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1                                              FANCI and EYA4 were identified as candidate DNA repair-r
2                                              FANCI and FANCD2 form the "ID" complex that loads onto c
3                                              FANCI is in close proximity to SF3B1 in the nucleoplasm
4                                              FANCI is integral to the Fanconi anemia (FA) pathway of
5                                              FANCI shares sequence similarity with FANCD2, likely evo
6                                              FANCI switches from FANCD2/repair to PIDD1/apoptosis sig
7                                              FANCI was localized in spermatocytes and spermatids and
8                                              FANCI:FANCD2 monoubiquitination is a critical event for
9 ANCD1 (1), FANCD2 (3), FANCF (2), FANCG (2), FANCI (1), FANCJ (2), and FANCL (3).
10 aster rate than FANCI, which can result in a FANCI-ubiquitinated ID2 complex (I(Ub) D2).
11 ions with RNA polymerase II on the BRCA1 and FANCI genes suggest a transcriptional defect in the abse
12 lized to viral replication compartments, and FANCI-D2 interacted with a multisubunit complex containi
13                               How FANCD2 and FANCI are anchored to chromatin remains unknown.
14                                   FANCD2 and FANCI are thought to form a functional heterodimer durin
15                In chromatin, both FANCD2 and FANCI associate with SF3B1, prevent accumulation of post
16 e model of the FXDs, but that the FANCD2 and FANCI associated nuclease 1 (FAN1), a component of the F
17 followed by monoubiquitination of FANCD2 and FANCI by the FA core complex.
18 structures of recombinant chicken FANCD2 and FANCI complexes.
19                   We propose that FANCD2 and FANCI contribute to the organization of functional domai
20 , monoubiquitination responses of FANCD2 and FANCI exhibit distinct DNA substrate specificities.
21          Our results suggest that FANCD2 and FANCI function separately at consecutive steps during DN
22                                   FANCD2 and FANCI function together in the Fanconi anemia network of
23 dimerization of monoubiquitinated FANCD2 and FANCI in chromatin is mediated in part through a noncova
24 ut cells display a unique lack of FANCD2 and FANCI localization to chromatin in exponentially growing
25                 Monoubiquitinated FANCD2 and FANCI localize in chromatin-associated nuclear foci wher
26 he role of a proper DNA ligand in FANCD2 and FANCI monoubiquitination, and reveal regulatory mechanis
27 d PCNA stimulates FANCL-catalyzed FANCD2 and FANCI monoubiquitylation.
28 via the monoubiquitination of the FANCD2 and FANCI proteins, targeting these proteins to discrete nuc
29  is the monoubiquitination of the FANCD2 and FANCI proteins, which occurs within chromatin.
30 ty of RAD18 in the recruitment of FANCD2 and FANCI to chromatin and the events leading to their ubiqu
31 ANCL, monoubiquitination of human FANCD2 and FANCI was examined.
32 s require Fanconi anemia proteins FANCD2 and FANCI, as well as Blm helicase, but not canonical DDR si
33 coni anemia (FA) pathway members, FANCD2 and FANCI, contribute to the repair of replication-stalling
34 rotein complex that ubiquitinates FANCD2 and FANCI, leading to formation of DNA repair structures.
35 lso play a role in mitosis, since FANCD2 and FANCI, the 2 key FA proteins, are localized to the extre
36 cruitment of two central players, FANCD2 and FANCI, to sites of stalled replication forks.
37 is positioned at the interface of FANCD2 and FANCI, where it acts as a covalent molecular pin to trap
38 nd chromatin localization of both FANCD2 and FANCI.
39 ion and chromatin localization of FANCD2 and FANCI.
40 onsible for monoubiquitination of FANCD2 and FANCI.
41 ination of the downstream targets FANCD2 and FANCI.
42 alyzing the monoubiquitination of FANCD2 and FANCI.
43 red for the monoubiquitylation of FANCD2 and FANCI.
44 machine for monoubiquitination of FANCD2 and FANCI.
45 ial for the monoubiquitination of FANCD2 and FANCI.
46 not for the monoubiquitination of FANCD2 and FANCI.
47  monoubiquitinates its substrates FANCD2 and FANCI.
48 nt attachment of monoubiquitin to FANCD2 and FANCI.
49 accumulation of monoubiquitinated FANCD2 and FANCI.
50 ns, FA complementation group D2 (FANCD2) and FANCI.
51 , retention of monoubiquitinated FANCD2, and FANCI in chromatin, and for efficient ICL repair.
52 assembly of the FA core complex, FANCD2, and FANCI into DNA repair foci.
53  FANCL with its partners, Ube2t, FANCD2, and FANCI.
54 romosome 15, likely underlain by FANCD2- and FANCI-associated nuclease 1 (FAN1), a nuclease involved
55 s, we generated isogenic FANCI-, FANCD2- and FANCI:FANCD2 double-null cells.
56 clude FANCD2, FANCA, FANCG, ERCC4, FANCE and FANCI, while DNA mismatch repair genes MSH3 and PMS1 out
57 stic insight into the functions of FANCL and FANCI in the catalysis of FANCD2 monoubiquitination.
58   Monoubiquitination and deubiquitination at FANCI K523 impact interactor selection.
59                                         Both FANCI and FANCD2 proteins co-localized with RPA along me
60 g these genes, eight, including CHEK1, CDC6, FANCI, GINS2, MAD2L1, ORC1, RACGAP1, and SMC4, have demo
61 x monoubiquitinates and recruits the central FANCI and FANCD2 proteins that subsequently coordinate I
62            Reciprocally, apoptosis-committed FANCI reverts from PIDD1 to FANCD2 after a failed attemp
63                                 In contrast, FANCI is dispensable for FANCD2-dependent BLMcx regulati
64 cient for FA complementation group I and D2 (FANCI and FANCD2) that function as part of the FA I-D2 c
65 y is the Fanconi anemia I-Fanconi anemia D2 (FANCI-FANCD2) (ID) complex, which is activated by DNA da
66           Upon the occurrence of DNA damage, FANCI becomes monoubiquitinated on Lys-523 and relocaliz
67    Here, we focus on an FA-I patient-derived FANCI mutant protein, R1299X (deletion of 30 residues fr
68                      Although loss of either FANCI or FANCD2 is known to prevent monoubiquitination o
69 hed DNA structures when compared with either FANCI or FANCD2 alone.
70 o germline mutations in FANCA, FANCB, FANCC, FANCI or BRIP1/FANCJ or proficient due to correction wit
71 on of FA effector proteins FANCI and FANCD2 (FANCI-D2) and required the viral DNA polymerase.
72                                 Like FANCD2, FANCI is monoubiquitinated and unexpectedly, ubiquitinat
73                                       FANCD2-FANCI adopts a closed conformation when the FANCD2 subun
74  which requires pathway activation by FANCD2-FANCI monoubiquitination and upstream FANC core complex
75 anched DNA-binding mode that enhances FANCD2-FANCI monoubiquitination through FA core complex interac
76 rylation is the molecular trigger for FANCD2-FANCI dissociation.
77 rst structural insight into the human FANCD2-FANCI complex by obtaining the cryo-EM structure.
78 n of a pseudosymmetric heterodimer of FANCD2-FANCI(4,5) by the FA core complex-a megadalton multiprot
79      Together, our work suggests that FANCD2-FANCI is a clamp that is locked onto DNA by ubiquitin, w
80                                   The FANCD2-FANCI (D2-I) protein complex is central to this process
81 ults uncover the mechanism of how the FANCD2-FANCI complex activates the FA pathway, and explains the
82                      We show that the FANCD2-FANCI complex forms independently of ATR and FA core com
83                                   The FANCD2-FANCI complex is central to the pathway, and localizes t
84 egulated or what the functions of the FANCD2-FANCI complex versus the monomeric proteins are.
85 diating the monoubiquitination of the FANCD2-FANCI complex.
86 k repair is monoubiquitination of the FANCD2-FANCI heterodimer, which then recruits nucleases to remo
87 essive mutations in the gene encoding FANCD2/FANCI-associated nuclease 1 (FAN1) cause KIN in humans.
88 lear core complex to monoubiquitinate FANCD2/FANCI in response to DNA damage.
89  of their ability to monoubiquitinate FANCD2/FANCI.
90                         Deficiency of FANCD2/FANCI-associated nuclease 1 (FAN1) in humans leads to ka
91      How USP1/UAF1 is targeted to the FANCD2/FANCI heterodimer has remained unknown.
92  each carried nonsense variant in the FANCD2/FANCI-associated nuclease 1 gene (FAN1), which encodes a
93 biquitination and deubiquitination of FANCD2:FANCI heterodimer is central to DNA repair in a pathway
94 s for temporal and spatial control of FANCD2:FANCI monoubiquitination that is critical for chemothera
95 nd restrict monoubiquitination to the FANCD2:FANCI heterodimer in only a DNA-bound form.
96  FANCC, FANCD1, FANCD2, FANCE, FANCF, FANCG, FANCI, FANCJ, FANCL, FANCM, and FANCN).
97 the first conditional inactivation model for FANCI in mouse.
98          These data reveal a unique role for FANCI as a modulator of dormant origin firing and link t
99 alysis finds evidence for multiple roles for FANCI in the maintenance of plant genome stability.
100 trating functional separation of FANCD2 from FANCI.
101 ivation triggers dissociation of FANCD2 from FANCI.
102 e report the functions of FANCONI ANAEMIA I (FANCI), an Arabidopsis thaliana homologue of the mammali
103 itylation of the FA complementation group I (FANCI)-FANCD2 (ID) complex by FA complementation group L
104                                To address if FANCI is also involved in these FANCD2-dependent mechani
105                                 Importantly, FANCI and FANCD2 monoubiquitination is co-dependent, sug
106                                  Mutation in FANCI is responsible for loss of a functional FA pathway
107                  Interestingly, mutations in FANCI that impair its DNA binding activity compromise DN
108 aracterize important structural region(s) in FANCI that is required to activate the FA pathway.
109 -dependent mechanisms, we generated isogenic FANCI-, FANCD2- and FANCI:FANCD2 double-null cells.
110                                Cells lacking FANCI have reduced number of origins, increased inter-or
111           Genetic analysis of plants lacking FANCI displays significant hypersensitivity to the DNA c
112                                          lnc-FANCI-2 in CaSki interacts with cellular proteins H13, H
113          Relative to the parental cells, lnc-FANCI-2 KO cells exhibited significantly increased RAS s
114                                     High lnc-FANCI-2 and low MCAM levels in cervical cancer tissues w
115 nology, we knocked out the expression of lnc-FANCI-2 in the HPV16-positive cervical cancer cell line,
116                        A key function of lnc-FANCI-2 intrinsically regulates RAS signaling to impact
117                  Increased expression of lnc-FANCI-2, a newly discovered long noncoding RNA, is assoc
118 ctor YY1 are two major factors promoting lnc-FANCI-2 expression.
119  We show that in plant cells, as in mammals, FANCI forms a nuclear localised complex with FANCD2.
120                   Intriguingly, ATR-mediated FANCI phosphorylation inhibits dormant origin firing whi
121  recruited to lesions by a monoubiquitinated FANCI-FANCD2 (ID) complex and participates in ICL repair
122     Our results reveal how monoubiquitinated FANCI:FANCD2, defective in many cancer types and all cas
123 n microscopy that purified monoubiquitinated FANCI:FANCD2 forms filament-like arrays on long dsDNA.
124               Simultaneously, FANCD2-but not FANCI-plays a major role in HDR-mediated replication res
125 E motif, that is critical for the ability of FANCI to properly monoubiquitinate FANCD2 and promote DN
126 in vitro to study functional consequences of FANCI:FANCD2 monoubiquitination.
127 o eradicable, and RNAi-mediated depletion of FANCI confirmed it as a potential target.
128             Recombination acts downstream of FANCI-FANCD2, yet RAD51 binds ICL-stalled replication fo
129 ly, removing key endonucleases downstream of FANCI/FANCD2, increasing ICL levels, or allowing damaged
130  ubiquitin molecule is conjugated to each of FANCI and FANCD2.
131 pressed in insect cells, a small fraction of FANCI forms a stable complex with FANCD2 (Fanconi anemia
132  highlights common and distinct functions of FANCI and FANCD2 during mouse development, meiotic recom
133 L-stalled replication forks independently of FANCI-FANCD2 and before DSB formation.
134 hat, although proper nuclear localization of FANCI is crucial for robust FANCD2 monoubiquitination, t
135     The 7.8 angstrom electron-density map of FANCI-DNA crystals and in vitro data show that each prot
136           Like FANCD2, monoubiquitination of FANCI requires the FA core complex.
137 significantly precedes monoubiquitination of FANCI; moreover, monoubiquitination responses of FANCD2
138                     Furthermore, mutation of FANCI in combination with mutations in a second ICL repa
139                       An increased number of FANCI foci form and become resistant to Triton X extract
140 hway activation relies on phosphorylation of FANCI by the ataxia telangiectasia and Rad3-related (ATR
141                   Although the C terminus of FANCI is dispensable for direct DNA binding, it seems to
142 on of chromatin-bound FANCD2 exceeds that of FANCI throughout replication.
143                       Mono-ubiquitination of FANCI-FANCD2 by the FA core complex promotes its mitotic
144 ting chromatin prior to-and independently of-FANCI.
145 nuclear speckles in a manner that depends on FANCI and on the activity of the checkpoint kinase ATR.
146 2 sequence of UAF1 or mutation of the SIM on FANCI disrupts UAF1/FANCI binding and inhibits FANCD2 de
147  SUMO-like domain-interacting motif (SIM) on FANCI.
148  USP1-UAF1, unless further ubiquitination on FANCI occurs.
149 r pathway that does not require incisions or FANCI-FANCD2.
150 . now demonstrate that FANCD2 has a paralog, FANCI.
151 uitination of FANCD2 and its binding partner FANCI.
152  the Fanconi anemia (FA) DNA repair pathway, FANCI, as a key effector of dormant origin firing in res
153                                A phosphodead FANCI mutant fails to dissociate from FANCD2, whereas ph
154 ssociate from FANCD2, whereas phosphomimetic FANCI cannot interact with FANCD2, indicating that FANCI
155         While FANCD2 ubiquitination precedes FANCI ubiquitination, FANCD2 is also deubiquitinated at
156 ere, we provide evidence that the FA protein FANCI also functions in ribosome biogenesis, the process
157              Here we describe the FA protein FANCI, identified as an ATM/ATR kinase substrate require
158 nd crosslinks (ICLs), the ICL-repair protein FANCI heterodimerizes with FANCD2 to initiate ICL excisi
159  of either FANCD2 or another key FA protein, FANCI.
160 n monoubiquitination of FA effector proteins FANCI and FANCD2 (FANCI-D2) and required the viral DNA p
161 epair pathway, the tumor suppressor proteins FANCI and FANCD2 (the ID complex), are SUMOylated in res
162       The ID complex, involving the proteins FANCI and FANCD2, is required for the repair of DNA inte
163 ubiquitination of 2 interacting FA proteins, FANCI and FANCD2.
164                   Intriguingly, the purified FANCI-FANCD2 complex preferentially binds to the branche
165 bust FANCD2 monoubiquitination, the putative FANCI EDGE motif is important for DNA crosslink repair.
166 istent with a role in meiotic recombination, FANCI interacted with RAD51 and stimulated D-loop format
167 TR (ataxia telangiectasia and Rad3-related), FANCI, and FANCD2.
168                                   Similarly, FANCI's target lysine (K523) is also primed for ubiquiti
169 protein interactions, but instead stabilizes FANCI:FANCD2 heterodimers on dsDNA.
170 n the absence of FANCD2, DNA also stimulates FANCI monoubiquitination, but in a FANCL-independent man
171 s also deubiquitinated at a faster rate than FANCI, which can result in a FANCI-ubiquitinated ID2 com
172                     We also demonstrate that FANCI can be ubiquitinated on Lys-523 by the UBE2T-FANCL
173                     We also demonstrate that FANCI forms discrete nuclear foci in HeLa cells in the a
174                                We found that FANCI alternatively interacts with a pro-apoptotic facto
175 tation with purified proteins indicates that FANCI interacts with FANCD2 through its C-terminal amino
176 cannot interact with FANCD2, indicating that FANCI phosphorylation is the molecular trigger for FANCD
177                              We propose that FANCI and FANCD2 have partially non-overlapping and poss
178 ir of CRISPR-Cas9-induced DSBs revealed that FANCI promotes single nucleotide insertions and reduces
179                                 We show that FANCI and FANCD2 are partially independent regarding the
180                            Here we show that FANCI and FANCD2 associate with splicing factor 3B1 (SF3
181                                 We show that FANCI and its C-terminal fragment possess a DNA binding
182 ng super-resolution microscopy, we show that FANCI co-localizes with MCM-bound chromatin in response
183                                 We show that FANCI localizes to the nucleolus and is functionally and
184     Using a cell-free system, we showed that FANCI-FANCD2 is required for replication-coupled ICL rep
185                                          The FANCI foci are colocalized perfectly with FANCD2 and par
186                                          The FANCI protein associates with FANCD2 and, together, as t
187 associates with FANCD2 and, together, as the FANCI-FANCD2 (ID) complex, localize to chromatin in resp
188          At the heart of this pathway is the FANCI-FAND2 (ID) complex, which, upon ubiquitination by
189                 Furthermore, addition of the FANCI protein enhances monoubiquitination and also restr
190 his pathway is the monoubiquitination of the FANCI-FANCD2 (ID) complex by the multiprotein "core comp
191 ty responsible for monoubiquitination of the FANCI-FANCD2 (ID) complex, which in turn initiates a cas
192                 Di-monoubiquitination of the FANCI-FANCD2 (ID2) complex is a central and crucial step
193 ia pathway is the mono-ubiquitylation of the FANCI-FANCD2 complex, but how this complex confers ICL r
194 onjugase is in the monoubiquitination of the FANCI-FANCD2 heterodimer, a central step in the Fanconi
195                    Our data suggest that the FANCI-FANCD2 complex may participate in repair of damage
196                                   Therefore, FANCI ubiquitination effectively maintains FANCD2 ubiqui
197 ain and monoubiquitin covalently attached to FANCI, and that this interaction shields monoubiquitinat
198 on forks collide with the lesion, leading to FANCI-FANCD2-dependent unhooking and formation of a doub
199 study, we report that the purified wild-type FANCI (Fanconi anemia complementation group I) protein d
200 r mutation of the SIM on FANCI disrupts UAF1/FANCI binding and inhibits FANCD2 deubiquitination and D
201 rsal of these defects requires ubiquitylated FANCI-FANCD2.
202  cleavage is prevented, unhooking occurs via FANCI-FANCD2-dependent incisions.
203 ts respective partner, it is unclear whether FANCI has any additional domains that may be important i
204                                        While FANCI is known to be monoubiquitinated when activated fo
205 dress the clinical phenotype associated with FANCI and the epistatic relationship with FANCD2, we cre
206  CUE domain is required for interaction with FANCI, retention of monoubiquitinated FANCD2, and FANCI

 
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