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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                                   Lon1 is an ATP-dependent protease and chaperone located in the mito
12 t human ClpX and ClpP constitute a bone fide ATP-dependent protease and confirm that substrate select
13 rain CB1541 there were mutations in clpP, an ATP-dependent protease, and two different hypothetical p
14                                          Lon ATP-dependent proteases are key components of the protei
15                       Integral components of ATP-dependent proteases are motor proteins that unfold s
16                                              ATP-dependent proteases are processive, meaning that the
17                       Self-compartmentalized ATP-dependent proteases are required for virulence of se
18                                              ATP-dependent proteases are responsible for most energy-
19                                              ATP-dependent proteases are vital to maintain cellular p
20                            As multicomponent ATP-dependent proteases are widespread in nature and sha
21  to gain insight into the mechanism by which ATP-dependent proteases attain processivity in protein d
22 -oligomer and represents one of the simplest ATP-dependent proteases because both the protease and AT
23                We propose that substrates of ATP-dependent proteases bind to specific sites on the di
24 e copies of genes encoding the ClpP and FtsH ATP-dependent proteases but lacks the Lon and HslV prote
25                 In the case of the bacterial ATP-dependent protease ClpAP, ATP hydrolysis by the ClpA
26 ptor protein ClpS, an essential regulator of ATP-dependent protease ClpAP, directly interacted with P
27                         The Escherichia coli ATP-dependent protease, ClpAP, is composed of the hexame
28 ity and proteolytic activity for the E. coli ATP-dependent protease, ClpAP, is modulated by an adapto
29 id not inhibit the activity of other E. coli ATP-dependent proteases, ClpAP or ClpYQ.
30 ontrolled at the level of proteolysis by the ATP-dependent protease ClpXP and a substrate-binding pro
31 ytic control exerted by the adaptor YjbH and ATP-dependent protease ClpXP in Bacillus subtilis.
32 centrations during unperturbed growth by the ATP-dependent protease ClpXP.
33 lis, is under the proteolytic control of the ATP-dependent protease ClpXP.
34 es the proteolytic elimination of Spx by the ATP-dependent protease ClpXP.
35 d by proteolysis, mediated by the ubiquitous ATP-dependent protease ClpXP.
36 concentration increases in cells lacking the ATP-dependent protease, ClpXP, resulting in severe effec
37 , but is instead rapidly degraded by another ATP-dependent protease, ClpXP.
38 l et al. (2015) report that proteasomes, the ATP-dependent protease complexes that execute ubiquitin-
39 including the major chaperone proteins, five ATP-dependent protease complexes, and several cold and h
40              HslVU is a new Escherichia coli ATP-dependent protease composed of two multimeric comple
41                                              ATP-dependent proteases control the concentrations of hu
42                                              ATP-dependent proteases degrade denatured or misfolded p
43                       Among other functions, ATP-dependent proteases degrade misfolded proteins and r
44                                              ATP-dependent proteases degrade proteins in the cytosol
45 leavage step is rate-limiting; that multiple ATP-dependent proteases degrade the cytoplasmic fragment
46                                    ClpXP, an ATP-dependent protease, degrades hundreds of different i
47                                              ATP-dependent proteases engage, translocate, and unfold
48               We have isolated a new type of ATP-dependent protease from Escherichia coli.
49  is the only membrane-anchored and essential ATP-dependent protease in Escherichia coli.
50 erved in prokaryotes, and the only essential ATP-dependent protease in Escherichia coli.
51                  The proteasome is the major ATP-dependent protease in eukaryotic cells, but limited
52  that demonstrates a direct role for the Lon ATP-dependent protease in the degradation of tmRNA-tagge
53 verlapping that of the Lon protease, another ATP-dependent protease in which a single subunit contain
54                         There are five known ATP-dependent proteases in Escherichia coli (Lon, ClpAP,
55 e removal of damaged or unneeded proteins by ATP-dependent proteases is crucial for cell survival in
56              Lon protease but no other known ATP-dependent proteases is required for persistence.
57 e show that PhoADelta2-22 is degraded by two ATP-dependent proteases, La (Lon) and ClpAP, and breakdo
58                                    Yme1p, an ATP-dependent protease localized in the mitochondrial in
59                                          The ATP-dependent protease Lon (La) of Escherichia coli degr
60 ium smegmatis gene encoding a homolog of the ATP-dependent protease Lon (La).
61                                          The ATP-dependent protease Lon was also found to negatively
62 itoxins are proteolytically regulated by the ATP-dependent proteases Lon and ClpP.
63 We found that Xis is degraded in vivo by two ATP-dependent proteases, Lon and FtsH (HflB).
64                           In this study, the ATP-dependent proteases LonA and B and the regulatory AT
65                                              ATP-dependent proteases maintain protein quality control
66                            The ClpYQ (HslUV) ATP-dependent protease of Escherichia coli consists of a
67                                Compartmented ATP-dependent proteases of diverse origin share conserve
68        The 26S proteasome is a multi-subunit ATP-dependent protease responsible for degrading most sh
69        Lon protein of Escherichia coli is an ATP-dependent protease responsible for the rapid turnove
70 ls of lysosomal proteolysis or the action of ATP-dependent proteases such as bacterial lon.
71 ting the activity of mitochondrial LONP1, an ATP-dependent protease that controls the selective turno
72                                    Lon is an ATP-dependent protease that degrades unstructured protei
73                                  ClpXP is an ATP-dependent protease that denatures native proteins an
74      ClpP is the proteolytic component of an ATP-dependent protease that is essential for the proper
75  The 26S proteasome is a 2.5-MDa, 32-subunit ATP-dependent protease that is responsible for the degra
76     Proteasomes are essential and ubiquitous ATP-dependent proteases that function in eukarya, archae
77 hat mycobacterial species contain additional ATP-dependent proteases that have broad substrate specif
78                                    Among the ATP-dependent proteases, those of the Clp family are par
79 ities of representatives from all classes of ATP-dependent proteases to unfold a model substrate prot
80                                              ATP-dependent proteases translocate and unfold their sub
81                                              ATP-dependent proteases translocate proteins through a n
82 AAA family of proteins, is the only membrane ATP-dependent protease universally conserved in prokaryo
83                           Other well-studied ATP-dependent proteases use ATP to unfold their substrat
84  also known as protease La, is an oligomeric ATP-dependent protease, which functions to degrade damag

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