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Wyszukujesz frazę "proteases" wg kryterium: Temat


Wyświetlanie 1-3 z 3
Tytuł:
Modes of inhibition of cysteine proteases.
Autorzy:
Rzychon, Malgorzata
Chmiel, Dorota
Stec-Niemczyk, Justyna
Powiązania:
https://bibliotekanauki.pl/articles/1041496.pdf
Data publikacji:
2004
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
cysteine proteases
serpins
inhibitors
cystatins
staphostatins
proteolysis
Opis:
Cysteine proteases are involved in many physiological processes and their hyperactivity may lead to severe diseases. Nature has developed various strategies to protect cells and whole organisms against undesired proteolysis. One of them is the control of proteolytic activity by inhibition. This paper presents the mechanisms underlying the action of proteinaceous inhibitors of cysteine proteinases and covers propeptides binding backwards relative to the substrate or distorting the protease catalytic centre similarly to serpins, the p35 protein binding covalently to the enzyme, and cystatins that are exosite binding inhibitors. The paper also discusses tyropins and chagasins that, although unrelated to cystatins, inhibit cysteine proteinases by a similar mechanism, as well as inhibitors of the apoptosis protein family that bind in a direction opposite to that of the substrate, similarly to profragments. Special attention is given to staphostatins, a novel family of inhibitors acting in an unusual manner.
Źródło:
Acta Biochimica Polonica; 2004, 51, 4; 861-873
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Znaczenie aktywności proteazy kapsydowej CP w rozwoju infekcji alfawirusowych
The role of capsid protease CP activity in the development of alphaviral infections
Autorzy:
Torzyk, Karolina
Skoreński, Marcin
Sieńczyk, Marcin
Powiązania:
https://bibliotekanauki.pl/articles/2200548.pdf
Data publikacji:
2022
Wydawca:
Polskie Towarzystwo Chemiczne
Tematy:
alfawirusy
arbowirusy
proteazy serynowe
proteaza kapsydowa CP
inhibitory
alphaviruses
arboviruses
serine proteases
capsid protease CP
inhibitors
Opis:
Alphaviruses belong to the worldwide distributed Togaviridae family and Alphavirus genus. They are spherical, enveloped, single-stranded RNA arthropodborne viruses. Alphaviruses are mostly transmitted by mosquitoes (Aedes spp. and Anopheles spp.) and are geographically distributed in restricted areas where appropriate vectors are present (Fig.1.). The most recognized members of this genus are Sindbis (SINV), Semliki Forest (SFV), Venezuelan equine encephalitis (VEEV), Ross River (RRV), and Chikungunya (CHIKV) viruses. Alphaviruses are infection agents for humans and many animals. Clinically, most human infections with arthritogenic alphaviruses are associated with symptoms such as fever, headache, joint pain, rash, chronic arthritis, and encephalitis. Major events during the alphaviral infection are virus entry, replication, assembly, and budding of new virions. Alphaviral RNA encodes four nonstructural and five structural proteins. Nonstructural proteins are mainly involved in the replication process and virus pathogenesis, while structural proteins form new virions. Both groups of viral proteins are produced as single polyproteins which undergo autoproteolytic maturation. This process is carried out by the two viral proteases, cysteine protease nsP4 and C protein serine protease (CP), and is considered to be critical for virus replication. The capsid protease CP is a chymotrypsin-like serine protease with the catalytic triad including His145, Asp167, and Ser219. What is important, after a suicidal autoproteolytic event the side chain of Trp267 remains bound in a hydrophobic S1 pocket thus inhibiting further trans-proteolytic activity. Alphaviral capsid protein undergoes a single proteolytic reaction before maturation and then, after selfinactivation, it assembles to form a viral capsid shell. Inhibitors of the capsid protease have significant antiviral activity. Compounds belonging to this group can be good candidates for new antiviral drugs.
Źródło:
Wiadomości Chemiczne; 2022, 76, 5-6; 309--321
0043-5104
2300-0295
Pojawia się w:
Wiadomości Chemiczne
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Nienaturalne aminokwasy jako strategia do otrzymywania substratów, inhibitorów i niskocząsteczkowych sond aktywności dla enzymów proteolitycznych
Unnatural amino acids as achemical tool for the development of protease substrates, inhibitors and activity - baseproblems
Autorzy:
Poręba, Marcin
Kasperkiewicz-Wasilewska, Paulina
Rut, Wioletta
Drąg, Marcin
Powiązania:
https://bibliotekanauki.pl/articles/2200587.pdf
Data publikacji:
2022
Wydawca:
Polskie Towarzystwo Chemiczne
Tematy:
proteolytic enzymes
substrate specificity
unnatural amino acids
substrates
inhibitors
activity-based probes
caspases
cathepsins
neuthrophil serine proteases
proteasome
SARS-CoV-2 proteases
enzymy proteolityczne
specyficzność substratowa
nienaturalne aminokwasy
niskocząsteczkowe sondy aktywności
kaspazy
katepsyny
proteasom
proteazy wirusa SARS-CoV-2
Opis:
Proteolytic enzymes are molecular scissors that are responsible for the amide bond breakdown in peptide and protein substrates. Over the years, the view on proteases has been considerably changed from non-specific digestive enzymes to sophisticated biocatalysts, which by performing limited proteolysis control virtually all biological processes. In order to better understand how proteases work and what are their biologically relevant target substrates, it is indispensable to determine their catalytic preferences. This knowledge can be further utilized to develop selective substrates, inhibitors and activity-based probes (ABPs) enabling the monitoring of proteases activity in various settings, from in vitro analysis on recombinant enzymes or cell lysates to ex vivo and in vivo imaging at the single cell level. Among many chemical-based approaches that have been developed and applied over the years, the Hybrid Combinatorial Substrate Library (HyCoSuL) technology has emerged as one of the most powerful one. HyCoSuL is a combinatorial peptide-based library of fluorogenic substrates, that comprise natural and unnatural amino acids, that can deeply explore the chemical space in proteases active site, providing a structural framework for the development of highly-selective chemical tools. In this review we present the most prominent examples of proteolytic enzymes that have been profiled with HyCoSuL approach yielding selective substrates, potent inhibitors, and very sensitive activity-based probes.
Źródło:
Wiadomości Chemiczne; 2022, 76, 5-6; 433--454
0043-5104
2300-0295
Pojawia się w:
Wiadomości Chemiczne
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-3 z 3

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