「Serine」の共起表現(1語右で並び替え)

「Serine」の共起表現一覧(1語右で並び替え)

Serine

1語右で並び替え

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se include SATase, L-serine acetyltransferase, serine acetyltransferase, and serine transacetylase.
ses a classic Ser-His-Asp catalytic triad with serine acting as the nucleophile and gly-met providin
It is acidic and contains hydroxyproline, serine, alanine and glycine amino acids predominantly
th several other metabolic processes: glycine, serine, and threonine metabolism which provides hydro
The amino acids serine and hydroxyproline
This enzyme participates in glycine, serine and threonine metabolism.
rine/threonine kinase, will then phosphorylate serine and threonine resides on the β-adrenergic rece
ne betaine aldehyde is a component of glycine, serine and threonine metabolism.
This enzyme participates in glycine, serine and threonine metabolism and aminoacyl-trna bi
This enzyme participates in glycine, serine and threonine metabolism and glyoxylate and di
This enzyme participates in glycine, serine and threonine metabolism and glycerophospholip
This enzyme participates in glycine, serine and threonine metabolism and vitamin B6 metabo
the addition of phosphate molecules on certain serine and threonine amino acids in particular cellul
an intermediate in the metabolism of glycine, serine and threonine.
nd Leder experiment, showed that UCU codes for Serine and CUC codes for Leucine.
Protein kinase C (PKC) is a family of serine- and threonine-specific protein kinases that c
ne, histidine, lysine, phenylalanine, proline, serine, and threonine belong to class-II synthetases.
participates in 4 metabolic pathways: glycine, serine and threonine metabolism, cysteine metabolism,
the bond formed in the first step between the serine and the carbonyl carbon moves to attack the hy
Protein kinase C (PKC) is a family of serine- and threonine-specific protein kinases that c
d in removal of N-acetylglucoamine groups from serine and threonine residues in the cytoplasm and nu
remove the phosphate group, restore the OH to serine and turn nitrogen from histidine back into its
cycle and metabolism of amino groups, glycine, serine and threonine metabolism, histidine metabolism
roteins that it acts on, it will phosphorylate serine and threonine residues on βARK.
ylation is inhibited: most kinases act on both serine and threonine, the tyrosine kinases act on tyr
In the image above, note that, since serine and threonine possess similar structures with
The phosphorylated serine and threonine residues act as binding sites fo
FMOC solid phase pepdide sysnthesis (SPPS) of serine- and threonine-containing peptides leads to re
osphogylcerate dehydrogenase, an enzyme in the serine biosynthetic pathway.
It is generated from homocysteine and serine by cystathionine beta synthase.
elenocysteine tRNAs are initially charged with serine by seryl-tRNA ligase, but the resulting Ser-tR
ound produced by actinomycetes, which inhibits serine, cysteine and threonine proteases.
reactions such as the reactions carried out by serine dehydratase and GDP-4-keto-6-deoxymannose-3-de
] cluster as active site (aconitase, fumarase, serine dehydratase)
This encoded protein is a calcium-dependent serine endoprotease that can efficiently cleave precu
serine esterase,
Other names in common use include serine ethanolamine phosphate synthetase, serine etha
of caspase-3 and the flipping of phosphatidyl serine followed by rapid apoptosis specifically in hu
cid amide hydrolase or FAAH is a member of the serine hydrolase family of enzymes.
ays high selectivity for MAGL over other brain serine hydrolases, including the anandamide-degrading
These treatments can dehydrate serine in the protein chain.
ingosine is synthesized from palmitoyl CoA and serine in a condensation required to yield dehydrosph
By virtue of the hydroxyl group, serine is classified as a polar amino acid.
In this reaction serine is decarboxylated and combined with palmitoyl-
he α-subunit which is a target for a number of serine kinases that phosphorylate serine 51.
gnal through a heteromeric complex of receptor serine kinases which include at least two type I (I a
gnal through a heteromeric complex of receptor serine kinases which include at least two type I ( I
Both enzymes contain serine linked phosphates in their active sites, both
Their only daughter Serine married Johan Jeremiassen and had a political
In enzymology, a serine O-acetyltransferase (EC 2.3.1.30)
ly charged phospholipids, such as phosphatidyl serine, on the cell surface.
not inhibit protein kinases that phosphorylate serine or threonine residues and can discriminate bet
es (EC 2.7.11.1) phosphorylate the OH group of serine or threonine (which have similar sidechains).
hosphate group to the sidechain oxygen atom of serine or threonine residues in proteins (protein-ser
pically the first monosaccharide that connects serine or threonine in particular forms of protein O-
e side chain of hydroxylysine, hydroxyproline, serine, or threonine.
n amino acid hydroxyl side chain (usually from serine or threonine) with the glycan.
The dipeptides are used by substituting a serine or threonine residue together with the precedi
sible for adding fucose sugars in O linkage to serine or threonine residues between the second and t
lose is also the first saccharide added to the serine or threonine in the proteoglycan type O-glycos
are extremely easy to use: simply substitute a serine or threonine residue together with the precedi
HtrA serine peptidase 2,
s as a key enzyme in the activation of granule serine peptidases in inflammatory cells, such as elas
lic enzyme that belongs to a distinct class of serine peptidases.
quence 131-151 of the 70k snRNP protein with a serine phosphorylated in position 140.
PKC theta promotes serine phosphorylation of IRS-1, thereby inhibiting t
The RS domain is subject to serine phosphorylation, which seems to control intera
Camostat (INN) is a serine protease inhibitor.
Mannose-binding protein-associated serine protease are serine proteases involved in the
Reaction of the DIFP with a serine protease
a serine protease inhibitor (7 kDa; UniProt Q7LZE4).
s complexed with (bound to) another protein, a serine protease called MASP-2 (MBL-associated serine
Brain-specific serine protease 4 (BSSP-4), also known as serine prot
Mannan-binding lectin serine protease 1 also known as mannose-associated se
Serine protease HTRA1 is an enzyme that in humans is
The gene is part of a cluster of serine protease genes on chromosome 16.
It is a member of the class of the serine protease inhibitors (serpins).
Batroxobin is a serine protease derived from the venom of Bothrops at
PRTN3 is a serine protease enzyme expressed mainly in neutrophil
Serpin A9 is a member of the serpin family of serine protease inhibitors.
The subtilisin family is the second largest serine protease family characterised to date.
A basic serine protease with biological activity against Melo
It is an enzyme (EC 3.4.21.21) of the serine protease class.
Mannan-binding lectin serine protease 2 also known as mannose-binding prote
are structurally homologous to the Kunitz-type serine protease inhibitors, including bovine pancreat
integral membrane gelatinase belonging to the serine protease family.
luoride or phenylmethylsulfonyl fluoride) is a serine protease inhibitor commonly used in the prepar
Protein C inhibitor (PCI, SERPINA5) is a serine protease inhibitor (serpin) which limits the e
The active subunit Bb is a serine protease that associates with C3b to form the
A splice variant of this gene which lacks the serine protease domain functions as an inhibitor of t
MASP-1 is a serine protease that functions as a component of the
gene is a receptor for activated protein C, a serine protease activated by and involved in the bloo
Many serpins ( serine protease inhibitors) are metastable, and under
Gabexate is a serine protease inhibitor which is used therapeutical
hydrochloride is a water soluble, irreversible serine protease inhibitor with a molecular weight of
The fI light chain is the serine protease domain containing the catalytic triad
A serine protease inhibitor domain, absent from the iso
inhibitor," as it is a cysteine rather than a serine protease inhibitor.
(or α2-antiplasmin or plasmin inhibitor) is a serine protease inhibitor (serpin) responsible for in
trecogin alfa (also known as Xigris (TM)) is a serine protease of human origin, designated protein C
Enteropeptidase is a serine protease (EC 3.4.21.9) consisting of a disulfi
e 2 or neuroendocrine convertase 2 (NEC2) is a serine protease and proprotein convertase PC2, like p
e key to understanding conformation changes in serine protease inhibitors, also known as serpins, mu
Cathepsin A ( serine protease)
with MASP-1 (Mannan-binding lectin-Associated Serine Protease), MASP-2 and MASP-3, two protease zym
The prothrombinase complex consists of the serine protease, Factor Xa, and the protein cofactor,
astase, prostate-specific antigen (PSA), 13 KD serine protease, or 24KD endopeptidase.
plement C2 or by activating another complement serine protease, MASP-2.
laprevir inhibits the hepatitis C virus NS3.4A serine protease.
Like many other coagulation factors, it is a serine protease.
opeptidase K) EC 3.4.21.64 is a broad-spectrum serine protease.
e zymogen, to thrombin (Factor IIa), an active serine protease.
The coagulation factors are generally serine proteases (enzymes).
Serine proteases act by cleaving other proteins at sp
In evolutionary history, serine proteases were originally digestive enzymes.
Serine proteases are paired with serine protease inhi
Elastases form a subfamily of serine proteases that hydrolyze many proteins in addi
e a central coordinator for activation of many serine proteases in immune/inflammatory cells.
Rhomboid family intramembrane serine proteases do not share common ancestry with th
ila species, a large group of enzymes known as serine proteases have been associated with female spe
survival in cancer and the role of coagulation serine proteases in tumour biology.
rokinase-type plasminogen activator, which are serine proteases belonging to MEROPS peptidase family
nhibitor proteins from plant seeds and various serine proteases and their inhibitors have been deter
serine proteases, including trypsin, chymotrypsin, an
Tryptases comprise a family of trypsin-like serine proteases, the peptidase family S1.
eptidase is a part of the chymotrypsin-clan of serine proteases, and is structurally similar to thes
n Madrid indicates that maslinic acid inhibits serine proteases, key enzymes necessary for the sprea
PMSF does not inhibit all serine proteases.
Subtilases are a family of subtilisin-like serine proteases.
gene encodes a member of the trypsin family of serine proteases.
inhibitor of trypsin, trypsin-like enzymes and serine proteases.
ne encodes a member of the sedolisin family of serine proteases.
p/Ser/His catalytic triad, like in the trypsin serine proteases.
the C-terminus by inflammatory and coagulation serine proteases.
It is a typical serine proteinase with trypsin-like specificity.
, E., Liu, L., Lucas, A. The Potential Role of Serine Proteinase Inhibitors for the Prevention of Pl
The product encoded by this gene is a serine proteinase inhibitor which rapidly inhibits th
Serine racemase is an enzyme which generates D-serine
Mammalian serine racemase is a pyridoxal 5'-phosphate dependent
In humans, the serine racemase protein is encoded by the SRR gene.
Conversely, serine recombinases like gamma-delta and Tn3 resolvas
PMSF binds specifically to the active site serine residue in a serine protease.
by forming a covalent bond with the particular serine residue at the active site.
This is a result of the hyperactivity of that serine residue caused by the specific environmental c
hosphorylated is the oxygen of the active-site serine residue (see diagram below).
erates the pyruvate precursor from an internal serine residue and results in the formation of two no
avage site and hydroxyl group of the conserved serine residue (S10) in resolvase.
ic triad contains an asparagine instead of the serine residue.
7 (base position 199) converts an alanine to a serine residue.
The catalytic histidine and stabilizing serine residues are colored orange.
It does not bind to any other serine residues in the protein.
Activation of the 4 catalytic serine residues within the Hin tetramer make a 2-bp d
ator of ACC, able to phosphorylate a number of serine residues on both isoforms of ACC.
phosphorylation/dephosphorylation of targeted serine residues and by allosteric transformation by c
o histidine kinases, but instead phosphorylate serine residues, and probably do not use a phospho-hi
of histidine is used to abstract a proton from serine, threonine, or cysteine to activate it as a nu
o acids that are phosphorylated in eukaryotes: serine, threonine, and tyrosine.
ed them to an assumption that an enzyme called serine transhydroxymethylase could be responsible for
eryl-transfer ribonucleic acid synthetase, and serine translase.
Serine was first obtained from silk protein, a partic
Glycerate 3-phosphate is also a precursor for serine, which, in turn, can create cysteine and glyci