The effect of modifications of the A5 and A19 amino acid residues on the biological activity of insulin. [Leu5-A] and [Phe19-A] sheep insulins

1983 ◽  
Vol 2 (2) ◽  
pp. 147-170 ◽  
Author(s):  
Nicolaos Ferderigos ◽  
G. Thompson Burke ◽  
Kouki Kitagawa ◽  
Panayotis G. Katsoyannis
Keyword(s):  
Biological Activity ◽  
Amino Acid ◽  
Amino Acid Residues

Biological Function and Chemistry of Endothelin. A Review

1999 ◽  
Vol 64 (8) ◽  
pp. 1211-1252 ◽  
Author(s):  
Jan Hlaváček ◽  
Renáta Marcová
Keyword(s):  
Biological Activity ◽  
Amino Acid ◽  
Biological Function ◽  
Biological Properties ◽  
Structural Basis ◽  
Amino Acid Residues ◽  
Snake Venoms ◽  
Vasoactive Peptides ◽  
Physico Chemical ◽  
Endothelin A

The first part of this review deals with the biosynthesis and a biological function of strongly vasoactive peptides named endothelins (ETs) including vasoactive intestinal contractor. Where it was useful, snake venoms sarafotoxins which are structural endothelin derivatives, were also mentioned. In the second part, an attention is paid to structural basis of the ETs biological activity, with respect to alterations of amino acid residues in the parent peptides modifying the conformation and consequently the physico-chemical and biological properties in corresponding ETs analogs. Special attention is focussed on the area of ETs receptors and their interaction with peptide and non peptide agonists and antagonists, important in designing selective inhibitors of ETs receptors potentially applicable as drugs in a medicine. A review with 182 references.

Metal complexes of polymers with amino acid residues. formation, stability and controlled biological activity

1990 ◽  
Vol 14 (1) ◽  
pp. 61-70 ◽  
Author(s):  
V.A. Lee ◽  
R.I. Musin ◽  
R.I. Tashmukhamedov ◽  
M.I. Shtilman ◽  
S.Sh. Rashidova
Keyword(s):  
Biological Activity ◽  
Amino Acid ◽  
Metal Complexes ◽  
Amino Acid Residues

Structure-activity studies of dermorphin. The role of side chains of amino acid residues on the biological activity of dermorphin

Peptides ◽  
1984 ◽  
Vol 5 (4) ◽  
pp. 687-689 ◽  
Author(s):  
Krzysztof Darłak ◽  
Zbigniew Grzonka ◽  
Pawel Krzaścik ◽  
Piotr Janicki ◽  
S.Witold Gumułka
Keyword(s):  
Biological Activity ◽  
Amino Acid ◽  
Side Chains ◽  
Amino Acid Residues ◽  
Structure Activity

scholarly journals Identification of Amino Acid Residues Critical for Biological Activity in Human Interleukin-18

2002 ◽  
Vol 277 (13) ◽  
pp. 10998-11003 ◽  
Author(s):  
Soo-Hyun Kim ◽  
Tania Azam ◽  
Daniela Novick ◽  
Do-Young Yoon ◽  
Leonid L. Reznikov ◽  
...  
Keyword(s):  
Biological Activity ◽  
Amino Acid ◽  
Amino Acid Residues ◽  
Interleukin 18

Interaction between the A2 and A19 amino acid residues is of critical importance for high biological activity in insulin: [19-leucine-A]insulin

Biochemistry ◽  
1984 ◽  
Vol 23 (19) ◽  
pp. 4444-4448 ◽  
Author(s):  
Kouki Kitagawa ◽  
Hiroshi Ogawa ◽  
G. Thompson Burke ◽  
Jacob D. Chanley ◽  
Panayotis G. Katsoyannis
Keyword(s):  
Biological Activity ◽  
Amino Acid ◽  
Amino Acid Residues ◽  
Critical Importance ◽  
High Biological Activity

scholarly journals The amino acid sequence of ribonuclease U2 from Ustilago sphaerogena

1975 ◽  
Vol 145 (2) ◽  
pp. 353-360 ◽  
Author(s):  
S Sato ◽  
T Uchida
Keyword(s):  
Biological Activity ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Crucial Role ◽  
Science And Technology ◽  
British Library ◽  
Amino Acid Residues ◽  
Complete Amino Acid Sequence ◽  
Lending Library

1. RNAase (ribonuclease) U2, a purine-specific RNAase, was reduced, aminoethylated and hydrolysed with trypsin, chymotrypsin and thermolysin. On the basis of the analyses of the resulting peptides, the complete amino acid sequence of RNAase U2 was determined, 2. When the sequence was compared with the amino acid sequence of RNAase T1 (EC 3.1.4.8), the following regions were found to be similar in the two enzymes; Tyr-Pro-His-Gln-Tyr (38-42) in RNAase U2 and Tyr-Pro-His-Lys-Tyr (38-42) in RNAase T1, Glu-Phe-Pro-Leu-Val (61-65) in RNAase U2 and Glu-Trp-Pro-Ile-Leu (58-62) in RNAase T1, Asp-Arg-Val-Ile-Tyr-Gln (83-88) in RNAase U2 and Asp-Arg-Val-Phe-Asn (76-81) in RNAase T1 and Val-Thr-His-Thr-Gly-Ala (98-103) in RNAase U2 and Ile-Thr-His-Thr-Gly-Ala (90-95) in RNAase T1. All of the amino acid residues, histidine-40, glutamate-58, arginine-77 and histidine-92, which were found to play a crucial role in the biological activity of RNAase T1, were included in the regions cited here. 3. Detailed evidence for the amino acid sequence of the sequence of the proteins has been deposited as Supplementary Publication SUP 50041 (33 PAGES) AT THE British Library (Lending Division)(formerly the National Lending Library for Science and Technology), Boston Spa, Yorks. LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1975), 145, 5.

scholarly journals Disease mutation study identifies essential residues for phosphatidylserine flippase ATP11A

2020 ◽  
Author(s):  
Kuanxiang Sun ◽  
Wanli Tian ◽  
Wenjing Liu ◽  
Yeming Yang ◽  
Xianjun Zhu
Keyword(s):  
Biological Activity ◽  
Amino Acid ◽  
Lipid Bilayer ◽  
Mutation Analysis ◽  
Cellular Function ◽  
Amino Acid Residues ◽  
Β Subunit ◽  
Mutant Proteins ◽  
Myotube Formation ◽  
Insight Into

AbstractPS flippase (P4-ATPase) transports PS from the outer to the inner leaflet of the lipid bilayer in the membrane to maintain PS asymmetry, which is important for biological activity of the cell. ATP11A is expressed in multiple tissues and plays a role in myotube formation. However, detailed cellular function of ATP11A remains elusive. Mutation analysis revealed that I91, L308 and E897 residues in ATP8A2 are important for flippase activity. In order to investigate the roles of these corresponding amino acid residues in ATP11A, we assessed the expression and flippase activity of the respective ATP11A mutant proteins. ATP11A mainly localizes to the Golgi when co-expressed with TMEM30A, the β-subunit of the complex. Y300F and D913K mutations affect correct Golgi localization and PS stimulated flippase activity. In addition, Y300F mutation causes reduced ATP11A expression. Our data provides insight into essential residues for expression and flippase activity of ATP11A.

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