Ignet

Gene Information

Gene symbol: PCBD2

Gene name:

HGNC ID:

Related Genes

#	Gene Symbol	Number of hits
1	HNF1A	1 hits
2	PCBD1	1 hits

Related Sentences

#	PMID	Sentence
1	15182178	Biochemical and structural basis for partially redundant enzymatic and transcriptional functions of DCoH and DCoH2.
2	15182178	Transcription by HNF1alpha is stimulated by the bifunctional coactivator DCoH (dimerization cofactor of HNF1).
3	15182178	Strikingly, an HNF1alpha deletion in mice causes more severe phenotypes than a DCoH deletion.
4	15182178	It has been hypothesized that a DCoH homolog, DCoH2, partially complements the DCoH deletion.
5	15182178	Like DCoH, DCoH2 forms a tetramer, displays pterin-4alpha-carbinolamine dehydratase activity, and binds HNF1alpha in vivo and in vitro.
6	15182178	DCoH and DCoH2 adopt identical folds with structural differences confined largely to the protein surfaces and the tetramer interface.
7	15182178	In contrast to the hyperstable DCoH tetramer, DCoH2 readily disproportionates and forms a 2:2 complex with HNF1 in vitro.
8	15182178	Phylogenetic analysis reveals six major subfamilies of DCoH proteins, including unique DCoH and DCoH2 branches in metazoans.
9	15182178	These results suggest distinct roles for DCoH and DCoH2.
10	15182178	We propose that HNF1alpha binding kinetics may distinguish regulation by DCoH2, under thermodynamic control, from regulation by DCoH, under kinetic control.
11	15182178	Biochemical and structural basis for partially redundant enzymatic and transcriptional functions of DCoH and DCoH2.
12	15182178	Transcription by HNF1alpha is stimulated by the bifunctional coactivator DCoH (dimerization cofactor of HNF1).
13	15182178	Strikingly, an HNF1alpha deletion in mice causes more severe phenotypes than a DCoH deletion.
14	15182178	It has been hypothesized that a DCoH homolog, DCoH2, partially complements the DCoH deletion.
15	15182178	Like DCoH, DCoH2 forms a tetramer, displays pterin-4alpha-carbinolamine dehydratase activity, and binds HNF1alpha in vivo and in vitro.
16	15182178	DCoH and DCoH2 adopt identical folds with structural differences confined largely to the protein surfaces and the tetramer interface.
17	15182178	In contrast to the hyperstable DCoH tetramer, DCoH2 readily disproportionates and forms a 2:2 complex with HNF1 in vitro.
18	15182178	Phylogenetic analysis reveals six major subfamilies of DCoH proteins, including unique DCoH and DCoH2 branches in metazoans.
19	15182178	These results suggest distinct roles for DCoH and DCoH2.
20	15182178	We propose that HNF1alpha binding kinetics may distinguish regulation by DCoH2, under thermodynamic control, from regulation by DCoH, under kinetic control.
21	15182178	Biochemical and structural basis for partially redundant enzymatic and transcriptional functions of DCoH and DCoH2.
22	15182178	Transcription by HNF1alpha is stimulated by the bifunctional coactivator DCoH (dimerization cofactor of HNF1).
23	15182178	Strikingly, an HNF1alpha deletion in mice causes more severe phenotypes than a DCoH deletion.
24	15182178	It has been hypothesized that a DCoH homolog, DCoH2, partially complements the DCoH deletion.
25	15182178	Like DCoH, DCoH2 forms a tetramer, displays pterin-4alpha-carbinolamine dehydratase activity, and binds HNF1alpha in vivo and in vitro.
26	15182178	DCoH and DCoH2 adopt identical folds with structural differences confined largely to the protein surfaces and the tetramer interface.
27	15182178	In contrast to the hyperstable DCoH tetramer, DCoH2 readily disproportionates and forms a 2:2 complex with HNF1 in vitro.
28	15182178	Phylogenetic analysis reveals six major subfamilies of DCoH proteins, including unique DCoH and DCoH2 branches in metazoans.
29	15182178	These results suggest distinct roles for DCoH and DCoH2.
30	15182178	We propose that HNF1alpha binding kinetics may distinguish regulation by DCoH2, under thermodynamic control, from regulation by DCoH, under kinetic control.
31	15182178	Biochemical and structural basis for partially redundant enzymatic and transcriptional functions of DCoH and DCoH2.
32	15182178	Transcription by HNF1alpha is stimulated by the bifunctional coactivator DCoH (dimerization cofactor of HNF1).
33	15182178	Strikingly, an HNF1alpha deletion in mice causes more severe phenotypes than a DCoH deletion.
34	15182178	It has been hypothesized that a DCoH homolog, DCoH2, partially complements the DCoH deletion.
35	15182178	Like DCoH, DCoH2 forms a tetramer, displays pterin-4alpha-carbinolamine dehydratase activity, and binds HNF1alpha in vivo and in vitro.
36	15182178	DCoH and DCoH2 adopt identical folds with structural differences confined largely to the protein surfaces and the tetramer interface.
37	15182178	In contrast to the hyperstable DCoH tetramer, DCoH2 readily disproportionates and forms a 2:2 complex with HNF1 in vitro.
38	15182178	Phylogenetic analysis reveals six major subfamilies of DCoH proteins, including unique DCoH and DCoH2 branches in metazoans.
39	15182178	These results suggest distinct roles for DCoH and DCoH2.
40	15182178	We propose that HNF1alpha binding kinetics may distinguish regulation by DCoH2, under thermodynamic control, from regulation by DCoH, under kinetic control.
41	15182178	Biochemical and structural basis for partially redundant enzymatic and transcriptional functions of DCoH and DCoH2.
42	15182178	Transcription by HNF1alpha is stimulated by the bifunctional coactivator DCoH (dimerization cofactor of HNF1).
43	15182178	Strikingly, an HNF1alpha deletion in mice causes more severe phenotypes than a DCoH deletion.
44	15182178	It has been hypothesized that a DCoH homolog, DCoH2, partially complements the DCoH deletion.
45	15182178	Like DCoH, DCoH2 forms a tetramer, displays pterin-4alpha-carbinolamine dehydratase activity, and binds HNF1alpha in vivo and in vitro.
46	15182178	DCoH and DCoH2 adopt identical folds with structural differences confined largely to the protein surfaces and the tetramer interface.
47	15182178	In contrast to the hyperstable DCoH tetramer, DCoH2 readily disproportionates and forms a 2:2 complex with HNF1 in vitro.
48	15182178	Phylogenetic analysis reveals six major subfamilies of DCoH proteins, including unique DCoH and DCoH2 branches in metazoans.
49	15182178	These results suggest distinct roles for DCoH and DCoH2.
50	15182178	We propose that HNF1alpha binding kinetics may distinguish regulation by DCoH2, under thermodynamic control, from regulation by DCoH, under kinetic control.
51	15182178	Biochemical and structural basis for partially redundant enzymatic and transcriptional functions of DCoH and DCoH2.
52	15182178	Transcription by HNF1alpha is stimulated by the bifunctional coactivator DCoH (dimerization cofactor of HNF1).
53	15182178	Strikingly, an HNF1alpha deletion in mice causes more severe phenotypes than a DCoH deletion.
54	15182178	It has been hypothesized that a DCoH homolog, DCoH2, partially complements the DCoH deletion.
55	15182178	Like DCoH, DCoH2 forms a tetramer, displays pterin-4alpha-carbinolamine dehydratase activity, and binds HNF1alpha in vivo and in vitro.
56	15182178	DCoH and DCoH2 adopt identical folds with structural differences confined largely to the protein surfaces and the tetramer interface.
57	15182178	In contrast to the hyperstable DCoH tetramer, DCoH2 readily disproportionates and forms a 2:2 complex with HNF1 in vitro.
58	15182178	Phylogenetic analysis reveals six major subfamilies of DCoH proteins, including unique DCoH and DCoH2 branches in metazoans.
59	15182178	These results suggest distinct roles for DCoH and DCoH2.
60	15182178	We propose that HNF1alpha binding kinetics may distinguish regulation by DCoH2, under thermodynamic control, from regulation by DCoH, under kinetic control.
61	15182178	Biochemical and structural basis for partially redundant enzymatic and transcriptional functions of DCoH and DCoH2.
62	15182178	Transcription by HNF1alpha is stimulated by the bifunctional coactivator DCoH (dimerization cofactor of HNF1).
63	15182178	Strikingly, an HNF1alpha deletion in mice causes more severe phenotypes than a DCoH deletion.
64	15182178	It has been hypothesized that a DCoH homolog, DCoH2, partially complements the DCoH deletion.
65	15182178	Like DCoH, DCoH2 forms a tetramer, displays pterin-4alpha-carbinolamine dehydratase activity, and binds HNF1alpha in vivo and in vitro.
66	15182178	DCoH and DCoH2 adopt identical folds with structural differences confined largely to the protein surfaces and the tetramer interface.
67	15182178	In contrast to the hyperstable DCoH tetramer, DCoH2 readily disproportionates and forms a 2:2 complex with HNF1 in vitro.
68	15182178	Phylogenetic analysis reveals six major subfamilies of DCoH proteins, including unique DCoH and DCoH2 branches in metazoans.
69	15182178	These results suggest distinct roles for DCoH and DCoH2.
70	15182178	We propose that HNF1alpha binding kinetics may distinguish regulation by DCoH2, under thermodynamic control, from regulation by DCoH, under kinetic control.