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 on 11 of LMNA (the gene encoding lamin C and prelamin A).
2 s a deletion of 50 aa near the C terminus of prelamin A.
3 A and leads to the accumulation of farnesyl-prelamin A.
4 ctive processing and nuclear accumulation of prelamin A.
5 that result in the deletion of 50 aa within prelamin A.
6 g mice lacking the farnesylated CAAX protein prelamin A.
7 rf, that binds the carboxyl-terminal tail of prelamin A.
8 xyl-terminal 18 amino acid residues of human prelamin A.
9 ulation of farnesylated, membrane-associated prelamin A.
10 ), where all of the lamin A is produced from prelamin A.
11 A processing, leading to the accumulation of prelamin A.
12 lead to an accumulation of non-farnesylated prelamin A.
13 its ZMPSTE24 and leads to an accumulation of prelamin A.
14 biogenesis and leading to an accumulation of prelamin A.
15 the accumulation of the farnesylated form of prelamin A.
16 TE24, leading to an accumulation of farnesyl-prelamin A.
17 show that HIV-PIs caused an accumulation of prelamin A.
20 n of a lipid-modified (farnesylated) form of prelamin A, a protein that contributes to the structural
22 oes not occur, a farnesylated and methylated prelamin A accumulates in cells, causing a severe proger
23 lamin A missense mutations in the absence of prelamin A accumulation (P = 0.0003 and P < 0.0001).
27 involved in prelamin A processing, leads to prelamin A accumulation, an absence of mature lamin A, m
31 e splicing reduces transcripts for wild-type prelamin A and increases transcripts for a truncated pre
33 s focused on mutations in LMNA (the gene for prelamin A and lamin C) that cause particular muscular d
34 is caused by mutations in LMNA (the gene for prelamin A and lamin C) that result in the deletion of 5
35 ficiency in humans causes an accumulation of prelamin A and leads to lipodystrophy and other disease
39 e significantly impaired in VSMCs expressing prelamin A and that chemical inhibition and siRNA deplet
42 use brain, whereas lamin A and its precursor prelamin A are restricted to endothelial cells and menin
43 icate that progerin and full-length farnesyl-prelamin A are toxic to neurons of the enteric nervous s
44 e studies identify ASO-mediated reduction of prelamin A as a potential strategy to treat prelamin A-s
45 Nevertheless, an accumulation of farnesyl-prelamin A (as occurs with a deficiency in the prelamin
46 sor, prelamin A, lead to the accumulation of prelamin A at the nuclear envelope, cause misshapen nucl
47 asonably ascribed to defective processing of prelamin A, but the brittle bone phenotype suggests a br
49 ent of the nuclear lamina, is generated from prelamin A by four post-translational processing steps:
51 ) is caused by the production of a truncated prelamin A, called progerin, which is farnesylated at it
52 In vitro, aged VSMCs rapidly accumulated prelamin A coincidently with nuclear morphology defects,
53 s migrated more rapidly than nonfarnesylated prelamin A, comigrating with the farnesylated form of pr
55 f prelamin A regulation likely explains why "prelamin A diseases" such as Hutchinson-Gilford progeria
56 In progeria, the accumulation of farnesyl-prelamin A disrupts this scaffolding, leading to misshap
57 This peptide acts as a substrate for the prelamin A endoprotease in vitro, with cleavage of the s
60 n remains unclear, but it is intriguing that prelamin A expression in the brain is low and is regulat
62 are present at high levels in the brain, but prelamin A expression levels are very low-due to regulat
65 essing exclusively progerin (a toxic form of prelamin A found in Hutchinson-Gilford progeria syndrome
70 ified mice that express full-length farnesyl-prelamin A in neurons (Zmpste24-deficient mice carrying
72 e proposed that miR-9-mediated regulation of prelamin A in the brain could explain the absence of pri
76 fering RNA knockdown of FACE1 reiterated the prelamin A-induced nuclear morphology defects characteri
80 uncated mutant protein termed "progerin." WT prelamin A is anchored to the nuclear envelope by a farn
82 We hypothesized that the farnesylation of prelamin A is important for its targeting to the nuclear
89 of lamin A from its farnesylated precursor, prelamin A, lead to the accumulation of prelamin A at th
90 A-specific antisense oligonucleotide reduced prelamin A levels and significantly reduced the frequenc
94 and leads to an in-frame deletion within the prelamin A mRNA and the production of a dominant-negativ
96 ) mice were indistinguishable from those in "prelamin A-only" mice (Lmna(PLAO/PLAO)), where all of th
97 caused by the retention of farnesyl lipid on prelamin A, or by the retention of the last 15 amino aci
98 We monitored the proteolysis of farnesylated prelamin A peptide by ZMPSTE24 and unexpectedly found re
99 ibitors and showed that drug binding blocked prelamin A peptide cleavage and conferred stability to Z
100 tory phenotype factors/cytokines released by prelamin A-positive VSMCs, including the calcification r
102 elamin A (as occurs with a deficiency in the prelamin A processing enzyme Zmpste24) caused dramatical
105 Here we have reexamined the cellular site of prelamin A processing, and show that the mammalian and y
106 s a rare genetic disease caused by defective prelamin A processing, leading to nuclear lamina alterat
107 ficiency in ZMPSTE24, a protease involved in prelamin A processing, leads to prelamin A accumulation,
110 HGPS results from a dominant mutant form of prelamin A (progerin) that has an internal deletion of 5
113 ogeria syndrome (HGPS) is caused by a mutant prelamin A, progerin, that terminates with a farnesylcys
116 duced the expression of progerin, the mutant prelamin A protein in HGPS, in fibroblasts derived from
117 -like protein 1 (IOP1; also known as nuclear prelamin A recognition factor like protein, or NARFL) is
119 y hydrogenase-like protein 1)/NARFL (nuclear prelamin A recognition factor-like), a cytosolic protein
122 Moreover, treating Zmpste24-/- cells with a prelamin A-specific antisense oligonucleotide reduced pr
124 progeria syndrome (HGPS), that are caused by prelamin A-specific mutations could be treated by shifti
128 ation or deletion of the CaaX motif from the prelamin A tail domain inhibits Narf binding in yeast tw
129 A, comigrating with the farnesylated form of prelamin A that accumulates in ZMPSTE24-deficient fibrob
131 disease caused by the synthesis of a mutant prelamin A that cannot undergo processing to lamin A.
132 tion that leads to the synthesis of a mutant prelamin A that is farnesylated but cannot be further pr
133 tively spliced products of LMNA, lamin C and prelamin A (the precursor to lamin A), are produced in s
136 e of the presumed lack of ZMPSTE24 activity, prelamin A, the unprocessed toxic form of lamin A, was d
137 lloproteinase required for the processing of prelamin A to lamin A, a structural component of the nuc
138 s the endoproteolytic processing of farnesyl-prelamin A to mature lamin A and leads to the accumulati
139 able in mice and that the failure to convert prelamin A to mature lamin A causes cardiomyopathy (at l
142 ents that target the DNA damage response and prelamin A toxicity may be potential therapies for the t
145 no lamin A, a consequence of the removal of prelamin A transcripts by miR-9, a brain-specific microR
146 a Lmna knock-in allele yielding full-length prelamin A transcripts lacking a miR-9 binding site).
147 all the output of the gene is channeled into prelamin A transcripts, large amounts of lamin A were fo
148 with a farnesyltransferase inhibitor (FTI), prelamin A was partially mislocalized away from the nucl
149 creased lamin C production at the expense of prelamin A when transfected into mouse and human fibrobl
151 ls of GFP-progerin or an uncleavable form of prelamin A with a Zmpste24 cleavage site mutation induce
153 is first synthesized as a 74-kDa precursor, prelamin A, with a C-terminal CaaX motif and undergoes a
154 24 deficiency results in the accumulation of prelamin A within cells, a complete loss of mature lamin
155 mpste24(-/-) mice with half-normal levels of prelamin A (Zmpste24(-/-) mice with one Lmna knockout al
WebLSDに未収録の専門用語(用法)は "新規対訳" から投稿できます。