「Proteases」の共起表現(1語右で並び替え)

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共起表現

「Proteases」の共起表現一覧(1語右で並び替え)

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However, there are milk-clotting	proteases able to cleave other peptide bonds in the κ-
Serine	proteases act by cleaving other proteins at specific s
TF, FVII is activated to FVIIa by different	proteases, among which are thrombin (factor IIa), fact
nterview, Rasnick stated that he had studied	proteases and their inhibitors for twenty years.
lso known as seprase, belongs to the clan SC	proteases and is a member of the S9B prolyl oligopepti
The enzyme belongs to the family of aspartic	proteases and is responsible for the conversion of ina
hains such as cysteine, backbone exposure to	proteases, and various hydrodynamic measurements.
in of P. lilacinus has been shown to produce	proteases and a chitinase, enzymes that could weaken a
proteins from plant seeds and various serine	proteases and their inhibitors have been determined by
They act as both	proteases and transpeptidases.
is a part of the chymotrypsin-clan of serine	proteases, and is structurally similar to these protei
loses its activity in alcohol, acetone, some	proteases and trichloroacetate, renaturates after addi
Once activated by cathepsin C, the	proteases are capable of degrading various extracellul
r to an area where digestive enzymes such as	proteases are prevalent in the liquid.
ADAMTS	proteases are complex secreted enzymes containing a pr
eat diseases where high levels of a cysteine	proteases are the primary cause.
Retroviral aspartyl	proteases are single domain aspartyl proteases from re
Retroviral	proteases are homologous to a single domain of the two
However specific	proteases are used for cleaving of proteins for regula
Serine	proteases are paired with serine protease inhibitors,
type plasminogen activator, which are serine	proteases belonging to MEROPS peptidase family S1A.
It is hypothesized that these	proteases break down various proteins in male seminal
It belongs to a family of cysteine	proteases called caspases that cleave proteins only at
residue, and belongs to a family of cysteine	proteases called caspases.
	Proteases capable of degrading aggrecans are called ag
, MENT is also an effective inhibitor of the	proteases cathepsin K, cathepsin L, and cathepsin V, a
titute a family of enzymes from the group of	proteases, classified by the nature of the most promin
	Proteases, dependent on their time of action and conce
Lysosomal	proteases digest endocytosed proteins
acaspases are, indicating that this group of	proteases diverged from caspases from a common metacas
Rhomboid family intramembrane serine	proteases do not share common ancestry with the other
ligand in protein crystallography to prevent	proteases from degrading a protein of interest; the tr
Cysteine	proteases have a common catalytic mechanism that invol
allikreins, several cascades involving these	proteases have been implicated in the regulation of ho
es, a large group of enzymes known as serine	proteases have been associated with female sperm stora
al coordinator for activation of many serine	proteases in immune/inflammatory cells.
is unique within the papain family cysteine	proteases in that it contains this additional N-termin
in cancer and the role of coagulation serine	proteases in tumour biology.
Known functions of the ADAMTS	proteases include processing of procollagens and von W
serine	proteases, including trypsin, chymotrypsin, and subtil
rotein-associated serine protease are serine	proteases involved in the complement system.
The ammonia and	proteases it produces, including several collagenases,
indicates that maslinic acid inhibits serine	proteases, key enzymes necessary for the spread of HIV
It is of a family of	proteases known as the cysteine endopeptidases, a grou
It inhibits	proteases like chymotrypsin, kallikrein, plasmin, thro
When cells are lysed for these studies,	proteases, many of which are contained within lysosome
Opiorphin inhibits two	proteases: neutral ecto-endopeptidase (MME) and ecto-a
He concentrates on secreted aspartic	proteases of Candida albicans as virulence factors and
In humans, the group of cathepsin cysteine	proteases or cysteine cathepsins comprises 11 family m
ergo caspases induced apoptosis, while other	proteases participate in the degradation and removal o
ng of the amyloid precursor protein (APP) by	proteases referred to as the β and γ secretases.
dent on thiol reactivity, including cysteine	proteases such as papain and acetylcholinesterase.
etes, which act specifically to inhibit acid	proteases such as pepsin and renin.
ibits the activity of certain enzymes called	proteases, such as cathepsin G that is found in neutro
Also inhibits some cysteine	proteases such as papain, bromelain or ficin.
serpin polymers are unable to inhibit target	proteases, suggesting that the RCL is unavailable and
dogenous pro-HGF for the catalytic domain of	proteases that cleave HGF precursors.
Elastases form a subfamily of serine	proteases that hydrolyze many proteins in addition to
There are also several milk-clotting	proteases that, being able to cleave the Phe105-Met106
l formed depend on the type of action of the	proteases, the type of milk, and the patterns of casei
ses comprise a family of trypsin-like serine	proteases, the peptidase family S1.
anted proteolysis by denaturing their target	proteases through non-competitive inhibition at an all
bilized toxin proteins are cleaved by midgut	proteases to smaller toxic polypeptides that attack th
Preproinsulin is a precursor processed by	proteases to proinsulin by removal of the signal pepti
In evolutionary history, serine	proteases were originally digestive enzymes.
Recently, several caspase-like	proteases were isolated from A.nidulans samples under
lternatively, the N-terminal pro-sequence of	proteases which must be cleaved prior to activation ca
t was later found to inhibit nearly all acid	proteases with high potency and, as such, has become a

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