「C-terminal」の共起表現(1語右で並び替え)

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共起表現

「C-terminal」の共起表現一覧(1語右で並び替え)

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RLI has two	C-terminal ABC domains; upon binding ATP they form a ch
a gene family whose products hydrolyze small	C-terminal adducts of ubiquitin to generate the ubiquit
ning an RNP-2-like consensus sequence; and a	C-terminal alpha-helical domain.
	C-terminal amidation
Carboxypeptidase E cleaves	C-terminal amino acid residues and is involved in neuro
It does that by cleaving off basic	C-terminal amino acids, producing the active form of th
lar anti-parallel beta sheets, followed by a	C-terminal amphipathic helix.
ts N-terminal a pyrin domain(PYD) and at its	C-terminal an FIIND motif and a CARD which distinguishe
He refined a method of	C-terminal analysis that was used in early sequencing w
ctrin homology located at 228-380 within the	C-terminal), and a putative coiled coil domain at amino
y an intramolecular attack by the soon-to-be	C-terminal asparagine.
led caspases that cleave their substrates at	C-terminal aspartic acid residues.
des), a second step involving the removal of	C-terminal basic residues is required; this step is med
l domain involved in receptor binding; and a	C-terminal beta-sandwich domain (IPR005638) that intera
catalytic (beta/alpha)(8)-like domain and a	C-terminal beta-sandwich domain.
tiation, n for N-terminal capping, and c for	C-terminal capping.
The	C-terminal carboxylate group of a polypeptide can also
and III through XV) based on their variable	C-terminal cargo-binding domains.
The structure of the presenilin-1	C-terminal catalytic fragment was determined using solu
The	C-terminal catalytic domain has a typical restriction e
The protein is also a receptor for the	C-terminal cell binding domain of thrombospondin, and i
e divergent region between the WD domain and	C-terminal coiled coil region.
requirement for its activation) through its	C-terminal coiled-coil domain (CCC), but remains in an
nyl groups onto two cysteine residues at the	C-terminal consensus sequence CXC or XXCC.
A	C-terminal conserved domain within this enzyme contains
tion of two geranylgeranyl groups on the two	C-terminal cysteines.
the exposed part of the binding groove, the	C-terminal cytoplasmic region interact with the other c
lasmic region, a transmembrane region, and a	C-terminal cytoplasmic region (middle and C-terminal do
a single transmembrane domain, and a short,	C-terminal cytoplasmic tail.
Through its	C-terminal death domain, this protein can be recruited
tical polypeptide chains linked by a pair of	C-terminal disulfide bonds.
omain of about 90 kDa separated from a basic	C-terminal domain of about 25 kDa by a proline-rich reg
minal "arm", containing two α-helices, and a	C-terminal domain with an unusual four-layered structur
length, a protein kinase domain and a short	C-terminal domain containing 15 to 20 residues.
gion of the cathepsin F precursor contains a	C-terminal domain similar to the pro-segment of catheps
The BRCT domain (after the	C_terminal domain of a breast cancer susceptibility pro
r165, Val6, Tyr164, Ser146, and Gly96 at the	C-terminal domain and Ser41, Thr50, Gly 62, Ala64, Ser6
th N-terminal domain of the α subunit; and a	C-terminal domain consisting of a β-roll and one short
d alpha/beta barrel at the N terminus, and a	C-terminal domain essentially composed of beta-strand.
The	C-terminal domain enters the phospholipid bilayer.
	C-terminal domain of restriction endonuclease BfiI (PDB
Specifically, the	c-terminal domain interacts with amphiphysin, endophili
The domain of interest is the	C-terminal domain which consists of three subdomains su
Other proteins often bind the	C-terminal domain of RNA polymerase in order to activat
eukaryote Pneumocystis carinii, DHPS is the	C-terminal domain of a multifunctional folate synthesis
his alters the 19th and 20th residues of the	C-terminal domain thereby altering the 2° structure of
functions as a coactivator and binds to the	C-terminal domain of RNA polymerase II holoenzyme, acti
tide substrates, MgATP or MgADP, bind to the	C-terminal domain of the enzyme.
s: an alpha helical N-terminal domain, and a	C-terminal domain composed of beta sheets.
n, a transmembrane region, and a cytoplasmic	C-terminal domain (Pereira 14).
proteins is the catalytic domain, while the	C-terminal domain is a pseudocatalyitc domain.
the anti-neural function protein SCP1 (small	C-terminal domain phosphatase 1).
The	C-terminal domain, has five disulfide bridges.
ates with RNA polymerase II, and through the	C-terminal domain, also interacts with histone deacetyl
ains, a small N-terminal domain, and a large	C-terminal domain.
inds to the initiation factor eIF-4G via its	C-terminal domain.
domain at its N-terminus and a proline-rich	C-terminal domain.
The	C-terminal domains of both MLSA2 and MLSB includes a th
, encodes a proteins that lacks a homologous	C-terminal domains, but as in mammals it acts as a part
It is bound at its	C-terminal end (a lysine) by a covalent bond to the pep
the bottle", associating especially with the	C-terminal end of RI; the interaction is largely electr
ane 4 times, with the N-terminal end and the	C-terminal end both located in the cytoplasm, and two e
s usually very short (4-10 amino acids), the	C-terminal end varies in length from 21 to 63 and is ne
for writing peptide sequences is to put the	C-terminal end on the right and write the sequence from
nultimate lysine and proline residues on the	C-terminal end of the B-chain are reversed.
The γ secretase, which produces the	C-terminal end of the Aβ peptide, cleaves within the tr
also known as phosphophoryn), taken from the	C-terminal end, dentin sialoprotein from the N-terminal
-terminal end and one globular domain at the	C-terminal end, separated by a large domain heavily mod
region, and a short cytoplasmic tail at the	C-terminal end.
erminal end and a proline-rich domain at the	C-terminal end.
directional and have distinct N-terminal and	C-terminal ends, propagation parameters may differ in e
ely conserved), and in some cases a distinct	C-terminal extension (F-domain).
Several bacterial CO II have a	C-terminal extension that contains a covalently bound h
Transporters with a	C-terminal extension are proposed to have an additional
inus is cleaved in all of the proteins and a	C-terminal extension is cleaved in some members.
he long NALP, NALP1 (MIM 606636), also has a	C-terminal extension containing a function to find doma
peroxisomes the targeting sequence is on the	C-terminal extension mostly.
saic proteins, whereas others contain N- and	C-terminal extensions that show no sequence similarity
conserved transmembrane domain, and a short	C-terminal extracellular region.
the DEAH-box family of helicases with N- and	C-terminal flanking regions of ~180 and ~380 amino acid
to produce a larger N-terminal and a smaller	C-terminal fragment which together form part of the fun
It is the 8-amino acid	C-terminal fragment of cholecystokinin, and also known
e catalytic residue has been identified as a	C-terminal glutamate, but these do not form the charact
was found to be ubiquitin (truncated by two	C-terminal glycine residues).
ce similar to that of protein kinases, and a	C-terminal guanylate cyclase domain.
esponding part of E. coli GlnRS, whereas the	C-terminal half exhibits a GluRS-specific structure.
The	C-terminal half of BVR contains the catalytic domain, w
been observed, there is no evidence that the	C-terminal half of the IgIII domain of this protein var
ond, the nucleus makes the proteins with the	C-terminal half of the α-agglutinins.
s, which have the genes of proteins with the	C-terminal half of α-agglutinins, are added to yeast ce
ells genetically as fusion proteins with the	C-terminal half of α-agglutinin.
rdinated to Cys 19 & 23 which are present in	C-terminal half of the alpha helix.
which is characterized by two motifs in the	C-terminal half of the protein: a basic region involved
eta-barrel, while the NAD(P)-binding domain (	C-terminal) has the topology of a classical pyridine di
Heavy metal pumps can have several N- and	C-terminal heavy metal-binding domains that have been f
en transmembrane helices, although the three	C-terminal helices are conserved.
two helices are antiparallel and the longer	C-terminal helix is roughly perpendicular to the axes e
helix (alpha-1), a flexible loop and a long	C-terminal helix (alpha-2).
f the animal proteins may have an additional	C-terminal helix.
rminal cytosolic oxidoreductase domain and a	C-terminal heme-containing transmembrane domain.
C-terminus, and all isoforms have identical	C-terminal heptapeptides.
The cyclic,	C-terminal hexapeptide sequence((-CYS*-TRY-LYS-TRP-PHE-
It has an unusually long	C-terminal intracellular tail of approximately 60 amino
The	C-terminal J domain is responsible for the interaction
different subcellular locations such as the	C-terminal KDEL motif which marks proteins for endoplas
main, a NACHT-associated domain (NAD), and a	C-terminal leucine-rich repeat (LRR) region.
main, a NACHT-associated domain (NAD), and a	C-terminal leucine-rich repeat (LRR) region.
calization signal; a central NACHT domain; a	C-terminal leucine-rich repeat (LRR) domain.
chains of the N-terminal methionines and the	C-terminal leucines of both subunits are immobilized in
ontains an N-terminal DNA binding domain and	C-terminal ligand binding domain and is localized to th
oRII monomer has two domains, N-terminal and	C-terminal, linked through a hinge loop.
Like NLRCs, NLRPs contain	C-terminal LRRs, which appear to act as regulatory doma
ames in common use include farnesyl cysteine	C-terminal methyltransferase, farnesyl-protein carboxym
The	C-terminal motif is required for association with LSm p
act both physically and functionally and the	C-terminal motif of Prp24 is important for this interac
Mutation of the two prolines within the	C-terminal motif results in reduced proliferation and I
ogranins and secretogranins together share a	C-terminal motif, whereas chromogranins A and B share a
n N-terminal cytochrome b5-like domain and a	C-terminal multiple membrane-spanning desaturase portio
drugs are known to bind to the S6 domain or	C-terminal of the hERG-channel.
The positively charged surface (	C-terminal) of SloTx has a specific short-range interac
helix bundle, formed by the seven amino-acid	C-terminal of CFP-10, is essential for binding and atta
(6xHis tag) residues which are added at the	C-terminal or N-terminal of the protein of interest.
ntains a SH3 domain, a SH2 domain and in the	C-terminal part the tyrosine kinase domain.
The	C-terminal peptide is constitutively expressed in sweat
on is exclusively attributed to the secreted	C-terminal peptide, while the N-terminal product may pl
h the outer membrane is contained within the	C-terminal portion of the translated protein itself, wh
The N-terminal and the	C-terminal portions of this enzyme contain lysine-ketog
The	C-terminal proline-rich motif in CD28 is important for
family members in that it lacks a conserved	C-terminal protein domain.
combination of 2 N-terminal LIM motifs and a	C-terminal protein kinase domain.
n gene resulting in the juxtaposition of the	C-terminal region of the RET protein with an N-terminal
This domain consists of the	C-terminal region of the DnaJ protein.
The	C-terminal region forms a hairpin-like domain that pene
rotein interactions, separates this from the	C-terminal region, which exhibits the greatest sequence
degron sequence can occur at either the N or	C-terminal region, these are called N-Degrons or C-degr
anchored to the membrane through a flexible	C-terminal region, they can be thought of as a 'balloon
and a less conserved hydrophobic/amphiphilic	C-terminal region.
eta, which possesses GAP activity within its	C-terminal region.
elicase core region and occupies 75 % of the	C-terminal region.
epending on the degree of proteolysis of the	C-terminal region.
Both the N-terminal and	C-terminal regions of this protein protrude toward the
cleotide-binding domain (NBD or NACHT) and a	C-terminal regulatory domain, found only in mammals, th
rin and CCK is associated with the last five	C-terminal residues.
protein with the N-terminal SH2 domain, the	C-terminal RhoGAP domain and the central C1 domain simi
enzyme are S-adenosyl methionine and protein	C-terminal S-farnesyl-L-cysteine, whereas its two produ
the prosaposin protein depicting the N- and	C-terminal SapA domains and the four SapB1 and four Sap
t 250 amino acids generally located in their	C-terminal section (currently the only exceptions are s
Two of these cysteines are clustered in the	C-terminal section of the subunit.
Only one short region, located in the	C-terminal section, is conserved in all these proteins.
a single cysteine residue, located in their	C-terminal section, which has been shown to be essentia
Some examples of this enzyme contain a	C-terminal sequence extension that contains a PLAT doma
ipt variants encoding proteins with distinct	C-terminal sequences have been described, but the full-
The	C-terminal SH3 domain binds to peptides conforming to a
PREP cleaves peptide bonds at the	C-terminal side of proline residues.
ps up proteins) that cleaves proteins on the	C-terminal side of lysine amino acids.
The	C-terminal subdomain consists of particles, including s
-terminal subdomain (Cys 167 to Cys 179) and	C-terminal subdomain (42 amino-acids residues).
ration and release of unfolded proteins by a	C-terminal substrate binding domain.
The	c-terminal tail domain contains a nuclear localization
ther tyrosine residues mainly located in the	C-terminal tail region of the molecule.
stabilized by three disulfide bridges and a	C-terminal tail with residues 35-39.
as the carboxyl-terminus, carboxy-terminus,	C-terminal tail, C-terminal end, or COOH-terminus) of a
llular loop, along with intracellular N- and	C-terminal tails.
In bone physiology, the	C-terminal telopeptide (or more formally, carboxy-termi
e peptides at about half the rate though the	C-terminal that compete with natriuretic peptides for h
ive chemical ligation a peptide containing a	C-terminal thioester reacts with another peptide contai
The	C-terminal translocator domain corresponds to an outer
It has a	C-terminal transmembrane alpha-helix.
mbers of this family differ in the number of	C-terminal TS motifs, and some have unique C-terminal d
The enzyme encoded by this gene contains two	C-terminal TS motifs and functions as aggrecanase to cl
ene contains two disintegrin loops and three	C-terminal TS motifs and has anti-angiogenic activity.
of Kir4.2 has demonstrated that removal of a	c-terminal tyrosine increased the K+ current more than
erminal, therefore removing the tag from the	C-terminal will require the use of other techniques.

共起表現

「C-terminal」の共起表現(1語右で並び替え) - Weblio英語共起表現検索

「C-terminal」の共起表現一覧(1語右で並び替え)