| Publication |
Sentence |
Publish Date |
Extraction Date |
Species |
| K Hiraga, K Yutan. Study of cysteine residues in the alpha subunit of Escherichia coli tryptophan synthase. 2. Role in enzymatic function. Protein engineering. vol 9. issue 5. 1996-12-05. PMID:8795043. |
to understand the functional roles of cys residues in the alpha subunit of tryptophan synthase from escherichia coli, single mutants of the alpha subunit, in which each of the three cys residues was substituted with ser, gly, ala or val, were constructed by site-directed mutagenesis. |
1996-12-05 |
2023-08-12 |
Not clear |
| K Hiraga, K Yutan. Study of cysteine residues in the alpha subunit of Escherichia coli tryptophan synthase. 2. Role in enzymatic function. Protein engineering. vol 9. issue 5. 1996-12-05. PMID:8795043. |
although the three cys residues are located away from the apparently important parts for enzymatic activity, substitutions at position 81 by ser, ala or val caused decreases in the intrinsic activity of the alpha subunit. |
1996-12-05 |
2023-08-12 |
Not clear |
| P Marchand, M Volkmann, J S Bon. Cysteine mutations in the MAM domain result in monomeric meprin and alter stability and activity of the proteinase. The Journal of biological chemistry. vol 271. issue 39. 1996-11-18. PMID:8798668. |
mutation of mouse meprin alpha cys-320 to ala in the mam domain (an extracellular domain found in meprin, a-5 protein, and receptor protein-tyrosine phosphatase mu) resulted in expression of a monomeric form of meprin, as determined by sds-polyacrylamide gel electrophoresis and nondenaturing gel electrophoresis. |
1996-11-18 |
2023-08-12 |
mouse |
| b' S Tuzi, A Naito, H Sait\\xc3\\xb. Temperature-dependent conformational change of bacteriorhodopsin as studied by solid-state 13C NMR. European journal of biochemistry. vol 239. issue 2. 1996-09-10. PMID:8706732.' |
no such spectral change in the absence of these cations was noted even if a preparation was cooled to -110 degrees c. the secondary structures of [3-13c]ala-labelled bacteriorhodopsin was not always identical at temperatures between ambient and low temperatures, since the 13c chemical shifts and relative peak intensities for purple membrane preparations containing these salts changed with temperature in the range -110 degrees c to 23 degrees c. in particular, we found that some residues involving ala residues at the alpha ii-helix and loop region were converted at temperatures below -60 degrees c to a conformation involving alpha 1-helix. |
1996-09-10 |
2023-08-12 |
Not clear |
| T Fujita, T Ito. Organization and nucleotide sequence of a gene cluster comprising the translation elongation factor 1 alpha, ribosomal protein S10 and tRNA(Ala) from Halobacterium halobium. Biochemistry and molecular biology international. vol 37. issue 1. 1996-07-31. PMID:8653072. |
lambda embl clone containing a gene cluster coding for the translation elongation factor 1alpha, ribosomal protein s10 and trna(ala) was identified in a genomic library for the halophilic archaebacterium halobacterium halobium using a pcr probe amplified by two oligonucleotide primers for conserved amino acid sequences of the elongation factor 1 alpha family. |
1996-07-31 |
2023-08-12 |
Not clear |
| H W Kim, T J Shen, N T Ho, M Zou, M F Tam, C H. Contributions of asparagine at alpha 97 to the cooperative oxygenation process of hemoglobin. Biochemistry. vol 35. issue 21. 1996-07-17. PMID:8639610. |
to clarify the structural and functional roles of the hydrogen bond between alpha 97asn and beta 99asp, we have engineered a recombinant hemoglobin in which alpha 97asn is replaced by ala, and have investigated its oxygen-binding properties, and have used proton nuclear magnetic resonance spectroscopy to determine the structural consequences of the mutation. |
1996-07-17 |
2023-08-12 |
human |
| H W Kim, T J Shen, N T Ho, M Zou, M F Tam, C H. Contributions of asparagine at alpha 97 to the cooperative oxygenation process of hemoglobin. Biochemistry. vol 35. issue 21. 1996-07-17. PMID:8639610. |
recombinant hb (alpha 97asn-->ala) shows a milder alteration of functional properties compared to the severely impaired beta 99 mutants of the human abnormal hemoglobins. |
1996-07-17 |
2023-08-12 |
human |
| H W Kim, T J Shen, N T Ho, M Zou, M F Tam, C H. Contributions of asparagine at alpha 97 to the cooperative oxygenation process of hemoglobin. Biochemistry. vol 35. issue 21. 1996-07-17. PMID:8639610. |
the addition of inositol hexaphosphate, an allosteric effector, causes recovery of the functional properties of recombinant hb (alpha 97 asn-->ala) almost to the level of human normal adult hemoglobin without this allosteric effector. |
1996-07-17 |
2023-08-12 |
human |
| H W Kim, T J Shen, N T Ho, M Zou, M F Tam, C H. Contributions of asparagine at alpha 97 to the cooperative oxygenation process of hemoglobin. Biochemistry. vol 35. issue 21. 1996-07-17. PMID:8639610. |
r hb (alpha 97 asn-->ala) shows very similar tertiary structure around the heme pockets and quaternary structure in the alpha 1 beta 2 interface compared to those of human normal adult hemoglobin. |
1996-07-17 |
2023-08-12 |
human |
| H W Kim, T J Shen, N T Ho, M Zou, M F Tam, C H. Contributions of asparagine at alpha 97 to the cooperative oxygenation process of hemoglobin. Biochemistry. vol 35. issue 21. 1996-07-17. PMID:8639610. |
preliminary molecular dynamics simulations have been used to calculate the contributions of specific interactions of several amino acid residues in r hb (alpha 97asn-->ala) to the free energy of cooperativity of this recombinant hemoglobin. |
1996-07-17 |
2023-08-12 |
human |
| H Wajcman, Y Blouquit, A Lahary, A M Soummer, P Groff, J Bardakdjian, C Préhu, J Riou, C Godard, F Galactèro. Three new neutral alpha chain variants: Hb Bois Guillaume [alpha 65(E14(Ala-->Val], Hb Mantes-la-Jolie [alpha 79(EF8)Ala-Thr], and Hb Mosella [alpha 111(G18)Ala-->Thr]. Hemoglobin. vol 19. issue 5. 1996-02-05. PMID:8537232. |
three new neutral alpha chain variants: hb bois guillaume [alpha 65(e14(ala-->val], hb mantes-la-jolie [alpha 79(ef8)ala-thr], and hb mosella [alpha 111(g18)ala-->thr]. |
1996-02-05 |
2023-08-12 |
Not clear |
| S V Cattini-Schultz, P G Stanton, D M Robertson, M T Hear. Contribution of specific amino acid residues within the hFSH alpha 26-46 sequence region to FSH receptor-binding activity. Peptide research. vol 8. issue 4. 1996-01-30. PMID:8527875. |
set 1 included two overlapping peptides (alpha 25-41 and alpha 31-45) spanning the alpha 26-46 region, while sets 2-6 included peptides of different size or structure in which the alpha 26-46 sequence was (i) sequentially truncated either from the n-terminus or from the c-terminus or both; (ii) alternatively reduced to a series of overlapping 13-mer peptides; or (iii) modified at the c-terminal arg and lys residues with substitution by ala residues. |
1996-01-30 |
2023-08-12 |
human |
| M Kimura, A Ishiham. Functional map of the alpha subunit of Escherichia coli RNA polymerase: amino acid substitution within the amino-terminal assembly domain. Journal of molecular biology. vol 254. issue 3. 1996-01-04. PMID:7490753. |
new types of assembly-deficient mutants were identified: alpha-r45a (having substituted ala for arg at residue 45) dimerized but did not assemble beta (and beta') subunits; and alpha-l48a showed a decreased level of alpha 2 beta subassembly formation, indicating that this region (residues 45 to 48) is responsible for beta-binding. |
1996-01-04 |
2023-08-12 |
Not clear |
| M Runnegar, N Berndt, S M Kong, E Y Lee, L Zhan. In vivo and in vitro binding of microcystin to protein phosphatases 1 and 2A. Biochemical and biophysical research communications. vol 216. issue 1. 1995-12-21. PMID:7488083. |
we demonstrate that the bond resulted from the reaction between the electrophilic alpha, beta unsaturated carbonyl of the methyldehydroalanine residue of mcyst and the thiol of cys 273 located in the c-terminal of pp1 (cys 266 in pp2a), since site-directed mutagenesis of cys 273 to ala in pp1 alpha led to complete loss of ability for the formation of a covalent mcyst-pp1 adduct. |
1995-12-21 |
2023-08-12 |
Not clear |
| A Dumoulin, L Kiger, R Jiang, V Baudin, C Vasseur, S G Sligar, M C Marden, J Pagnier, C Poyar. Loss of allosteric behaviour in recombinant hemoglobin alpha 2 beta 2(92)(F8) His-->Ala: restoration upon addition of strong effectors. FEBS letters. vol 374. issue 1. 1995-12-05. PMID:7589508. |
loss of allosteric behaviour in recombinant hemoglobin alpha 2 beta 2(92)(f8) his-->ala: restoration upon addition of strong effectors. |
1995-12-05 |
2023-08-12 |
Not clear |
| I L Karle, D Ranganatha. Polymethylene spacer linked bis(Ala) peptides form modified beta-sheet structures. Crystal structure and self-assembly pattern of adipoyl and suberoyl analogues. International journal of peptide and protein research. vol 46. issue 1. 1995-11-13. PMID:7558593. |
the adipoyl- and suberoyl-linked bis(ala) peptides have an extended backbone between the two c alpha atoms in each molecule. |
1995-11-13 |
2023-08-12 |
Not clear |
| D D Beusen, L M McDowell, U Slomczynska, J Schaefe. Solid-state nuclear magnetic resonance analysis of the conformation of an inhibitor bound to thermolysin. Journal of medicinal chemistry. vol 38. issue 14. 1995-09-01. PMID:7629812. |
the 31p-13c', 31p-15n, and 31p-13c alpha distances (3.61 +/- 0.10, 3.89 +/- 0.12, and 5.37 +/- 0.13 a, respectively) measured in a complex of cbz-glyp-[1-13c]leu-[15n,2-13c]ala and the enzyme are consistent with those observed by x-ray diffraction in other comparable thermolysin/inhibitor complexes (average values of 3.58 +/- 0.04, 3.91 +/- 0.13, and 5.17 +/- 0.18 a, respectively). |
1995-09-01 |
2023-08-12 |
Not clear |
| E G Kazanetz, J Y Leonova, J B Wilson, S K McMillan, M Walbrecht, J M de Pablos Gallego, T H Huisma. Hb Anamosa or alpha 2(111)(G18)Ala-->Val beta 2 (alpha 2 mutation) and Hb Mulhacen or alpha 2(123)(H6)Ala-->Ser beta 2 (alpha 1 mutation) are two silent, stable variants detected by sequencing of amplified DNA. Hemoglobin. vol 19. issue 1-2. 1995-08-24. PMID:7615398. |
hb anamosa or alpha 2(111)(g18)ala-->val beta 2 (alpha 2 mutation) and hb mulhacen or alpha 2(123)(h6)ala-->ser beta 2 (alpha 1 mutation) are two silent, stable variants detected by sequencing of amplified dna. |
1995-08-24 |
2023-08-12 |
Not clear |
| E G Kazanetz, J Y Leonova, J B Wilson, S K McMillan, M Walbrecht, J M de Pablos Gallego, T H Huisma. Hb Anamosa or alpha 2(111)(G18)Ala-->Val beta 2 (alpha 2 mutation) and Hb Mulhacen or alpha 2(123)(H6)Ala-->Ser beta 2 (alpha 1 mutation) are two silent, stable variants detected by sequencing of amplified DNA. Hemoglobin. vol 19. issue 1-2. 1995-08-24. PMID:7615398. |
both involve an alanine residue in the core peptide, namely ala-->val at position 111 (codon change in the alpha 2 gene; gcc->gtc; hb anamosa) and ala-->ser at position 123 (codon change in the alpha 1 gene; gcc-->tcc; hb mulhacen). |
1995-08-24 |
2023-08-12 |
Not clear |
| M Kimura, A Ishiham. Functional map of the alpha subunit of Escherichia coli RNA polymerase: insertion analysis of the amino-terminal assembly domain. Journal of molecular biology. vol 248. issue 4. 1995-06-20. PMID:7752238. |
for fine mapping of the site(s) within this region required for subunit-subunit contacts, we constructed a set of insertion mutants of the rpoa gene, each encoding mutant alpha with two extra amino acid residues, ala (a) and ser (s), inserted at 20 residue intervals. |
1995-06-20 |
2023-08-12 |
Not clear |