-
Je něco špatně v tomto záznamu ?
15gag proteinase of myeloblastosis-associated virus: specificity studies with substrate-based inhibitors
L Pavlickova, D Stys, M Soucek, J Urban, O Hruskova, J Sedlacek, P Strop
Jazyk angličtina Země Spojené státy americké
Typ dokumentu srovnávací studie
Grantová podpora
PL19
MZ0
CEP - Centrální evidence projektů
- MeSH
- aspartátové endopeptidasy * antagonisté a inhibitory MeSH
- HIV-1 enzymologie MeSH
- HIV-proteasa metabolismus MeSH
- inhibitory proteas farmakologie chemická syntéza MeSH
- kinetika MeSH
- molekulární sekvence - údaje MeSH
- oligopeptidy farmakologie chemická syntéza MeSH
- sekvence aminokyselin MeSH
- substrátová specifita MeSH
- virus ptačí myeloblastózy * enzymologie MeSH
- vztahy mezi strukturou a aktivitou MeSH
- Publikační typ
- srovnávací studie MeSH
The specificity of the proteinase of myeloblastosis-associated virus (MAV) was studied with (a) 21 substrate-based inhibitors, (b) 9 inhibitors with pseudopalindrome sequences, (c) 8 chimeric inhibitors, and (d) 3 compounds designed as human immunodeficiency virus 1 (HIV-1) proteinase inhibitors. The central inhibitory unit (transition state or cleaved bond analog) and the role of the inhibitor side chains from P4 to P4' were investigated. MAV proteinase prefers an aromatic side chain in P1 and a small aliphatic nonpolar chain in P2 and P2'. Residues in P5 and P4 positions are outside of the short catalytic cleft of the enzyme, but still influence binding considerably. The data obtained provide evidence that the MAV proteinase has generally lower specificity and poorer binding than the HIV proteinase.
Institute of Molecular Genetics Czechoslovak Academy of Science Prague Czechoslovakia
Institute of Organic Chemistry and Biochemistry Czechoslovak Academy of Science Prague
Citace poskytuje Crossref.org
Literatura
- 000
- 00000naa a2200000 a 4500
- 001
- bmc13027641
- 003
- CZ-PrNML
- 005
- 20130827103904.0
- 007
- ta
- 008
- 130826s1992 xxu f 000 0|eng||
- 009
- AR
- 024 __
- $a 10.1016/0003-9861(92)90476-d $2 doi
- 035 __
- $a (PubMed)1417001
- 040 __
- $a ABA008 $d ABA008 $e AACR2 $b cze
- 041 0_
- $a eng
- 044 __
- $a xxu
- 100 1_
- $a Pavlíčková, Libuše $7 _AN054697 $u Institute of Organic Chemistry and Biochemistry, Czechoslovak Academy of Science, Prague
- 245 10
- $a 15gag proteinase of myeloblastosis-associated virus: specificity studies with substrate-based inhibitors / $c L Pavlickova, D Stys, M Soucek, J Urban, O Hruskova, J Sedlacek, P Strop
- 504 __
- $a Literatura
- 520 9_
- $a The specificity of the proteinase of myeloblastosis-associated virus (MAV) was studied with (a) 21 substrate-based inhibitors, (b) 9 inhibitors with pseudopalindrome sequences, (c) 8 chimeric inhibitors, and (d) 3 compounds designed as human immunodeficiency virus 1 (HIV-1) proteinase inhibitors. The central inhibitory unit (transition state or cleaved bond analog) and the role of the inhibitor side chains from P4 to P4' were investigated. MAV proteinase prefers an aromatic side chain in P1 and a small aliphatic nonpolar chain in P2 and P2'. Residues in P5 and P4 positions are outside of the short catalytic cleft of the enzyme, but still influence binding considerably. The data obtained provide evidence that the MAV proteinase has generally lower specificity and poorer binding than the HIV proteinase.
- 590 __
- $a bohemika - dle Pubmed
- 650 02
- $a sekvence aminokyselin $7 D000595
- 650 12
- $a aspartátové endopeptidasy $x antagonisté a inhibitory $7 D016282
- 650 12
- $a virus ptačí myeloblastózy $x enzymologie $7 D009189
- 650 02
- $a HIV-proteasa $x metabolismus $7 D016333
- 650 02
- $a HIV-1 $x enzymologie $7 D015497
- 650 02
- $a kinetika $7 D007700
- 650 02
- $a molekulární sekvence - údaje $7 D008969
- 650 02
- $a oligopeptidy $x farmakologie $x chemická syntéza $7 D009842
- 650 02
- $a inhibitory proteas $x farmakologie $x chemická syntéza $7 D011480
- 650 02
- $a vztahy mezi strukturou a aktivitou $7 D013329
- 650 02
- $a substrátová specifita $7 D013379
- 655 _2
- $a srovnávací studie $7 D003160
- 700 1_
- $a Štys, Dalibor, $d 1962- $7 uzp2008440404 $u Institute of Organic Chemistry and Biochemistry, Czechoslovak Academy of Science, Prague
- 700 1_
- $a Souček, Milan, $d 1930- $7 jk01120477 $u Institute of Organic Chemistry and Biochemistry, Czechoslovak Academy of Science, Prague
- 700 1_
- $a Urban, Jan $u Institute of Organic Chemistry and Biochemistry, Czechoslovak Academy of Science, Prague
- 700 1_
- $a Hrušková-Heidingsfeldová, Olga $7 xx0060514 $u Institute of Organic Chemistry and Biochemistry, Czechoslovak Academy of Science, Prague
- 700 1_
- $a Sedláček, Juraj $7 xx0128467 $u Institute of Molecular Genetics, Czechoslovak Academy of Science, Prague, Czechoslovakia
- 700 1_
- $a Štrop, Petr $7 xx0247035 $u Institute of Organic Chemistry and Biochemistry, Czechoslovak Academy of Science, Prague
- 773 0_
- $t Archives of biochemistry and biophysics $x 0003-9861 $g Roč. 298, č. 2 (1992), s. 753-756 $p Arch Biochem Biophys $w MED00009241
- 773 0_
- $p Arch Biochem Biophys $g 298(2):753-6, 1992 Nov 1 $x 0003-9861
- 910 __
- $a ABA008 $b B 410 $y 3 $z 0
- 990 __
- $a 20130826094108 $b ABA008
- 991 __
- $a 20130827104343 $b ABA008
- 999 __
- $a ok $b bmc $g 991613 $s 826070
- BAS __
- $a 3
- BMC __
- $a 1992 $b 298 $c 2 $d 753-756 $i 0003-9861 $m Archives of biochemistry and biophysics $x MED00009241 $n Arch Biochem Biophys
- GRA __
- $a PL19 $p MZ0
- LZP __
- $a 2013-08/išbo
