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1  with autologous dendritic cells pulsed with Id protein.
2 : muscle regulatory factors, E proteins, and Id proteins.
3 y another class of HLH proteins known as the Id proteins.
4  dependency on the unlimited availability of Id proteins.
5 el transcriptional activity of the mammalian Id proteins.
6 eins MyoD and E12, and not at all with other Id proteins.
7 ele, leading to an overall reduced dosage of Id proteins.
8 n emphasis on the known requirements for the ID proteins.
9 sarcomas coordinately overexpressed USP1 and ID proteins.
10 ergistic activity of Gata4 and Nkx2.5 by the Id proteins.
11  characteristic of intrinsically disordered (ID) proteins.
12                                              Id proteins act as negative regulators of bHLH transcrip
13                               E proteins and Id proteins also function to inhibit or promote cell pro
14 dimer partners-the Inhibitor of DNA-binding (ID) proteins-also exists.
15  proliferation and enhanced the secretion of Id protein and cytokines by myeloma cells.
16 dritic cells (DCs) pulsed with tumor-derived Id protein and now report on 35 patients treated using t
17  indicating that myeloma cells could process Id protein and present Id peptides in the context of the
18   Myozap is a recent addition to the list of ID proteins and has been implicated in serum-response fa
19 he G1 progression and apoptosis functions of Id proteins and hint at a common mechanism for this fami
20  those in the corresponding positions of the Id proteins and MyoD.
21 /2 (Id-1/2) by catalyzing phosphorylation of Id proteins and recruiting TRAF-6.
22  responses, suggesting a mechanism involving Id protein- and E protein-mediated survival and differen
23 atio of E-box transcription factors to their Id protein antagonists.
24                                              Id proteins antagonize basic helix-loop-helix proteins,
25                                              Id proteins are a class of dominant-negative antagonists
26                                          The Id proteins are a family of related mammalian helix-loop
27                                              Id proteins are believed to block expression of muscle-s
28                                              Id proteins are dominant negative regulators of basic he
29                                   Therefore, Id proteins are good candidates for regulating Math1 in
30                                              Id proteins are helix-loop-helix (HLH) transcriptional f
31                                              Id proteins are helix-loop-helix transcription factors t
32                                              Id proteins are inhibitors of basic helix-loop-helix tra
33                                              Id proteins are known negative regulators of E-box prote
34                                              Id proteins are known to play important roles in the pro
35                                              ID proteins are master regulators of stemness and anchor
36                                              Id proteins are negative regulators of basic helix-loop-
37 ng near a specific set of 170 genes encoding ID proteins are significantly enriched for association w
38        The helix-loop-helix (HLH)-containing Id proteins are trans-acting negative regulators of DNA
39                           The E proteins and Id proteins are, respectively, the positive and negative
40 hibitors of differentiation and DNA binding (Id) proteins are known to negatively regulate many bHLH
41 es encoding cardiomyocyte intercalated disc (ID) proteins are more enriched for associations with QT
42                    Inhibitor of DNA binding (ID) proteins are transcriptional targets of TGF-beta1 an
43                        This study identifies Id proteins as negative regulators of T cell specificati
44 , including modulation of DNA binding by the Id proteins, association with the transcriptional modula
45 th adaptive and innate-like requirements for ID proteins at distinct checkpoints during iNKT cell dev
46 en receptor and/or cytokine signaling, the E-Id protein axis modulates the activities of the PI3K-AKT
47    It is now well established that the E and Id protein axis regulates multiple steps in lymphocyte d
48 previous observations, we propose that the E-Id protein axis specifies innate and adaptive lymphoid c
49                                              Id proteins belong to a class of nuclear transcription f
50                                          The Id proteins belong to a family of nuclear HLH proteins l
51                                              Id proteins bind basic helix-loop-helix transcription fa
52                    Inhibitor of DNA binding (Id) proteins bind to and inhibit the function of basic h
53                    In addition, the OLIG and ID proteins both interacted with the E2A proteins E12 an
54 ctivities of E proteins and their antagonist Id proteins, but how these factors regulate early T cell
55           Induction of phospho-Smad1/5/8 and Id protein by BMP4 was also reduced in female hPASMCs.
56 s effector RBPSuh (CSL), GATA-3, E2A/HEB and Id proteins, c-Myb, TCF-1, and members of the Runx, Ets,
57 NA-binding domain, all four of the mammalian Id proteins can activate GAL4-dependent transcription.
58                                              Id proteins can also act as positive regulators of cell
59 ants and in vivo overexpression to show that Id proteins can differentially inhibit the activities of
60 mechanism by which autophagic degradation of Id proteins can regulate cell differentiation.
61    Inhibitor of differentiation/DNA binding (Id) proteins comprise a class of helix-loop-helix transc
62                                          TCR Id protein conjugated to keyhole limpet hemocyanin (KLH)
63 insight into the mechanisms by which E2A and Id proteins control cell growth.
64 n factors and their negative regulators, the Id proteins, control the development of iNKT sublineages
65 E proteins and their natural inhibitors, the Id proteins, control the timing of differentiation and t
66                                              Id proteins coordinate cell growth and differentiation p
67                          In mammalian cells, Id proteins coordinate proliferation and differentiation
68                      The presence of several Id proteins could reflect simple redundancy in function,
69 suggest that pharmacological inactivation of ID proteins could serve as a therapeutic strategy.
70               Our results demonstrate a new, Id protein-dependent, molecular mechanism of Notch1 repr
71 knockdown in osteosarcoma cells precipitated ID protein destabilization, cell-cycle arrest, and osteo
72 nisms that control the balance between E and Id proteins during DC subset specification remain unknow
73 insight into the dynamic regulation of E and Id proteins during this process.
74 of lineage-specific transcription factors by Id proteins enables the self-renewal response to LIF/STA
75  rate (FDR) of 5%, we had identified 28 such ID protein-encoding genes.
76  in myoblasts (a) decreased the level of the Id proteins, even in a culture in growth medium, and (b)
77 on of tumor-specific Ags or patient-specific Id protein expression.
78 ins to activate them, with expression of the Id protein Extramacrochaetae (Emc), which antagonizes bH
79 ifier screen in Drosophila, we show that the Id protein Extramacrochaetae enables growth by suppressi
80  by members of the inhibitor of DNA binding (Id) protein family.
81                   Together, Cbfa1, p204, and Id proteins form a regulatory circuit and act in concert
82                              In contrast, an Id protein-FrC conjugate boosted both Id-specific and Fr
83  the depletion of CD4+ T cells converted the Id protein-FrC conjugate vaccine into an inhibitor.
84 sponses; yet, these were cross-reactive with Id proteins from other patient's tumors.
85 ific immune response detecting tumor-derived Id proteins from the original tumor and from all tumor v
86 unized 2 healthy human stem-cell donors with Id proteins from their recipients.
87                                              ID proteins function as antagonists of the E protein tra
88                                          The Id proteins function as dominant negative inhibitors of
89 d identifiers, such as UniProt, ChEBI and GO IDs, protein, gene and complex names or synonyms.
90                   Enforced overexpression of Id proteins has previously been shown to promote the cel
91 ese studies show that the entire ensemble of Id proteins has the ability to interact with E47, identi
92 esults are consistent with the idea that the Id proteins have a transcriptional activity when present
93 s a "hot spot" for heart disease, as several ID proteins have been found mutated in cardiomyopathy.
94        As negative regulators of E proteins, Id proteins have been implicated in lymphocyte developme
95                                          The Id proteins have been reported generally to function as
96 bers of the helix-loop-helix (HLH) family of Id proteins have demonstrated roles in the regulation of
97                                              ID-proteins have been implicated in the control of diffe
98 oteins and their functional antagonists, the ID proteins, have significant roles in normal hematopoie
99  in clinical studies of Id vaccination using Id proteins.However, Id protein is laborious and time-co
100                                              Id proteins (Id1 to Id4) are helix-loop-helix transcript
101                        Dimerization of three Id proteins (Id1, Id2, and Id3) with the four class A E
102 tivities of the MyoD and E47 proteins by the Id proteins: Id1, Id2, and Id3.
103                  Consistent with the role of Id proteins, Id2 prevents activation of p57Kip2 expressi
104  consequence of (i) binding and sequestering Id proteins, (ii) accelerating their ubiquitination and
105 quamous cell carcinoma of the head and neck, Id protein immunoreactivity was observed in the majority
106 nd in knockout mice implicate E proteins and ID proteins in a wide variety of diseases, belying the n
107                         The participation of Id proteins in advanced human malignancy, where they are
108 ht to determine the functional role of these Id proteins in BMP-induced osteoblast differentiation.
109             p204 overcame this inhibition by Id proteins in consequence of (i) binding and sequesteri
110   We found that lentiviral overexpression of ID proteins in cord blood HSCs biases myeloerythroid com
111                  The divergent regulation of Id proteins in distinct hypoxic cells may explain some o
112  steroid hormone receptors in particular and ID proteins in general can have multiple functionally di
113 e discuss the function and regulation of the Id proteins in lymphocyte development.
114 training factor of the oncogenic activity of Id proteins in neural tumors.
115                 Depletion of Cdh1 stabilizes Id proteins in neurons, whereas Id2 D-box mutants are im
116 s directly interact with previously reported ID proteins in six known pathways essential for cognitiv
117 stem cells is the constitutive expression of ID proteins in the former and inducible expression in th
118 oteasomes, and (iii) decreasing the level of Id proteins in the nucleus by increasing their transloca
119                       (ii) p204 bound to the Id proteins in vitro and in vivo.
120 which bind to the helix-loop-helix domain of Id proteins in vitro and in vivo.
121 tablished that inhibitor of differentiation (Id) proteins, including Id1, Id2, and Id3, associate wit
122                    Inhibitor of DNA binding (Id) proteins, including Id1-4, are transcriptional regul
123                                              Id proteins inhibit differentiation by HLH-mediated hete
124 ous or ectopic inhibitor of differentiation (Id) proteins inhibited the differentiation of P19 cells
125 ression in mesenchymal stem cells stabilized ID proteins, inhibited osteoblastic differentiation, and
126 of Id vaccination using Id proteins.However, Id protein is laborious and time-consuming to produce.
127 ion of the Id-specific memory B cells by the Id protein is largely independent of the FcgammaRIIB and
128                     Although upregulation of Id proteins is associated with a broad spectrum of tumor
129  hypoxic, but it is unknown if expression of Id proteins is regulated in hypoxic cells.
130  transcription factors and their inhibitors, Id proteins, is important for the myeloid-versus-lymphoi
131                          Expression of other ID proteins like N-cadherin, desmoplakin, connexin-43, a
132 s and suggest that deregulated expression of Id proteins may be an epigenetic mechanism to silence ex
133                                              Id proteins may control cell differentiation by interfer
134 on of protein-protein interactions involving ID proteins may therefore be possible through the target
135        However, it remains unknown how E and Id proteins mechanistically enforce and maintain the nai
136 ture and myelinating oligodendrocytes via an ID protein-mediated negative regulation and may serve as
137                              DCs pulsed with Id proteins modified to include foreign constant regions
138                       Users may query by PDB ID, protein name, function and Enzyme Classification num
139 s queries based on contributing site, target ID, protein name, sequence, status and other data.
140 at E47 interacts with the entire ensemble of Id proteins, namely, Id1, Id2, Id3, and Id4.
141                                              Id proteins negatively regulate the dimerization, DNA bi
142                                              Id protein not only failed to boost the response, but pe
143 dium, and (b) overcame the inhibition by the Id proteins of MyoD- and E47 dependent transcription and
144 ition of p204 overcame the inhibition by the Id proteins of the binding of MyoD and E47 to DNA in vit
145 ulated that demonstrates dominant effects of Id proteins on different aspects of cellular growth.
146                    Of the four characterized Id proteins, only Id2 is found in the nucleus of Sertoli
147              Since the identification of the Id proteins over a decade ago, a great many cell cycle a
148 uctural features underlying the functions of ID proteins/peptides by conventional methods, such as X-
149                    Intrinsically disordered (ID) proteins/peptides are considered equally important f
150                                        Thus, Id proteins play a central and evolutionarily conserved
151                We hypothesized that BMP4 and Id proteins play a role in the expansion and differentia
152                                          The Id proteins play an important role in proliferation, dif
153                                          The Id proteins play an important role in proliferation, dif
154                                              Id proteins play important roles in osteogenic different
155                    Inhibitor of DNA binding (Id) proteins play important roles in regulating cardiac
156 iption factors and their natural inhibitors, Id proteins, play critical and complex roles during lymp
157                               However, which Id protein plays a physiologic role during lymphocyte de
158          Thus, we provide insight into E and Id protein regulation of iNKT cell proliferation and dif
159                                    Idiotype (Id) protein, secreted by myeloma cells, is a tumor-speci
160 how the folding of intrinsically disordered (ID) protein sequences, in particular, and population shi
161                                     Although Id-protein-specific T-cell responses have been reported
162                             Mechanistically, Id proteins specify cardiac cell fate by repressing two
163 at the deubiquitinating enzyme USP1 promotes ID protein stability and stem cell-like characteristics
164 eterodimers in a manner similar to MISTI and Id proteins, suggesting a possible transcriptional inhib
165 an inhibitor of differentiation/DNA binding (Id) proteins that comprise a class of helix-loop-helix f
166                                              Id proteins, the inhibitors of E2A, have opposite effect
167 plained experimental observations related to Id proteins; the speed of response varies with the initi
168                                          The Id proteins thus display a signature range of interactio
169 , we explore relationships of E proteins and ID proteins to a variety of disease processes and highli
170 ese activities are related to the ability of Id proteins to antagonize E proteins and other transcrip
171 on can be functionally replaced by fusion of Id proteins to SAP-1, whereby the Id moiety then acts to
172 apitulate those physiologically propelled by Id proteins to support normal development.
173 y expressed E2A or inhibitor of DNA binding (Id) proteins to activate or inhibit transcription, respe
174 pression levels of Inhibitor of DNA binding (ID) proteins to ask whether lineage priming affects self
175 ation affects the inhibitory activity of the Id proteins towards the TCFs.
176 e demonstrated a potent inhibitory effect of ID proteins upon CLOCK-BMAL1 transactivation of clock ge
177                                              Id protein vaccination has demonstrated clinical activit
178 s equivalent or superior to that afforded by Id protein vaccination.
179 ection than a traditional lymphoma idiotype (Id) protein vaccine, and in combination with chemotherap
180 al antibody, whereas the response to soluble Id protein was dependent on MHC class II.
181                                  Recombinant Id protein was manufactured and covalently linked with k
182 s expressed in T-BET(+) NKT1 cells, and both Id proteins were required for the formation of this subl
183                                     All four ID proteins were significantly increased in Mecp2-defici
184 ther ILCs, iNKT cells constitutively express ID proteins, which antagonize the E protein transcriptio
185      Studies involving ectopic expression of Id proteins, which inhibit E2A as well as other basic he
186                            Overexpression of Id proteins within a variety of cell types has been show

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