「Cysteine」の共起表現(1語右で並び替え)

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共起表現

「Cysteine」の共起表現一覧(1語右で並び替え)

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A	cysteine adduct is formed with the methylene group and
Disulfide bridges in proteins are reduced and	cysteine amino acids are carboxymethylated chemically
0-35 amino acids and 4 disulfide bonds; eight	cysteine amino acids among its total number of amino a
uced by actinomycetes, which inhibits serine,	cysteine and threonine proteases.
It is an intermediate in the synthesis of	cysteine and adenosine.
It is cleaved into	cysteine and α-ketobutyrate by cystathionine gamma-lya
cursor for serine, which, in turn, can create	cysteine and glycine through the homocysteine cycle.
olic pathway involving the interconversion of	cysteine and homocysteine, through the intermediate cy
dium carbonate and was first synthesized from	cysteine and β-chloroalanine.
The N-terminal	cysteine as well as the internal cysteines are able to
(chemical reactivity) of side chains such as	cysteine, backbone exposure to proteases, and various
ionine is considered an essential amino acid,	cysteine becomes an essential amino acid when the tran
Is activated by	cysteine, bisulfite salt, NaCN, H2S, Na2S and benzoate
rdination bond to an evolutionarily-conserved	cysteine bound to the iron center of heme B.
Other names in common use include farnesyl	cysteine C-terminal methyltransferase, farnesyl-protei
Likewise,	cysteine can be made from homocysteine but cannot be s
The	cysteine can be introduced using site-directed mutagen
	Cysteine cathepsins are synthesized as inactive zymoge
Other names in common use include	cysteine conjugate aminotransferase, and cysteine-conj
Other names in common use include	cysteine conjugate beta-lyase, glutamine transaminase
RI has a surprisingly high	cysteine content (~6.5%, cf.
s aided in protein samples by the presence of	cysteine, cystine, tyrosine, and tryptophan side chain
	Cysteine deposition is most evident in the conjunctiva
In enzymology, a	cysteine desulfurase (EC 2.8.1.7)
ommon use include IscS, NIFS, NifS, SufS, and	cysteine desulfurylase.
ino transferases, and other enzymes including	cysteine desulphurase EC:4.4.1.-.
	Cysteine desulphurase related IPR011340
	Cysteine desulphurase IPR010240
	Cysteine desulphurase related, unknown function IPR010
	Cysteine desulphurases, SufS IPR010970
It is formed by	cysteine dioxygenase.
Homocysteine permanently degrades	cysteine disulfide bridges and lysine amino acid resid
ds after the reduction of cystine residues to	cysteine during protein sequencing.
It is of a family of proteases known as the	cysteine endopeptidases, a group that also includes pa
ssulfuration pathway is critical for creating	cysteine from the essential amino acid methionine.
hate,geranylgeranyl-diphosphate:protein-, and	cysteine geranyltransferase.
The synthetases specific for arginine,	cysteine, glutamic acid, glutamine, isoleucine, leucin
be converted back into methionine, SAM-e, or	cysteine, glutathione, and other useful substances.
The key characteristic is the	cysteine group which is required for phosphorylation;
een oxidized to an alpha-keto-acid (i.e., the	cysteine has been replaced by a pyruvate).
In organisms that synthesize	cysteine in sulfur assimilation such as bacteria and y
trienes due to the presence of the amino acid	cysteine in their structure.
, by a thiolate anion derived from a reactive	cysteine in a reduced partner.
PKS) and the thiazole ring was derived from a	cysteine incorporated by a nonribosomal peptide synthe
where 'C' denotes a conserved	cysteine involved in a disulfide bond.
	Cysteine is an important source of sulfide in human me
The side chain on	cysteine is thiol, which is nonpolar and thus cysteine
is reaction is ideal for situations where the	cysteine is located away from the desired epitope (e.g
The nucleophilicity of the	cysteine is facilitated by an oxyanion hole formed wit
tif suggestive of a leucine zipper in which 1	cysteine is found instead of all leucines.
	Cysteine is named after cystine.
The amino acid	cysteine is produced industrially from substituted thi
ch is encoded by CG13419 gene and made of two	cysteine knot subunits, Burs-α and Burs-β.
elongs to the structural family of ‘inhibitor	cysteine knot' spider peptides.
Glutamate	cysteine ligase is a heterodimeric enzyme composed of
Glutamate	cysteine ligase modifier subunit (GCLM, ~31 kDa) incre
Glutamate	cysteine ligase catalytic subunit (GCLC, ~73 kDa) poss
ylcysteine synthetase (EC 6.3.2.2) (glutamate	cysteine ligase, GCL) is the first enzyme in the gluta
This enzyme participates in	cysteine metabolism and sulfur metabolism.
This enzyme participates in	cysteine metabolism and aminoacyl-trna biosynthesis.
This enzyme participates in	cysteine metabolism and glutathione metabolism.
enzyme participates in 3 metabolic pathways:	cysteine metabolism, selenoamino acid metabolism, and
5 metabolic pathways: methionine metabolism,	cysteine metabolism, selenoamino acid metabolism, nitr
4 metabolic pathways: methionine metabolism,	cysteine metabolism, selenoamino acid metabolism, and
ys: glycine, serine and threonine metabolism,	cysteine metabolism, D-glutamine and D-glutamate metab
	Cysteine metabolism.
This enzyme participates in	cysteine metabolism.
yme participates in methionine metabolism and	cysteine metabolism.
Cysteic acid is an intermediate in	cysteine metabolism.
fide bridges (cystines - formed from pairs of	cysteine molecules) are formed.
ein sequence and distinguished by a conserved	cysteine motif.
succinyl-L-homoserine succinate-lyase (adding	cysteine), O-succinylhomoserine (thiol)-lyase, homoser
ovalent attachment of E-64 to the active site	cysteine occurs via nucleophillic attack from the thio
When	cysteine or methionine is available in the environment
Not to be confused with cytosine,	cysteine, or cystine.
The most common reaction with amino acids is	cysteine oxidation.
another thiolate from the reagent, leaves the	cysteine oxidised.
Mechanism of irreversible inhibition of	cysteine peptidases with iodoacetate.
Mechanism of irreversible inhibition of	cysteine peptidases with iodoacetamide.
Mechanism of irreversible inhibition of	cysteine peptidases by E-64.
, and has since been shown to inhibit many	cysteine peptidases (e.g.
This group of	cysteine peptidases belong to MEROPS peptidase family
doacetate is an irreversible inhibitor of all	cysteine peptidases, with the mechanism of inhibition
acetamide is an irreversible inhibitor of all	cysteine peptidases, with the mechanism of inhibition
hich can irreversibly inhibit a wide range of	cysteine peptidases.
Cathepsin O is a	cysteine protease and a member of the cathepsin family
Endoprotease B, isoform 2 (EP-B2) is a	cysteine protease found in barley.
The TEV protease is a highly site-specific	cysteine protease that is found in the Tobacco Etch Vi
e protein encoded by this gene is a lysosomal	cysteine protease involved in bone remodeling and reso
Autophagin-1 (Atg4/Apg4) is a unique	cysteine protease responsible for the cleavage of the
Caspase 13 is an enzyme known as a	cysteine protease that was identified in cattle that i
lant is a hypothesised protein, most likely a	cysteine protease enzyme (EC 3.4.22.26), that occurs o
o recruit caspase-8, and thereby activate the	cysteine protease cascade.
e is an endogenous calpain (calcium-dependent	cysteine protease) inhibitor.
Cathepsin C (	cysteine protease)
	Cysteine proteases have a common catalytic mechanism t
Also inhibits some	cysteine proteases such as papain, bromelain or ficin.
In humans, the group of cathepsin	cysteine proteases or cysteine cathepsins comprises 11
proregion is unique within the papain family	cysteine proteases in that it contains this additional
It belongs to a family of	cysteine proteases called caspases that cleave protein
are dependent on thiol reactivity, including	cysteine proteases such as papain and acetylcholineste
rtic acid residue, and belongs to a family of	cysteine proteases called caspases.
rugs to treat diseases where high levels of a	cysteine proteases are the primary cause.
athepsin L, and cathepsin V, all of which are	cysteine proteases.
e protein encoded by this gene is a lysosomal	cysteine proteinase that plays a major role in intrace
ne, a member of the peptidase C1 family, is a	cysteine proteinase that may have a specific function
Cathepsin F (	cysteine proteinase)
Cathepsins are papain family	cysteine proteinases that represent a major component
Plant	cysteine proteinases isolated from these plants have b
tic peptides typically used as substrates for	cysteine proteinases and its proteolytic activity was
termed a "cross-class inhibitor," as it is a	cysteine rather than a serine protease inhibitor.
ear export sequence (NES), by glycosylating a	cysteine residue (cysteine 529 in S. pombe).
m DNA bases and sugar-phosphate backbone to a	cysteine residue inactivating itself.
at inhibits MurA by alkylating an active site	cysteine residue (Cys 115 in the Escherichia coli enzy
It is composed of a	cysteine residue with an acetylated amino group linked
and consists of a glutamic acid residue and a	cysteine residue that interact with opposite sides of
ram of human IPP isomerase with the catalytic	cysteine residue (Cys87) in red and the catalytic glut
ide exchange reactions; a thiolate group of a	cysteine residue attacks one of the protein's own disu
The	cysteine residue at 302 in ALDH1 and 200 in ALDH2 is i
minal fragment 1) and the other an N-terminal	cysteine residue (C-terminal fragment 2).
in that AGT II transfers the alkyl group to a	cysteine residue in its own structure, thereby inactiv
transfer on the RNR2 subunit activates a RNR1	cysteine residue in the active site with a free radica
from geranylgeranyl diphosphate to one or two	cysteine residue(s) at the C-terminus of specific prot
aleimide or DTNB irreversibly blocks critical	cysteine residue(s), abolishing the ability of the enz
MTSL is attached via a disulfide bond to a	cysteine residue, enabling site-directed spin labellin
All these proteins contain a single	cysteine residue, located in their C-terminal section,
with another peptide containing an N-terminal	cysteine residue, in the presence of an added thiol ca
cin, which covalently modifies an active site	cysteine residue.
TCEP is particularly useful when labeling	cysteine residues with maleimides.
For example,	cysteine residues in the peptide may be temporarily bl
The mature protein contains 8	cysteine residues that establish 4 disulfide bridges (
in a common post-translational modification,	cysteine residues are converted into thiazolines.
The primary structure contains 28	cysteine residues forming multiple disulfide bonds.
This sequence contains 6	cysteine residues that form three intramolecular disul
The two amino acid	cysteine residues in contryphans are linked by a disul
inked glycan allows the cell to control which	cysteine residues will form disulfide bonds.
form of disulfide bridges formed between two	cysteine residues or the formation of metal clusters.
to the conversion of thiol groups, including	cysteine residues in proteins, to form S-nitrosothiols
vitro, but does not hydrolyze palmitate from	cysteine residues in proteins.
no acid residues that contains four conserved	cysteine residues involved in two disulphide bonds:.
y acyl groups such as palmitate from modified	cysteine residues in proteins or peptides during lysos
shown in red, the alpha carbons of the eight	cysteine residues in green, and the disulfide bridges
a total of two geranylgeranyl groups onto two	cysteine residues at the C-terminal consensus sequence
lmitoyl groups may be added to the Sγ atom of	cysteine residues to anchor proteins to cellular membr
rved between these two forms is the number of	cysteine residues exposed at the surface of the enzyme
-G-V/L 'pediocin box' motif and two conserved	cysteine residues joined by a disulfide bridge.
nd a large extracellular loop, which has many	cysteine residues with conserved spacing.
s, are largely acidic, contain four conserved	cysteine residues known to form two disulfide bonds, m
It has two	cysteine residues on the N-terminal segment, a hydroph
ther scorpion toxins; this unusual pairing of	cysteine residues may be mediated by the presence of a
N-terminal section; this region includes two	cysteine residues involved in a disulfide bond.
known as 6Ckine (because it has six conserved	cysteine residues instead of the four cysteines typica
aryotic organisms examined, and contain seven	cysteine residues that are absolutely conserved, inclu
It reacts with	cysteine residues in proteins.
cid side chain (e.g., iodoacetamide to modify	cysteine residues), an isotopically coded linker, and
It contains 4 conserved	cysteine residues, which probably form disulphide brid
domain is characterised by a conserved set of	cysteine residues, which form four disulfide bonds to
protein contains two free thiol groups at the	cysteine residues, whereas the oxidized form contains
groups from the damaged DNA to one of its two	cysteine residues, rendering the protein enzymatically
nked fatty acyl groups such as palmitate from	cysteine residues.
coordinated by two histidine residues and two	cysteine residues.
of the protein backbone and the side chain of	cysteine residues.
close to the ‘long chain' family but with six	cysteine residues.
130 and contain the WSXWS motif and preserved	cysteine residues.
e a mature protein containing seven conserved	cysteine residues.
uster in which two zinc ions are bound by six	cysteine residues.
hioether bonds involving sulphydryl groups of	cysteine residues.
common active site sequence with two reactive	cysteine residues: Cys-X-Y-Cys, where X and Y are ofte
o 70-residue range and known to contain eight	cysteine residues; and the ‘short chain neurotoxins' (
domains: a FIMAC domain, a Scavenger Receptor	Cysteine Rich (SRCR) domain and two LDL-receptor Class
ily(metalloproteinase-like, Disintegrin-like,	cysteine rich).
arine cone snails and belong to the four-loop	cysteine scaffold structural class.
ional groups can be added to selectively bind	cysteine side chains and this method is often used to
J homolog subfamily C member 5, also known as	cysteine string protein or CSP is a protein, that in h
arbon diketide is delivered by the ACP to the	cysteine sulfhydryl group at the KS active site, by th
	Cysteine sulfinic acid is an intermediate in cysteine
Other names in common use include alliinase,	cysteine sulfoxide lyase, alkylcysteine sulfoxide lyas
me of this enzyme class is L-cysteine:[enzyme	cysteine] sulfurtransferase.
In enzymology, a	cysteine synthase (EC 2.5.1.47)
and some species have alternative pathways of	cysteine synthesis.
ydrogen-sulfide), acetylserine sulfhydrylase,	cysteine synthetase, S-sulfocysteine synthase, 3-O-ace
However, when administering labeled	cysteine, they found that C-4' did not contain any 13C
disulfide exchange reactions that oxidise the	cysteine thiol groups of nascent polypeptides.
new carboxy-terminus of the substrate to the	cysteine thiol is formed.
xidized state, molybdenum is coordinated by a	cysteine thiolate, the dithiolene group of molybdopter
EA5 patients have a	cysteine to phenylalanine mutation at position 104.
e β-lactone, and hetero-conjugate addition of	cysteine to dehydroalanine.
abstract a proton from serine, threonine, or	cysteine to activate it as a nucleophile.
ible for the observation by conversion of the	cysteine to serine residue.
steinyl-transfer ribonucleate synthetase, and	cysteine translase.
on, which is then converted to the amino acid	cysteine via the transsulfuration pathway.
clusters and in nitrogenase is extracted from	cysteine, which is converted to alanine in the process
ally rich in the sulfur-containing amino acid	cysteine, which facilitates chemical cross-linking of
the outer membrane by its hydrophobic head (a	cysteine with lipids attached).
Carbocisteine is produced by alkylation of	cysteine with chloroacetic acid.

共起表現

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「Cysteine」の共起表現一覧(1語右で並び替え)