| Publication |
Sentence |
Publish Date |
Extraction Date |
Species |
| R Bachoual, J Tankovic, C J Souss. Analysis of the mutations involved in fluoroquinolone resistance of in vivo and in vitro mutants of Escherichia coli. Microbial drug resistance (Larchmont, N.Y.). vol 4. issue 4. 1999-04-02. PMID:9988045. |
by pcr and sequencing, two mutations in gyra, leading to ser-83 --> leu and asp-87 --> asn (7) or gly (2) or tyr (1) changes, were found in 10 strains, the eleventh presenting only the ser-83 --> leu change. |
1999-04-02 |
2023-08-12 |
Not clear |
| A S Ito, R D Turchiello, I Y Hirata, M H Cezari, M Meldal, L Julian. Fluorescent properties of amino acids labeled with ortho-aminobenzoic acid. Biospectroscopy. vol 4. issue 6. 1999-02-11. PMID:9851720. |
we report in this article the optical absorption and fluorescent properties, in aqueous media, of abz bound to the alpha-amino group of ala, gly, leu, ile, val, pro, phe, arg, glu, met, asn, tyr, and trp, with monomethylamidated alpha-carboxyl group. |
1999-02-11 |
2023-08-12 |
Not clear |
| P Jarolim, H L Rubin, D Zakova, J Storry, M E Rei. Characterization of seven low incidence blood group antigens carried by erythrocyte band 3 protein. Blood. vol 92. issue 12. 1999-02-05. PMID:9845551. |
we found that the putative first ectoplasmic loop of band 3 carries blood group antigen elo, 432 arg-->trp; the third putative loop harbors antigens vga (van vugt), 555 tyr-->his, bow 561 pro-->ser, wu (wulfsberg), 565 gly-->ala, and bpa (bishop), 569 asn-->lys; and the putative fourth ectoplasmic loop carries antigens hga (hughes), 656 arg-->cys, and moa (moen), 656 arg-->his. |
1999-02-05 |
2023-08-12 |
Not clear |
| T Araki, T Matsumoto, T Torikat. The amino acid sequence of monal pheasant lysozyme and its activity. Bioscience, biotechnology, and biochemistry. vol 62. issue 10. 1999-01-07. PMID:9836434. |
the established amino acid sequence had one amino acid substitution at position 102 (arg to gly) comparing with indian peafowl lysozyme and four amino acid substitutions at positions 3 (phe to tyr), 15 (his to leu), 41 (gln to his), and 121 (gln to his) with chicken lysozyme. |
1999-01-07 |
2023-08-12 |
chicken |
| A Errami, N J Finnie, B Morolli, S P Jackson, P H Lohman, M Z Zdzienick. Molecular and biochemical characterization of new X-ray-sensitive hamster cell mutants defective in Ku80. Nucleic acids research. vol 26. issue 19. 1998-11-17. PMID:9742232. |
dna sequence analysis of the ku80 cdna from these mutants showed a deletion of 252 bp in xr-v10b; a 6 bp deletion that results in a new amino acid residue at position 107 and the loss of two amino acid residues at positions 108 and 109 in xr-v11b; a missense mutation resulting in a substitution of cys for tyr at position 114 in xr-v13b; and two missense mutations in xr-v16b, resulting in a substitution of met for val at position 331 and arg for gly at position 354. |
1998-11-17 |
2023-08-12 |
Not clear |
| J S DIXON, C H L. The amino acid composition of human pituitary growth hormone. The Journal of general physiology. vol 45(4)Pt 2. 1998-11-01. PMID:13886645. |
on the basis of 29,000 for the molecular weight, the empirical formula of the hormone was obtained: lys(13)his(5)arg(14)asp(27) thr(14)ser(23)glu(34)pro(12)gly(13)ala(12)-(1/2 cys)(6)val(12)met(4)-ileu(10)leu(31)tyr(10)phe(15)try(1)(nh(3))(32). |
1998-11-01 |
2023-08-12 |
human |
| J Geisel, J Gielen, K Oette, W Herrmann, K Wielcken. Mutation analysis of exon 3 of the LDL receptor gene in patients with severe hypercholesterolemia. Clinical chemistry and laboratory medicine. vol 36. issue 5. 1998-10-09. PMID:9676383. |
by direct dna sequencing, the underlying mutations could be confirmed (cys54-->tyr, trp66-->gly, glu80-->lys, 2 bp insertion (at between codon 44 and 45, 9 bp deletion (codons 65 to 67)). |
1998-10-09 |
2023-08-12 |
Not clear |
| A Bevan, C Brenner, R S Fulle. Quantitative assessment of enzyme specificity in vivo: P2 recognition by Kex2 protease defined in a genetic system. Proceedings of the National Academy of Sciences of the United States of America. vol 95. issue 18. 1998-09-28. PMID:9724712. |
p2 preference followed the rank order: lys > arg > thr > pro > glu > ile > ser > ala > asn > val > cys > asp > gln > gly > his > met > leu > tyr > phe > trp. |
1998-09-28 |
2023-08-12 |
Not clear |
| S K Shyue, S Boissinot, H Schneider, I Sampaio, M P Schneider, C R Abee, L Williams, D Hewett-Emmett, H G Sperling, J A Cowing, K S Dulai, D M Hunt, W H L. Molecular genetics of spectral tuning in New World monkey color vision. Journal of molecular evolution. vol 46. issue 6. 1998-09-02. PMID:9608052. |
from the deduced amino acid sequences and the spectral peak information and from previous studies of the spectral tuning of x-linked pigments in humans and new world monkeys, we estimated that the ala --> ser, ile --> phe, gly --> ser, phe --> tyr, and ala --> tyr substitutions at residue positions 180, 229, 233, 277, and 285, respectively, cause spectral shifts of about 5, -2, -1, 8, and 15 nm. |
1998-09-02 |
2023-08-12 |
monkey |
| A M Smith, K P Klugma. Alterations in PBP 1A essential-for high-level penicillin resistance in Streptococcus pneumoniae. Antimicrobial agents and chemotherapy. vol 42. issue 6. 1998-08-13. PMID:9624469. |
for pbp 2x/2b/1a-r6 transformants, the introduction of the reversal of thr-371 by ser or ala in pbp 1a decreased the mic from 1.5 to 0.5 micrograms/ml, whereas the reversal of four consecutive amino acid substitutions (thr-574 by asn, ser-575 by thr, gln-576 by gly, and phe-577 by tyr) decreased the mic from 1.5 to 0.375 micrograms/ml. |
1998-08-13 |
2023-08-12 |
Not clear |
| V S Rao, K Lam, P K Qasb. Three dimensional structure of the soybean agglutinin Gal/GalNAc complexes by homology modeling. Journal of biomolecular structure & dynamics. vol 15. issue 5. 1998-08-05. PMID:9619508. |
three of the invariant residues asp, gly, and asn, besides an aromatic residue (phe or tyr), are involved in carbohydrate binding. |
1998-08-05 |
2023-08-12 |
Not clear |
| R D Wind, R M Buitelaar, L Dijkhuize. Engineering of factors determining alpha-amylase and cyclodextrin glycosyltransferase specificity in the cyclodextrin glycosyltransferase from Thermoanaerobacterium thermosulfurigenes EM1. European journal of biochemistry. vol 253. issue 3. 1998-07-29. PMID:9654055. |
all alpha-amylases studied have a small residue at this position (gly, leu, ser, thr or val), in contrast to cgtases which have a more bulky aromatic residue (tyr or phe) at this position, which is highly conserved. |
1998-07-29 |
2023-08-12 |
Not clear |
| A L Karamyshev, Z N Karamysheva, A V Kajava, V N Ksenzenko, M A Nesmeyanov. Processing of Escherichia coli alkaline phosphatase: role of the primary structure of the signal peptide cleavage region. Journal of molecular biology. vol 277. issue 4. 1998-05-26. PMID:9545377. |
amber suppressor mutagenesis, used to create mutant proteins, included: (i) introduction of amber mutations into respective positions of the phoa gene; and (ii) expression of each mutant phoa allele in e. coli strains producing amber suppressor trnas specific to ala, cys, gln, glu, gly, his, leu, lys, phe, pro, ser and tyr. |
1998-05-26 |
2023-08-12 |
Not clear |
| L Kiger, A L Klinger, L D Kwiatkowski, A De Young, M L Doyle, J M Holt, R W Noble, G K Acker. Thermodynamic studies on the equilibrium properties of a series of recombinant betaW37 hemoglobin mutants. Biochemistry. vol 37. issue 13. 1998-04-23. PMID:9521754. |
these alterations from wild-type function are dependent on the particular side chain substituted, with the magnitude of change increasing as trp is substituted by tyr, ala, gly, and glu. |
1998-04-23 |
2023-08-12 |
human |
| L D Kwiatkowski, H L Hui, A Wierzba, R W Noble, R Y Walder, E S Peterson, S G Sligar, K E Sander. Preparation and kinetic characterization of a series of betaW37 variants of human hemoglobin A: evidence for high-affinity T quaternary structures. Biochemistry. vol 37. issue 13. 1998-04-23. PMID:9521753. |
four variants of human beta globin in which the trp at position 37 has been replaced with a tyr, ala, gly, or glu have been expressed in escherichia coli. |
1998-04-23 |
2023-08-12 |
human |
| J S Kavanaugh, J A Weydert, P H Rogers, A Arnon. High-resolution crystal structures of human hemoglobin with mutations at tryptophan 37beta: structural basis for a high-affinity T-state,. Biochemistry. vol 37. issue 13. 1998-04-23. PMID:9521756. |
the high-resolution x-ray structures of the deoxy forms of four recombinant hemoglobins in which trp37(c3)beta is replaced with tyr (betaw37y), ala (betaw37a), glu (betaw37e), or gly (betaw37g) have been refined and analyzed with superposition methods that partition mutation-induced perturbations into quaternary structure changes and tertiary structure changes. |
1998-04-23 |
2023-08-12 |
human |
| M Sharma, R Jai. Isolation and analysis of dityrosine from enzyme-catalyzed oxidation of tyrosine and X-irradiated peptide and proteins. Chemico-biological interactions. vol 108. issue 3. 1998-04-15. PMID:9528688. |
hplc analysis of dansylated hydrolysate of the major product from an irradiated tripeptide (tyr gly gly) detected gly and dt (2:0.5). |
1998-04-15 |
2023-08-12 |
Not clear |
| L Schoofs, A Hamdaoui, B Devreese, J Van Beeumen, A De Loo. The ovary of the desert locust Schistocerca gregaria contains a glycine- and proline-rich peptide that displays sequence similarities with a new class of GPRP proteins from plants. Biochemical and biophysical research communications. vol 243. issue 2. 1998-03-27. PMID:9480819. |
the partial amino acid sequence as determined by edman degradation based automated microsequencing is as follows: ala-tyr-pro-ala-his-gln-gly-tyr- pro-ala-his-val-gly-tyr-ala-arg-val-gly-tyr-gly- gly-tyr-pro-ser-tyr-gly-tyr-pro-ala. four amino acids (gly, pro, ala, and tyr) account for more than 80% of the composition of this sequence. |
1998-03-27 |
2023-08-12 |
Not clear |
| T L Lentz, V Chaturvedi, B M Conti-Fin. Amino acids within residues 181-200 of the nicotinic acetylcholine receptor alpha1 subunit involved in nicotine binding. Biochemical pharmacology. vol 55. issue 3. 1998-03-19. PMID:9484801. |
affinity was not affected significantly by substitution of arg 182, lys 185 (with gly or arg), val 188, tyr 189, pro 194, asp 195, thr 196, and asp 200. |
1998-03-19 |
2023-08-12 |
Not clear |
| D G Arquès, C J Miche. A code in the protein coding genes. Bio Systems. vol 44. issue 2. 1998-02-04. PMID:9429747. |
the trinucleotides of t0 code for 13 amino acids: ala, asn, asp, gln, glu, gly, ile, leu, lys, phe, thr, tyr and val. |
1998-02-04 |
2023-08-12 |
Not clear |