戻る
「早戻しボタン」を押すと検索画面に戻ります。 [閉じる]

コーパス検索結果 (１語後でソート)

通し番号をクリックするとPubMedの該当ページを表示します
1 of substrate release from ClpXP, a bacterial ATP-dependent protease.
2 d that FtsZ is degraded by E. coli ClpXP, an ATP-dependent protease.
3 ifferent form after its first turnover as an ATP-dependent protease.
4 tity to the Escherichia coli Lon protein, an ATP-dependent protease.
5 ein degradation is a common feature found in ATP-dependent proteases.
6 emoved in an efficient and timely fashion by ATP-dependent proteases.
7 y Lon or any of the cell's known cytoplasmic ATP-dependent proteases.
8 ss some membranes and protein degradation by ATP-dependent proteases.
9 o protect normal proteins, is carried out by ATP-dependent proteases.
10 yotes for marking proteins to be degraded by ATP-dependent proteases.
11 o assign substrates to the known cytoplasmic ATP-dependent proteases.
12                     We also showed that this ATP-dependent protease activity is essential for PrkA fu
13                                   Lon1 is an ATP-dependent protease and chaperone located in the mito
14 t human ClpX and ClpP constitute a bone fide ATP-dependent protease and confirm that substrate select
15 hese changes reduce regulated proteolysis by ATP-dependent proteases and protein synthesis in a syste
16 e them resistant to enzymatic degradation by ATP-dependent proteases and recent studies have shown th
17 rain CB1541 there were mutations in clpP, an ATP-dependent protease, and two different hypothetical p
18                                          Lon ATP-dependent proteases are key components of the protei
19                       Integral components of ATP-dependent proteases are motor proteins that unfold s
20                                              ATP-dependent proteases are processive, meaning that the
21                       Self-compartmentalized ATP-dependent proteases are required for virulence of se
22                                              ATP-dependent proteases are responsible for most energy-
23                                              ATP-dependent proteases are vital to maintain cellular p
24                            As multicomponent ATP-dependent proteases are widespread in nature and sha
25  to gain insight into the mechanism by which ATP-dependent proteases attain processivity in protein d
26 -oligomer and represents one of the simplest ATP-dependent proteases because both the protease and AT
27                We propose that substrates of ATP-dependent proteases bind to specific sites on the di
28 e copies of genes encoding the ClpP and FtsH ATP-dependent proteases but lacks the Lon and HslV prote
29                 In the case of the bacterial ATP-dependent protease ClpAP, ATP hydrolysis by the ClpA
30 ptor protein ClpS, an essential regulator of ATP-dependent protease ClpAP, directly interacted with P
31                         The Escherichia coli ATP-dependent protease, ClpAP, is composed of the hexame
32 ity and proteolytic activity for the E. coli ATP-dependent protease, ClpAP, is modulated by an adapto
33 id not inhibit the activity of other E. coli ATP-dependent proteases, ClpAP or ClpYQ.
34 ontrolled at the level of proteolysis by the ATP-dependent protease ClpXP and a substrate-binding pro
35 ytic control exerted by the adaptor YjbH and ATP-dependent protease ClpXP in Bacillus subtilis.
36 centrations during unperturbed growth by the ATP-dependent protease ClpXP.
37 lis, is under the proteolytic control of the ATP-dependent protease ClpXP.
38 es the proteolytic elimination of Spx by the ATP-dependent protease ClpXP.
39 d by proteolysis, mediated by the ubiquitous ATP-dependent protease ClpXP.
40 concentration increases in cells lacking the ATP-dependent protease, ClpXP, resulting in severe effec
41 , but is instead rapidly degraded by another ATP-dependent protease, ClpXP.
42 l et al. (2015) report that proteasomes, the ATP-dependent protease complexes that execute ubiquitin-
43 including the major chaperone proteins, five ATP-dependent protease complexes, and several cold and h
44              HslVU is a new Escherichia coli ATP-dependent protease composed of two multimeric comple
45                                    ClpAP, an ATP-dependent protease consisting of ClpA, a double-ring
46                                              ATP-dependent proteases control the concentrations of hu
47                                              ATP-dependent proteases degrade denatured or misfolded p
48                       Among other functions, ATP-dependent proteases degrade misfolded proteins and r
49                                              ATP-dependent proteases degrade proteins in the cytosol
50 leavage step is rate-limiting; that multiple ATP-dependent proteases degrade the cytoplasmic fragment
51                                    ClpXP, an ATP-dependent protease, degrades hundreds of different i
52                                              ATP-dependent proteases engage, translocate, and unfold
53               We have isolated a new type of ATP-dependent protease from Escherichia coli.
54                                        These ATP-dependent proteases function as homohexamers, in whi
55  is the only membrane-anchored and essential ATP-dependent protease in Escherichia coli.
56 erved in prokaryotes, and the only essential ATP-dependent protease in Escherichia coli.
57                  The proteasome is the major ATP-dependent protease in eukaryotic cells, but limited
58  that demonstrates a direct role for the Lon ATP-dependent protease in the degradation of tmRNA-tagge
59       In this study, we identified LONP1, an ATP-dependent protease in the matrix, as a top Abeta42 i
60 verlapping that of the Lon protease, another ATP-dependent protease in which a single subunit contain
61                                  ClpXP is an ATP-dependent protease in which the ClpX AAA+ motor bind
62                         There are five known ATP-dependent proteases in Escherichia coli (Lon, ClpAP,
63 e removal of damaged or unneeded proteins by ATP-dependent proteases is crucial for cell survival in
64              Lon protease but no other known ATP-dependent proteases is required for persistence.
65 e show that PhoADelta2-22 is degraded by two ATP-dependent proteases, La (Lon) and ClpAP, and breakdo
66                                    Yme1p, an ATP-dependent protease localized in the mitochondrial in
67                                          The ATP-dependent protease Lon (La) of Escherichia coli degr
68 ium smegmatis gene encoding a homolog of the ATP-dependent protease Lon (La).
69                                          The ATP-dependent protease Lon was also found to negatively
70 itoxins are proteolytically regulated by the ATP-dependent proteases Lon and ClpP.
71 We found that Xis is degraded in vivo by two ATP-dependent proteases, Lon and FtsH (HflB).
72                           In this study, the ATP-dependent proteases LonA and B and the regulatory AT
73                                              ATP-dependent proteases maintain protein quality control
74                            The ClpYQ (HslUV) ATP-dependent protease of Escherichia coli consists of a
75                                Compartmented ATP-dependent proteases of diverse origin share conserve
76        The 26S proteasome is a multi-subunit ATP-dependent protease responsible for degrading most sh
77        Lon protein of Escherichia coli is an ATP-dependent protease responsible for the rapid turnove
78 ls of lysosomal proteolysis or the action of ATP-dependent proteases such as bacterial lon.
79 ting the activity of mitochondrial LONP1, an ATP-dependent protease that controls the selective turno
80                                    Lon is an ATP-dependent protease that degrades unstructured protei
81                                  ClpXP is an ATP-dependent protease that denatures native proteins an
82      ClpP is the proteolytic component of an ATP-dependent protease that is essential for the proper
83  The 26S proteasome is a 2.5-MDa, 32-subunit ATP-dependent protease that is responsible for the degra
84        The mitochondrial protein LonP1 is an ATP-dependent protease that mitigates cell stress and ca
85     Proteasomes are essential and ubiquitous ATP-dependent proteases that function in eukarya, archae
86 hat mycobacterial species contain additional ATP-dependent proteases that have broad substrate specif
87                                    Among the ATP-dependent proteases, those of the Clp family are par
88 ities of representatives from all classes of ATP-dependent proteases to unfold a model substrate prot
89 se of the outer membrane) induced YME1L1, an ATP-dependent protease, to eliminate translocase of the
90                                              ATP-dependent proteases translocate and unfold their sub
91                                              ATP-dependent proteases translocate proteins through a n
92 AAA family of proteins, is the only membrane ATP-dependent protease universally conserved in prokaryo
93                           Other well-studied ATP-dependent proteases use ATP to unfold their substrat
94  also known as protease La, is an oligomeric ATP-dependent protease, which functions to degrade damag
95 ng the proteolysis of functional proteins by ATP-dependent proteases while in the slow-growth state o