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「RNASE」の共起表現一覧(1語右で並び替え)

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s gene and the gene that encodes ribonuclease, RNase A family, 4 share promoters and 5' exons.
The importance of bovine pancreatic RNase A was secured when the Armour & Co. (of hot do
The positive charges of RNase A lie mainly in a deep cleft between two lobes
If RNase A is digested with subtilisin, a single peptid
The N-terminal α-helix of RNase A (residues 3-13) is connected to the rest of
a single lot of purified enzyme instantly made RNase a predominant model system for protein studies
eptide derived from pancreatic ribonuclease A ( RNase A).
The N-terminus of the original RNase A, also called S-peptide, consists of 20 amino
he key catalytic residues of bovine pancreatic RNase A, it cleaves standard RNA substrates 105-106
lar to other ribonucleases such as barnase and RNase A, ribonuclease T1 has been popular for foldin
cal to that of bovine pancreatic ribonuclease ( RNase) A. Moreover, although Ang has the same genera
sts double strands RNA (dsRNS)-Dicer family of RNAse, cutting pre-miRNA (60-70bp long) at a specifi
Exoribonucleases can be single proteins (like RNase D or RNase PH) but also can be complexes of mu
RNase D has homologues in many other organisms.
RNase D is one of the seven exoribonucleases identif
r protein has a domain that is very similar to RNase D, this is called an RNase D domain.
onger precursor RNAs that are processed by the RNase Dicer/DCR-1 and members of the RDE-1/AGO1 fami
ne-II RNAs fulfill the same functional role as RNase E 5' UTR elements, which is to regulate the le
ting by binding to FinP and protecting it from RNase E degradation.
targets the mgtA transcript for degradation by RNase E when cells are grown in high Mg2+ environmen
The RNase E 5' UTR element is a previously identified RN
(5' UTRs) of genes that encode Ribonuclease E ( RNase E).
ell, this is dependent on the endoribonuclease RNase E.
ding enzymes: polynucleotide phosphorylase and RNase E. Polynucleotide phosphorylase binds to the 3
Its protein product is an RNase enzyme homologous to the yeast protein Rrp44,
o its lysing action, is to prevent activity of RNase enzymes and DNase enzymes by denaturing them.
Other proteins belonging to the pancreatic RNAse family include: bovine seminal vesicle and bra
n human immunodeficiency virus type 1 (HIV-1), RNase H exists as a domain in the heterodimeric HIV-
Proposed HIV-1 RNase H mechanism
eplication intermediate and must be cleaved by RNase H before the process can continue.
It was found that both the RNase H domain and the enzyme reverse transcriptase
tested for reverse transcriptase activity and RNase H activity.
Members of the RNase H family can be found in nearly all organisms,
The enzyme RNase H is a non-specific endonuclease and catalyzes
RNase H performs three types of cleaving actions: no
Rather RNase H creates a "primer" from the purine-rich poly
of polynucleotidyl transferases that includes RNase H, RuvC Holliday resolvase, RAG proteins, and
ExoIII has also been reported to have RNase H, 3´-phosphatase and AP-endonuclease activiti
mbe contains at least a piwi domain-containing RNase H-like argonaute, a chromodomain protein Chp1,
ligonucleotide to allow cleavage by the enzyme RNase H.
h an endoribonuclease such as Escherichia coli RNase III or dicer.
This RNA is subsequently digested with RNase III from Escherichia coli to generated short o
Dicer contains two RNase III domains and one PAZ domain; the distance b
The distance between the RNase III and PAZ domains, determined by the length
Dicer is an endoribonuclease in the RNase III family that cleaves double-stranded RNA (d
into a 21 nucleotides long mature miRNA by the RNAse III family endoribonuclease dicer.
The RNase III domains are colored green, the PAZ domain
Example includes both single proteins like RNase III, RNase A, RNase T1 and RNase H but also, c
RNase MRP is an enzymatically active ribonucleoprote
Co-precipitation of U19 snoRNA with RNase MRP RNA suggests that U19 may be involved in p
Despite distinct functions, RNase MRP has been shown to be evolutionarily relate
utations near or within the ncRNA component of RNase MRP, RMRP, has been identified.
don't generally matter unless a peptide is an RNase or DNase, and then only if the enzyme manages
started the work that led to the discovery of RNase P and the enzymatic properties of the RNA subu
Recent findings also reveal that RNase P has a new function .
Examples: rRNA/rDNA, RNase P RNA, ATPase, RecA protein (involved in genet
It has been shown that human nuclear RNase P is required for the normal and efficient tra
The pseudoknot region of RNase P is one of the most conserved elements in all
P3, P4, and P10/11 are common to all cellular RNase P RNAs.
ng sequences and was the first to characterize RNase P and its activity in processing of the 5' lea
Further RNase P is one of two known multiple turnover ribozy
RNase P is unique from other RNases in that it is a
Isolated eukaryotic and archaeal RNase P RNA has not been shown to retain its catalyt
Bacterial RNase P has two components: an RNA chain, called M1
In molecular biology, nuclear ribonuclease P ( RNase P) is a ubiquitous endoribonuclease, found in
Ribonuclease P ( RNase P) is a type of ribonuclease which cleaves RNA
RNase PH is an 3'-5' exoribonuclease and nucleotidyl
y a homohexameric complex, consisting of three RNase PH dimers.
RNase PH has homologues in many other organisms, whi
n use include phosphate-dependent exonuclease, RNase PH, and ribonuclease PH.
r protein has a domain that is very similar to RNase PH, this is called an RNase PH domain (RPD).
by several different methods including RT-PCR, RNase protection assays, microarrays, serial analysi
Cellular RNase Ps are ribonucleoproteins.
The RNA from bacterial RNase Ps retains its catalytic activity in the absen
RNase R is an 3'-5' exoribonuclease closely related
RNase R has homologues in many other organisms.
r protein has a domain that is very similar to RNase R, this is called an RNase R domain.
Owing to its specificity for guanine, RNase T1 is often used to digest denatured RNA prior
RNase T1 has two disulfide bonds, Cys2-Cys10 and Cys
RNase T1 also has four prolines, two of which (Pro39
Ribonuclease T1 (sometimes abbreviated RNase T1) is a fungal endonuclease that cleaves sing
analysis to the study of barnase, a bacterial RNAse used in many protein folding studies.
RNase V1 is non-sequence specific for double-strande
                                                                                                   


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