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1                                              FOP (FGFR1 Oncogene Partner) is a known centrosome prote
2                                              FOP is caused by dominantly acting mutations in the gene
3                                              FOP is caused by mutations in the type I BMP receptor ge
4                                              FOP mutations break critical interactions that stabilize
5                                              FOP showed high uptake and slow clearance of radioactivi
6                                              FOP-associated mutations in the BMP receptor ALK2 reduce
7                                              FOP-FGFR1, an oncogenic fusion that causes a form of leu
8                                           15 FOP patients (age 10-52) and 13 healthy controls were as
9 n-specific enolase (NSE) promoter develops a FOP-like phenotype.
10 al partner of centriolar proteins CEP350 and FOP.
11  by twinned, N-terminal TOF (TON1, OFD1, and FOP) and LisH motifs, motifs that otherwise facilitate l
12 bition of YAP or SHH abolished HO in POH and FOP and acquired HO mouse models without affecting norma
13                                 As for BBS4, FOP localization to satellites is cell cycle dependent,
14 derstanding and drug development hard-won by FOP researchers to pediatric neurooncology.
15 genetic protein (BMP) type 1 receptor, cause FOP by dramatically altering the normal physiologic func
16 liopathy protein, CEP19, we identify CEP350, FOP, and the RABL2B GTPase as proteins organizing the fi
17                                   The CEP350-FOP complex in association with CEP78 or OFD1 controls c
18 ompromised CEP350-/- cells, while the CEP350-FOP-WDR90 axis secures centriole integrity.
19 to the ciliary base by the centriolar CEP350/FOP complex and then specifically captures GTP-bound RAB
20 s significantly more active than the classic FOP mutation ACVR1(R206H) when overexpressed in chicken
21  that the ACVR1(Q207E) resembles the classic FOP receptor in these assays, not the engineered ACVR1(Q
22 cated in a codon adjacent to the most common FOP mutation [c.617G>A, p.R206H] of Activin A Receptor,
23                 DIs underpinning most common FOP nutrition labels and reflecting nutrient-poor diets
24                        Relative to controls, FOP patients demonstrated significantly lower regional a
25                    When iodide-bridged dimer FOP precatalysts are activated by reaction with excess s
26 p.Q207D-c.a. mice have served as a model for FOP HO in several in vivo studies.
27 tation has severe limitations as a model for FOP, whereas the naturally occurring mutations p.R206H a
28 rminal M2 motif of CAP350 is responsible for FOP recruitment at the centrosome.
29 should not be considered as therapeutics for FOP.
30 PCs) single-cell transcriptome analyses from FOP also revealed unusually increased ECM and osteogenic
31 istance values, were associated with greater FOP burden (CAJIS score range: 4-30) and lower physical
32 by liver and the high sensitivity of hepatic FOP DV to changes of HMFAO with CPT-I inhibition and hyp
33 ic differentiation in primary mouse or human FOP cells, and diminished in vivo extraskeletal ossifica
34                                           In FOP, ALK2 variants display increased and dysregulated si
35      We aimed to define a novel biomarker in FOP that enables reliable assessment of musculoskeletal
36       Further investigation of garetosmab in FOP is ongoing.
37 f ACVR1 by ligands should also inhibit HO in FOP and provide an additional therapeutic option for thi
38 operty is underscored by the fact that HO in FOP is exquisitely dependent on activation of FOP-mutant
39 2 may be a candidate for prevention of HO in FOP.
40 apable of characterizing muscle integrity in FOP.
41  demonstrate that failure to form the NSC in FOP results in more severe disease pathology.
42 s contribute to endochondral ossification in FOP remains unknown.
43 sion that the mutant R206H ACVR1 receptor in FOP patients is an activating mutation that induces BMP
44 esis, osteogenesis and joint fusions seen in FOP.
45 and tested its effect on HO in 2 independent FOP mouse models.
46 om human exfoliated deciduous teeth with key FOP signaling components, including activin A receptor t
47                                    We mapped FOP to chromosome 2q23-24 by linkage analysis and identi
48 ssays revealed that both naturally occurring FOP receptors (ACVR1(R206H) and ACVR1(Q207E)) were activ
49 OP is exquisitely dependent on activation of FOP-mutant ACVR1 by activin A, an effect countered by in
50 our understanding of the clinical aspects of FOP.
51                                 All cases of FOP are caused by activating mutations in the type I BMP
52  The fundamental pathological consequence of FOP-causing ACVR1 receptor mutations is to enable activi
53              Although the genetic defects of FOP are not known, several lines of evidence have sugges
54                                 Depletion of FOP strongly inhibits primary cilium formation in human
55  to clarify the intracellular disposition of FOP in the liver and test its validity as a tracer of HM
56 tor regulation and to address the effects of FOP mutation, we determined the crystal structure of the
57 mmol/L), the externally measured kinetics of FOP showed reversible binding in tissue.
58 ly small levels of diffusible metabolites of FOP were formed in vivo and in isolated rat liver.
59  article examines the emergent properties of FOP's diverse phenotypes, proposes a schema for targetin
60 se results uncover an additional property of FOP-mutant ACVR1 and indicate that anti-ACVR1 antibodies
61 ies stimulated HO and activated signaling of FOP-mutant ACVR1.
62 6H) inhibitor developed for the treatment of FOP.
63                      The selective uptake of FOP by liver and the high sensitivity of hepatic FOP DV
64 3Kalpha, without directly affecting ACVR1 or FOP-inducing ACVR1(R206H) kinase activities.
65        Here, we showed that the wild-type or FOP-mutant ACVR1 localized in the cilia of stem cells fr
66 healthfulness of foods for front-of-package (FOP) labeling, which have been proposed as an effective
67 ased on a ferrocenyloxazoline palladacyclic (FOP) scaffold were synthesized and evaluated for the rea
68 r-added 15-[18F]fluoro-3-oxa-pentadecanoate (FOP) was synthesized and evaluated in living rats and is
69 undus images from Remidio's Fundus-on-Phone (FOP NM-10).
70                      Rare and unique primary FOP human muscle stem cells (Hu-MuSCs) isolated from cad
71 order fibrodysplasia ossificans progressiva (FOP) and have been shown to constitutively activate the
72 ns of fibrodysplasia ossificans progressiva (FOP) in human history are unknown but the condition has
73 assic fibrodysplasia ossificans progressiva (FOP) is a congenital syndrome resulting from highly cons
74       Fibrodysplasia ossificans progressiva (FOP) is a disabling genetic disorder of progressive hete
75       Fibrodysplasia ossificans progressiva (FOP) is a genetic form of HO caused by mutations in the
76       Fibrodysplasia ossificans progressiva (FOP) is a rare autosomal dominant disorder of skeletal m
77       Fibrodysplasia ossificans progressiva (FOP) is a rare but devastating disorder of extraskeletal
78       Fibrodysplasia ossificans progressiva (FOP) is a rare disease characterized by heterotopic ossi
79       Fibrodysplasia ossificans progressiva (FOP) is a rare genetic disease characterized by progress
80       Fibrodysplasia ossificans progressiva (FOP) is a rare genetic disease driven by gain-of-functio
81       Fibrodysplasia ossificans progressiva (FOP) is a rare genetic disorder whose most debilitating
82       Fibrodysplasia ossificans progressiva (FOP) is a rare hereditary connective tissue disease char
83       Fibrodysplasia ossificans progressiva (FOP) is a rare human genetic disorder characterized by a
84       Fibrodysplasia ossificans progressiva (FOP) is a severely disabling, autosomal-dominant disorde
85       Fibrodysplasia ossificans progressiva (FOP) is an ultra-rare disorder involving skeletal dyspla
86 order fibrodysplasia ossificans progressiva (FOP) provides a unique window into ACVR1/Activin A signa
87 s for fibrodysplasia ossificans progressiva (FOP), a debilitating and progressive heterotopic ossific
88  with fibrodysplasia ossificans progressiva (FOP), a disease in which heterotopic ossification occurs
89 e use fibrodysplasia ossificans progressiva (FOP), a disease of progressive HO caused by ACVR1(R206H)
90       Fibrodysplasia ossificans progressiva (FOP), a disorder of congenital skeletal malformations an
91 as in fibrodysplasia ossificans progressiva (FOP), another genetic HO, and nonhereditary HO mouse mod
92 ed in fibrodysplasia ossificans progressiva (FOP), diffuse intrinsic pontine gliomas, and ependymomas
93 ) and fibrodysplasia ossificans progressiva (FOP), respectively.
94 drome fibrodysplasia ossificans progressiva (FOP), resulting in the transformation of soft tissue int
95 order fibrodysplasia ossificans progressiva (FOP), which is characterized by ectopic cartilage and bo
96  from fibrodysplasia ossificans progressiva (FOP).
97 calization and binding to centriolar protein FOP, we propose that imbalanced activity of this centros
98       Crossover events localize the putative FOP gene within a 36-cM interval bordered proximally by
99 on in Acvr1(Q207D), Sox2-Cre; Acvr1(R206H/+) FOP mice and in burn tenotomy-treated wild-type mice.
100 ng signaling from ALK2(R206H) and other rare FOP variants in cells in vitro without affecting signali
101 6%-4.3% for Topcon vs. 1.7%-2.1% for Remidio FOP) and more images as excellent from the Remidio FOP (
102 nd more images as excellent from the Remidio FOP (59%-74%) than the Topcon device (52%-61%).
103 d from three fields of view with the Remidio FOP and a Topcon tabletop fundus camera (Topcon Medical
104                                  The Remidio FOP device was found to have high sensitivity and specif
105   Sensitivity and specificity of the Remidio FOP for the detection of any DR compared to clinical exa
106 l examination, using images from the Remidio FOP, graders 1 and 2 reported a sensitivity of 93.1% (95
107 ality was marginally better with the Remidio FOP.
108               These results demonstrate that FOP-ACVR1 is not constrained by the same receptor/ligand
109     Considering logistical difficulties that FOP patients often face, our goal was to identify an at-
110                                 We find that FOP partially co-localizes with the satellite component
111 to support the widely shared hypothesis that FOP labels, possibly in conjunction with other intervent
112                   These results suggest that FOP is a centriolar satellite cargo protein and, as for
113                                          The FOP phenotype is linked to markers located in the 4q27-3
114  To identify the chromosomal location of the FOP gene, we conducted a genomewide linkage analysis, us
115             Male-to-male transmission of the FOP phenotype excluded X-linked inheritance.
116                          Localization of the FOP-FGFR1 fusion kinase to centriolar satellites may be
117                       We determined that the FOP mutants ACVR1-R206H and -G328R do not require their
118 easurement, and fundus photography using the FOP NM-10 camera.
119 at disease Activin can either signal through FOP-mutant ACVR1 or form NSCs with wild-type ACVR1.
120              This property was restricted to FOP-mutant ACVR1 and resulted from anti-ACVR1 antibody-m
121 , including bioinformatics analysis and TOP-/FOP-flash reporter assays, demonstrated that the activat
122 , including bioinformatics analysis and TOP-/FOP-flash reporter assays, demonstrated that the activat
123  along with TrkC-miR2 overexpression and TOP/FOP flash assays confirmed the positive effect of TrkC-m
124  exposure was any dietary index underpinning FOP nutrition labels [e.g., the modified Food Standard A
125  association of dietary indices underpinning FOP nutrition labels with all-cause mortality and incide
126 ent, with few satellites labeled in G1, when FOP protein levels are lowest, and most labeled in G2.
127        To investigate the mechanism by which FOP-ACVR1 enhances pSmad1/5 activation, we used zebrafis
128 diverse ALK2 mutant proteins associated with FOP and DIPG.
129 ivation in fibroblasts from individuals with FOP in a dose-dependent manner.
130 a human centrosomal protein interacting with FOP, and the C-terminal M2 motif of CAP350 is responsibl
131 ings may also explain why some patients with FOP develop ectopic bones through endochondral ossificat
132  phase 2 LUMINA-1 trial, adult patients with FOP were randomized to garetosmab, an activin A-blocking
133 anti-ACVR1 antibodies to treat patients with FOP.
134 (TON1) proteins, which share similarity with FOP, a human centrosomal protein, are essential for micr

 
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