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1 er, lysosomal-associated membrane protein 2 (LAMP2).
2 ransgene LAMP2B, which encodes an isoform of LAMP2.
3 P1 and CD63 and an increase in the amount of LAMP2.
4 assays were used to localize cathepsin B and Lamp2.
5 r Gag and the late endosome/lysosomal marker Lamp2.
6 localization but little co-localization with LAMP2.
7 mples contained mutations in GLA, PRKAG2, or LAMP2.
8 AG2, lysosome-associated membrane protein 2 (LAMP2), alpha-galactosidase (GLA), and acid alpha-1,4-gl
9      Mutations in sarcomere protein, PRKAG2, LAMP2, alpha-galactosidase A (GLA), and several mitochon
10 eless, the protease plays a role in reducing LAMP2 and LAP activity levels, as these are partially re
11 th viral proteins (p17 and sigmaC), p62 with LAMP2 and LC3 with Rab7 was observed under a fluorescenc
12                     Quantitation of cellular LAMP2 and NPC1 protein levels suggest that LAMP proteins
13 ompe's disease (GAA) were not found, but two LAMP2 and one PRKAG2 mutations were identified in proban
14  and the autophagy-lysosome pathway proteins Lamp2 and p62 relocalized to the area of the vimentin ac
15 ting ventricular preexcitation revealed four LAMP2 and seven PRKAG2 mutations.
16 ed markers specific for lysosomes (LAMP1 and LAMP2) and autophagosomes (LC3-II/I).
17 r, decreased lysosomal associated protein 2 (LAMP2) and HIF-1alpha levels and modified cytokine produ
18 p62, lysosome-associated membrane protein 2 (LAMP2), and microtubule-associated protein light chain (
19                                 While LAMP1, LAMP2, and Cathepsin D were abundant across LELs, markin
20 resence of acid phosphatase, accumulation of LAMP2, and fusion with rhodamine B-isothiocyanate-labele
21 did not colocalize with the lysosomal marker LAMP2, and lysosomes were redistributed and dramatically
22 ive specific genes, AP3B1, ATP6AP1, BLOC1S1, LAMP2, and RAB11A, has confirmed novel roles for these p
23 A1 treatment, and increased levels of LAMP1, LAMP2, and RAB7 proteins required for lysosomal biogenes
24 ins; ARH, a coat protein that binds megalin; LAMP2; and LC3.
25 tophagy (specific factors including mTOR and LAMP2), apoptosis (including BAD and BID), ferroptosis a
26            We show here that human LAMP1 and LAMP2 bind cholesterol in a manner that buries the chole
27                                              LAMP2 cardiomyopathy is a profound disease process chara
28 stribution of seven key LEL proteins (LAMP1, LAMP2, CD63, Cathepsin D, TMEM192, NPC1, and LAMTOR4).
29 of bone marrow-derived DC were retained in a LAMP2+ compartment.
30 arged acidic vesicles that were positive for LAMP2, confirming their endolysosomal origin.
31     The B5R protein was also associated with LAMP2-containing vesicles when F13L-GFP was coexpressed,
32 d lysosome-associated membrane protein gene (LAMP2; Danon disease) produce a cardiomyopathy in young
33                                              LAMP2 deficiency causes Danon's disease, an X-linked hyp
34 f the Hprt region as: Agtr2-Pem-Ant2-DXMit50-Lamp2-DXMit49.
35 d to be safe and was associated with cardiac LAMP2 expression and evidence of clinical improvement ov
36 n culture, reduced LC3 levels, and increased LAMP2 expression.
37 some-associated membrane proteins, LAMP1 and LAMP2, from Pompe iPSC-CMs demonstrated higher electroph
38 s caused by loss of function variants in the LAMP2 gene and is among the most severe and penetrant of
39 2A), one of the three splice variants of the lamp2 gene, and this binding is limiting for their degra
40   Isoelectric focusing studies revealed that LAMP2 has a more alkaline pI in Pompe compared with cont
41 in genes and 3 other genes (GLA, PRKAG2, and LAMP2) implicated in idiopathic cardiac hypertrophy.
42 1, which in turn, resulted in degradation of LAMP2 in activated microglia.
43 ization and substantial co-localization with LAMP2 in late endosomes.
44 d by alcohol, targets mTOR, Rheb, LAMP1, and LAMP2 in the authophagy pathway.
45 and lysosomal-associated membrane protein 2 (LAMP2) in livers with ALD.
46 Clinical features associated with defects in LAMP2 included male sex, severe hypertrophy, early onset
47 Mechanistically, down-regulation of LAMP1 or LAMP2 increased exosome release in hepatocytes and macro
48                    A detailed examination of LAMP2 indicated that the reduced LAMP2 levels are not th
49 ealed incorporation of CD63 and CD81 but not Lamp2 into virions budding at the plasma membrane, and t
50                         We also observe that LAMP2 is located at the plasma membrane in clinical samp
51                                              LAMP2 is needed for chaperone-mediated autophagy, and it
52   Furthermore, we show that the depletion of LAMP2 is sufficient to increase acidosis-mediated toxici
53 ceptor, epidermal growth factor receptor, or Lamp2, is detected.
54  deletion of both Lamp2a and Lamp2c, another Lamp2 isoform, producing Lamp2AC global knockout (L2ACgK
55                 The gene expression of other LAMP2 isoforms and proteasome and lysosomal proteases ac
56                    Transcripts for the three LAMP2 isoforms increased with B cell activation, althoug
57 mination of LAMP2 indicated that the reduced LAMP2 levels are not the result of an altered biosynthet
58 6 treated cells to sorafenib reduced p62 and LAMP2 levels, decreased the ratio of LC3 to LC3II, and r
59 the levels of three other lysosomal markers: LAMP2, lysosomal acid phosphatase (LAP), and CD63.
60 n be distinguished from cholesterol-enriched LAMP2(+) lysosomes.
61 l in the first 2 h and were instead found in LAMP2+, major histocompatibility complex class II+ (MHC-
62 t of lysosome-associated membrane protein-2 (LAMP2)(+)/mannose 6-phosphate receptor(-) vesicles that
63 ient samples, there is a high correlation of LAMP2 mRNA and protein expression with progression.
64 ster of the proband is a carrier of the same LAMP2 mutation and has HCM without skeletal myopathy or
65 ly in 7 young patients (6 boys) with defined LAMP2 mutations from the time of diagnosis (age 7-17 yea
66  this study we investigated the frequency of LAMP2 mutations in an unselected pediatric HCM populatio
67                                              LAMP2 mutations may account for a significant proportion
68                                              LAMP2 mutations typically cause multisystem glycogen-sto
69 ellular acidosis (as indicated by the marker LAMP2 near/at the plasmalemma), which can explain the ad
70  abnormalities revealed mutations in neither LAMP2 nor PRKAG2.
71 tion breakpoint and six genes (ANT2, NDUFA1, LAMP2, OCRL, IGSF1, and HDGF) at better than 100-kb reso
72  glycogen-storage cardiomyopathy produced by LAMP2 or PRKAG2 mutations resembles hypertrophic cardiom
73 hagosome-lysosome fusion by shRNAs targeting LAMP2 or Rab7a resulted in inhibition of viral protein s
74                             The knockdown of LAMP2 or the knockout of GBA in conjunction with PFF adm
75 number; pH; expression of lysosomal proteins LAMP2, P62, and LC3B; and lysosomal function.
76  by lysosomal-associated membrane protein 2 (LAMP2)-positive lysosomes, whereas virulent Staphylococc
77 ed, lysosomal-associated membrane protein 2 (LAMP2)-positive lysosomes.
78 nts (lysosome-associated membrane protein 2 (LAMP2)-positive).
79 y alanines, only partially co-localized with LAMP2-positive compartments following inhibition of lyso
80 elet-derived growth factor receptor alpha to LAMP2-positive endomembranes in the absence of ligand, s
81  receptor, where the receptor is shuttled to LAMP2-positive lysosomes.
82 2 receptor trafficking in Rab11-, Rab7-, and Lamp2-positive vesicles, indicating recycling and degrad
83                      Inhibition of LAMP1 and LAMP2 promotes exosome release in ALD.
84 on fraction at baseline, we observed cardiac LAMP2 protein expression and a reduction from baseline i
85 d membrane 2 gene (LAMP2), which encodes the LAMP2 protein.
86                                    LAMP1 and LAMP2 proteins are highly abundant, ubiquitous, mammalia
87 ociated with an HCM mimic (GLA, TTR, PRKAG2, LAMP2, PTPN11, RAF1, and DES).
88 anocytes (ie, Silver/Pmel17, Melan-A/MART-1, LAMP2, Rab 27, transferrin, c-kit, adaptin-3, and the HP
89 of the lysosomal membrane proteins LAMP1 and LAMP2 resulted in decreased cell viability, as did treat
90 phagosome maturation) by chloroquine (CQ) or Lamp2 shRNA, it was substantially diminished by inhibiti
91 d with a marker of late endosomes/lysosomes, LAMP2, specifying redirection from a recycling to a degr
92 68, lysosomal-associated membrane protein 2 (LAMP2), stabilin-1, and macrophage receptor with collage
93 rate doxorubicin (DOX) became sequestered in LAMP2-stained lysosomes, but this was not observed in no
94 ated that intracellular Pgp was localized to LAMP2-stained lysosomes.
95                     Prominent among these is LAMP2 that functions to protect lysosomal membranes from
96 degradation pathway due to overexpression of lamp2, the human form of lgp96, the degradation of Ikapp
97 e experiments show that the ability of human LAMP2 to facilitate cholesterol export from lysosomes re
98 cise resulted in rapid translocation of mTOR/LAMP2 towards the cell membrane.
99 ety and toxic effects of RP-A501, myocardial LAMP2 transduction and protein expression, stabilization
100                                              LAMP2 upregulation by acidosis is confirmed both in vitr
101 ds to endolysosomes and the formation of the LAMP2+VAMP3+ hybrid compartment in which IFN-I productio
102 hus facilitates degradation of a fraction of LAMP2 via microautophagy to regenerate the lysosomal mem
103                                              LAMP2 was amplified from genomic DNA isolated from perip
104  and lysosome-associated membrane protein 2 (LAMP2) was observed.
105 cifically, in ARSACS HDFs cellular levels of Lamp2 were elevated while levels of p62, which is degrad
106               mTOR and the lysosomal protein LAMP2 were highly co-localised in basal samples.
107 sylation of the heavily glycosylated protein LAMP2 were normal.
108                      Accumulation of p62 and Lamp2 were prominent in the brain suggesting the impairm
109 in the lysosomal-associated membrane 2 gene (LAMP2), which encodes the LAMP2 protein.
110 es of GBM tissue presented overexpression of LAMP2, which correlated with advanced glioma grade and p
111                 We also sequenced PRKAG2 and LAMP2, which encode metabolic proteins; mutations in the

 
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