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Exclusive A-ring linkage for singly attached phycocyanobilins and phycoerythrobilins in phycobiliproteins. Absence of singly D-ring-linked bilins.
Lagarias JC, Klotz AV, Dallas JL, Glazer AN, Bishop JE, O'Connell JF, Rapoport H. Lagarias JC, et al. Among authors: glazer an. J Biol Chem. 1988 Sep 15;263(26):12977-85. J Biol Chem. 1988. PMID: 3417648 Free article.
O., Schoenleber, R.W., Rapoport, H., Klotz, A.V., and Glazer, A.N. (1986) J. Biol. Chem. 261, 6790-6796; Klotz, A.V., Glazer, A.N., Bishop, J.E., Nagy, J.O., and Rapoport, H. (1986) J. ...Examination of the phycoerythrobilin beta-2 position in B-phycoerythrin also r …
O., Schoenleber, R.W., Rapoport, H., Klotz, A.V., and Glazer, A.N. (1986) J. Biol. Chem. 261, 6790-6796; Klotz, A.V., Glazer, …
gamma-N-methylasparagine in phycobiliproteins. Occurrence, location, and biosynthesis.
Klotz AV, Glazer AN. Klotz AV, et al. Among authors: glazer an. J Biol Chem. 1987 Dec 25;262(36):17350-5. J Biol Chem. 1987. PMID: 2447072 Free article.
The novel post-translationally modified residue gamma-N-methylasparagine, previously detected in the beta subunit of allophycocyanin (Klotz, A. V., Leary, J. A., and Glazer, A. N. (1986) J. Biol. Chem. 261, 15891-15894), has been found in the beta subunits of a variety of …
The novel post-translationally modified residue gamma-N-methylasparagine, previously detected in the beta subunit of allophycocyanin (Klotz, …
Phycobiliprotein-bilin linkage diversity. I. Structural studies on A- and D-ring-linked phycocyanobilins.
Bishop JE, Lagarias JC, Nagy JO, Schoenleber RW, Rapoport H, Klotz AV, Glazer AN. Bishop JE, et al. Among authors: glazer an. J Biol Chem. 1986 May 25;261(15):6790-6. J Biol Chem. 1986. PMID: 3084489 Free article.
The above results together with those of an earlier study (Lagarias, J. C., Glazer, A. N., and Rapoport, H. (1979) J. Am. Chem. ...
The above results together with those of an earlier study (Lagarias, J. C., Glazer, A. N., and Rapoport, H. (1979) J. Am. Chem …
In vitro attachment of bilins to apophycocyanin. II. Determination of the structures of tryptic bilin peptides derived from the phycocyanobilin adduct.
Arciero DM, Dallas JL, Glazer AN. Arciero DM, et al. Among authors: glazer an. J Biol Chem. 1988 Dec 5;263(34):18350-7. J Biol Chem. 1988. PMID: 3192538 Free article.
In vitro reaction of phycocyanobilin (PCB) with apophycocyanin results in the specific addition of the bilin to two of the cysteinyl residues, alpha-Cys-84 and beta-Cys-82, which normally function in PCB attachment (Arciero, D. M., Bryant, D. A., and Glazer, A. N. (1988) J …
In vitro reaction of phycocyanobilin (PCB) with apophycocyanin results in the specific addition of the bilin to two of the cysteinyl residue …
Post-translational methylation of asparaginyl residues. Identification of beta-71 gamma-N-methylasparagine in allophycocyanin.
Klotz AV, Leary JA, Glazer AN. Klotz AV, et al. Among authors: glazer an. J Biol Chem. 1986 Dec 5;261(34):15891-4. J Biol Chem. 1986. PMID: 3782095 Free article.
Structure determination was accomplished by isolating a decapeptide, AP-beta (63-72) shown to have the following structure: Ser-Asp-Ile-Thr-Arg-Pro-Gly-Gly- Asn[N-CH3]-homoserine lactone Fast atom bombardment-mass spectrometry established that the residue corresponding to positio …
Structure determination was accomplished by isolating a decapeptide, AP-beta (63-72) shown to have the following structure: Ser-Asp-Ile-Thr- …
199 results