic fishes Atedidraco orianae and Pogonophryne scotti. Amino acid sequence, lack of cooperativity, and ligand binding properties. Tamburrini M, Romano M, Carratore V, Kunzmann A, Coletta M, di Prisco G. J Biol Chem; 1998 Dec 04; 273(49):32452-9. PubMed ID: 9829976 [Abstract] [Full Text] [Related]
6. The unique hemoglobin system of Pleuragramma antarcticum, an antarctic migratory teleost. Structure and function of the three components. Tamburrini M, D'Avino R, Fago A, Carratore V, Kunzmann A, Prisco G. J Biol Chem; 1996 Sep 27; 271(39):23780-5. PubMed ID: 8798605 [Abstract] [Full Text] [Related]
7. The hemoglobins of the sub-Antarctic fish Cottoperca gobio, a phyletically basal species--oxygen-binding equilibria, kinetics and molecular dynamics. Giordano D, Boechi L, Vergara A, Martí MA, Samuni U, Dantsker D, Grassi L, Estrin DA, Friedman JM, Mazzarella L, di Prisco G, Verde C. FEBS J; 2009 Apr 27; 276(8):2266-77. PubMed ID: 19292863 [Abstract] [Full Text] [Related]
16. Hemoglobin from the antarctic fish Notothenia coriiceps neglecta. Amino acid sequence of the beta chain. D'Avino R, Caruso C, Schinina ME, Rutigliano B, Romano M, Camardella L, Bossa F, Barra D, di Prisco G. Comp Biochem Physiol B; 1990 Jul 21; 96(2):367-73. PubMed ID: 2361365 [Abstract] [Full Text] [Related]
17. The cathodic hemoglobin of Anguilla anguilla. Amino acid sequence and oxygen equilibria of a reverse Bohr effect hemoglobin with high oxygen affinity and high phosphate sensitivity. Fago A, Carratore V, di Prisco G, Feuerlein RJ, Sottrup-Jensen L, Weber RE. J Biol Chem; 1995 Aug 11; 270(32):18897-902. PubMed ID: 7642546 [Abstract] [Full Text] [Related]
18. GC bias lead to increased small amino acids and random coils of proteins in cold-water fishes. Zhang D, Hu P, Liu T, Wang J, Jiang S, Xu Q, Chen L. BMC Genomics; 2018 May 02; 19(1):315. PubMed ID: 29720106 [Abstract] [Full Text] [Related]