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1 a preprotein with a 50-amino acid N-terminal presequence.
2 its native form by removal of the N-terminal presequence.
3  and it recognizes a mitochondrial targeting presequence.
4 s of mature QPs3 and a 55-amino acid residue presequence.
5 ed to a size consistent with cleavage of the presequence.
6  includes a putative chloroplastic targeting presequence.
7 ibiting a step other than proteolysis of the presequence.
8  matrix, based on an N-terminal, amphipathic presequence.
9 and function of the 20-amino acid N-terminal presequence.
10 l step in import, i.e., translocation of the presequence.
11 rane by a bipartite, cleaved, amino-terminal presequence.
12 ytoplasm without a conventional mt-targeting presequence.
13 uits other motor subunits and binds incoming presequence.
14 ed M(r) of 52,000 containing a 31-amino acid presequence.
15 ssessing independent mitochondrial targeting presequences.
16  residues and contain 9-amino-acid cleavable presequences.
17  inner membrane Tim17/23 translocon by their presequences.
18 ns targeted by positively charged N-terminal presequences.
19 (1) protein has been shown to lack a cleaved presequence; a single methionine is removed from the ami
20 teins carry a positively charged, N-terminal presequence and are imported by the TIM23 complex (prese
21 c, allowing recognition of both the incoming presequence and other translocase components at the tran
22 ows that MPP recognizes a second site in the presequence and processing occurs between residues 43 an
23 is not imported using a conventional cleaved presequence and show that sequences at the N-terminus of
24 efore MIP cleaves off the second part of the presequence and that this second processing step takes p
25 oteins of the intermembrane space (IMS) lack presequences and are imported in an oxidation-driven rea
26 e two major IMS-targeting signals, bipartite presequences and cysteine motifs.
27 d us to propose that the length of targeting presequences and the subunit composition of organellar p
28 s are targeted to mitochondria by N-terminal presequences and use the TIM23 complex for their translo
29 independent of proteolytic processing of the presequence, and that o-phenanthroline together with EDT
30 tructure unveils how mitochondrial targeting presequences are recognized.
31                                        These presequences are rich in positive charges, mainly argini
32  reveals the highly conserved nature of such presequences, as well as of the import machinery.
33                                The cleavable presequence at the amino terminus of the precursor form
34 the Deltapsi is not linked to the respective presequence, but rather to the mature portion of the pol
35 ired in TOM-TIM23 coupling and the import of presequence-carrying preproteins.
36  can assume a conformation incompatible with presequence cleavage.
37 al peptide are important for Som1p-dependent presequence cleavage; however, no specific cargo sequenc
38 ing plasmids lacking either the IDH1 or IDH2 presequence coding regions were unexpectedly found to be
39 ecursors have functionally similar bipartite presequences composed of an N-terminal signal peptide do
40 ing experiments indicate that the N-terminal presequence-containing domain of the substrate proteins
41               Here, we report that import of presequence-containing precursors and carrier proteins i
42 0 along with Tim23 regulate translocation of presequence-containing proteins across the mitochondrial
43                         As shown herein, the presequence contains significant secondary structure and
44 ransit peptides, and processing of the LAP-N presequence could generate the mature 55-kD LAP-N.
45           Only 24% of carriers met EHR-based presequencing criteria for probable or definite FH diagn
46 sparagine-linked glycosylation reporters and presequence deletion constructs of the precursor to the
47 , while shorter hydrogenosomal and mitosomal presequences did not.
48 al target presequence of 64 residues and the presequence directed the green fluorescent protein to to
49                                The bipartite presequences directing the products of these genes back
50                                          The presequence dramatically altered SCP-2 structure as dete
51 x) sorts precursor proteins with a cleavable presequence either into the matrix or into the inner mem
52                          We propose that the presequence either targets Atp6p to the Atp9p or signals
53    The 16-amino acid mitochondrial targeting presequence, encoded by the second and third exons, was
54 h subunit was found to be dependent upon its presequence for mitochondrial localization, and the subu
55 gulator2 homolog (SRT2) contains a predicted presequence for mitochondrial targeting.
56 her CCS nor SOD1 contains typical N-terminal presequences for mitochondrial uptake; however, the mito
57 ity of mitochondrial proteins use N-terminal presequences for targeting to mitochondria and are trans
58 id N-terminal presequence that is similar to presequences found on all examined hydrogenosomal protei
59 dria, even after fusion of the mitochondrial presequence from pmAAT to its N-terminal end.
60 -directed mutagenesis was used to remove the presequences from each gene and from both genes carried
61 st three peptidases are involved in cleaving presequences from imported mitochondrial proteins.
62 was shown by expressing the LipDH N-terminal presequences fused to green fluorescent protein in eryth
63 ssed a natural substrate, pre-23K, and a 23K presequence-green fluorescent protein (GFP) chimera in v
64                                    The LAP-A presequence had features similar to chloroplast transit
65                                     The 5-kD presequence had features similar to plastid transit pept
66 ex we used iron-sulfur proteins in which the presequences had been changed by site-directed mutagenes
67 nosomal AAC contains a cleavable, N-terminal presequence; however, this sequence is not necessary for
68 ta indicate the importance of the N-terminal presequence in regulating SCP-2 structure, cholesterol l
69 his study has examined the role of the Atp6p presequence in the function and assembly of the ATPase c
70 PP), is capable of cleaving a hydrogenosomal presequence in vitro, in contrast to MPP which requires
71  of Sf9 cells and required the mitochondrial presequences in both subunits.
72 ial proteins are synthesized with N-terminal presequences in the cytosol.
73 sized as preproteins carrying amino-terminal presequences in the cytosol.
74 studies of Pex5p(C) binding], the N-terminal presequence increased SCP-2's affinity for Pex5p(C) by 1
75                      Inspection of the LAP-A presequence indicated the presence of a dibasic protease
76                         Translocation of the presequence is an early event in import of preproteins a
77 rt competence can be retained as long as the presequence is capable of forming a relatively more stab
78                If proline-20 of the S. pombe presequence is changed into a serine, a second cleavage
79 onversely, if serine-24 of the S. cerevisiae presequence is changed to a proline, the first cleavage
80                                  The mutated presequence is cleaved and forms mature-sized protein in
81 uggesting that the N-terminal portion of the presequence is essential for membrane binding.
82 surface is dramatically accelerated when its presequence is long enough to span both membranes and to
83 cates that the precursor of Tic22 (preTic22) presequence is necessary and sufficient for targeting to
84 ges in the N-terminal helical segment of the presequence is necessary for import competence.
85 sults indicate that removal of the subunit 6 presequence is not an essential event for ATPase biogene
86 ate of DeltapH-driven translocation, and the presequence is optimized in its natural acidic residue c
87 icate that a single amino acid change in the presequence is responsible for one-step processing in S.
88                                       If the presequence is too short, import is slow but can be stro
89 rotein and the COOH-terminal residues of its presequence is used as a substrate.
90 d us to postulate that the N-terminus of the presequence is vital for import and the C-terminal end i
91           Specifically, longer mitochondrial presequences may have evolved to require an alpha/beta h
92  long 105-amino acid mitochondrial targeting presequence (mTP).
93  domain hydrophobic region oriented with the presequence N terminus formed by signal peptidase cleava
94  (NTD) is intrinsically disordered and binds presequence near a region important for interaction with
95 presequence of the ribosomal protein L29 and presequence of 1-aminocyclopropane-1-carboxylic acid dea
96 rame of 2634 nucleotides encoding a putative presequence of 31 amino acid residues and a mature prote
97                                    A peptide presequence of 52 amino acids is cleaved to give the mat
98 ed a typical N-terminal mitochondrial target presequence of 64 residues and the presequence directed
99 lacking negative charges in the unstructured presequence of LF(N) translocate independently of the De
100             The latter effect depends on the presequence of LMP7, but not on LMP7 catalytic activity.
101 st for the first time that the 20-amino acid presequence of pro-SCP-2 alters SCP-2 structure to facil
102  these positive charges in the 19-amino acid presequence of rat liver aldehyde dehydrogenase was inve
103 from the first 25 amino acid residues in the presequence of subunit IV of yeast cytochrome c oxidase
104                  The mitochondrial targeting presequence of the "Rieske" protein (subunit 9) is lodge
105 N- and C-terminal fragments derived from the presequence of the ATPase beta subunit ranging in size f
106              We previously reported that the presequence of the F(1)-ATPase beta subunit precursor (p
107 e cytochrome bc1 complex, we mutagenized the presequence of the iron-sulfur protein to eliminate the
108 s, respectively, in the cleaved NH2-terminal presequence of the precursor protein (pre-LMP3), and six
109      Short mitochondrial targeting peptides (presequence of the ribosomal protein L29 and presequence
110 asts of a chimeric protein consisting of the presequence of the small subunit of ribulose 1,5-bisphos
111 imeric precursor proteins, consisting of the presequence of the small subunit of Rubisco fused to the
112 ue peptide derived from the membrane-binding presequence of yeast cytochrome c oxidase, and the pepti
113                   On the basis of the unique presequences of the nuclear genes and the recent mitocho
114     In contrast, the mitochondrial targeting presequences of these same proteins have not undergone a
115                  The mitochondrial targeting presequences of two sdh3 genes are derived from preexist
116 rt rates of artificial precursors containing presequences of varying length fused to either mouse dih
117 ese observations suggest that the N-terminal presequence on the avidin-bound precursor is available f
118 ed question in gene evolution: the origin of presequences or transit peptides that generally exist in
119  hierarchical dominance of the mitochondrial presequence over the NLS.
120 The protein analytes were positively charged presequences (pb2) of varying length fused to the small
121 f mitochondrial Abeta-degrading enzyme PreP (presequence peptidase) was enhanced in Tg mAPP mitochond
122 etic peptide corresponding to the 29-residue presequence peptide (mAAT-pp) with anionic phospholipid
123  could be re-assigned and characterized as a presequence peptide degrading enzyme in the matrix.Prote
124 om40 constructs specifically interact with a presequence peptide in a concentration- and voltage-depe
125 sistent with only a shallow insertion of the presequence peptide in the bilayer.
126 supported by the fact that the addition of a presequence peptide induces transient pore closure.
127  Based on these results, we propose that the presequence peptide may contain dual recognition element
128 no acid sequence, indicating a mitochondrial presequence peptide of only nine amino acids.
129 channel in the presence of the mitochondrial presequence peptide pF(1)beta revealed the kinetics of p
130 nnel formation or for the interaction with a presequence peptide.
131 o not, however, alter the activity of PSC, a presequence-peptide sensitive channel in the mitochondri
132                                      Cleaved presequence peptides then need to be efficiently degrade
133 s not significantly blocked by mitochondrial presequence peptides.
134 uded that positively charged residues in the presequence play a vital role in the import of precursor
135 m the mature protein portion and less on the presequence portion, when a synthetic peptide composed o
136                              Analysis of the presequence predicts that the protein is targeted to out
137                   Although the 20-amino acid presequence present in 15-kDa pro-sterol carrier protein
138 ure the correct functioning of the essential presequence processing machinery.
139                                              Presequence protease (PreP), a mitochondrial peptidasome
140 gradation of targeting peptides catalyzed by presequence protease.
141                      A role for the cargo in presequence recognition distinguishes Imp1p and Imp2p fr
142 otosystem II (pLHCPII) were used to identify presequence regions translocated into the ER lumen and s
143 y brominated phospholipids reveals that this presequence residue inserts to a depth of approximately
144 of the peptide corresponding to the R3Q/R10Q presequence revealed that this peptide was only somewhat
145  of hydrogenosomal and mitochondrial protein presequences reveals striking similarities.
146               These results suggest that the presequence segment lies close to the surface of the mem
147  peptide corresponding to the linker-deleted presequence showed that it was substantially more prone
148                                  Analysis of presequence structure and in vitro import experiments in
149                                  Analysis of presequence structure and in vitro import into microsoma
150                      They have an N-terminal presequence that allows recognition by the mitochondrial
151 to precursors with an NH2-terminal targeting presequence that are imported in a linear NH2-terminal m
152 ine-rich, 69-residue mitochondrial targeting presequence that is absent in the mature protein.
153 synthesized with an N-terminal 10-amino acid presequence that is cleaved during assembly of the compl
154 e presence of an eight amino acid N-terminal presequence that is similar to presequences found on all
155  as a preprotein with a cleavable N-terminal presequence that is the mitochondrial targeting signal,
156 ino-acid amino-terminal, organelle-targeting presequence that was cleaved in vivo.
157 their respective organelles using N-terminal presequences that are subsequently cleaved by a peptidas
158 tions of three peptides, which correspond to presequences that direct mitochondrial protein import, w
159 interaction, including the length of the pb2 presequence, the position of the electrostatic traps wit
160      Tim23p does not carry an amino-terminal presequence; therefore, the targeting information reside
161 ith the structural similarity of all Euglena presequences, these results demonstrate that chloroplast
162 to drive translocation of positively charged presequences through the TIM23 complex (presequence tran
163  of a conserved leucine at position 2 in the presequence to a glycine disrupts import of pFd into the
164 ct on the affinity or mode of binding of the presequence to model membranes.
165                                          The presequence translocase (TIM23 complex) sorts precursor
166                                          The presequence translocase constituent Pam17 is specificall
167 nclude that Mgr2 is a coupling factor of the presequence translocase crucial for cell growth at eleva
168                                          The presequence translocase of the inner membrane (TIM23 com
169  of the outer mitochondrial membrane and the presequence translocase of the inner membrane.
170                                          The presequence translocase of the inner mitochondrial membr
171 uence and are imported by the TIM23 complex (presequence translocase) located in the inner mitochondr
172 rged presequences through the TIM23 complex (presequence translocase), the activity of the Hsp70-powe
173  chaperone cooperates with cochaperones, the presequence translocase, and other chaperone systems.
174 ates with partner protein complexes like the presequence translocase-associated import motor and the
175 a through interactions with the import motor presequence translocase-associated motor (PAM).
176 ormal channel activity and disruption of the presequence translocase-associated motor complex did not
177  from the channel to the import motor of the presequence translocase.
178  to mitochondria and are translocated by the presequence translocase.
179 nown energy-dependent steps: Deltapsi-driven presequence translocation and adenosine triphosphate-dri
180 ot modify TIM23 channel activity nor prevent presequence translocation.
181  With precursors that have sufficiently long presequences, unfolding by the inner membrane import mac
182                                         This presequence was necessary to target Hsp60 to one (and oc
183 , whose sequences mimic mitochondrial import presequences, was measured using a novel, qualitative, f
184  the putative mitochondrial matrix targeting presequences) were co-expressed in Escherichia coli on o
185 are imported from the cytosol via N-terminal presequences, which are cleaved upon exposure to the mit
186 east promoters and a mitochondrial targeting presequence with the bacterial coding sequence.

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