Ignet

Gene Information

Gene symbol: PCBD1

Gene name: pterin-4 alpha-carbinolamine dehydratase/dimerization cofactor of hepatocyte nuclear factor 1 alpha

HGNC ID: 8646

Synonyms: PCD

Related Genes

#	Gene Symbol	Number of hits
1	HNF1A	1 hits
2	HNF1B	1 hits
3	HNF4A	1 hits
4	PCBD2	1 hits
5	SLC3A1	1 hits

Related Sentences

#	PMID	Sentence
1	11668623	Studies of the variability of the hepatocyte nuclear factor-1beta (HNF-1beta / TCF2) and the dimerization cofactor of HNF-1 (DcoH / PCBD) genes in relation to type 2 diabetes mellitus and beta-cell function.
2	11668623	To investigate whether mutations in HNF-1 are implicated in the pathogenesis of MODY or late-onset diabetes with and without nephropathy in Danish Caucasians we examined the HNF-1beta (TCF2) and the dimerization cofactor of HNF-1 (DCoH, PCBD) genes for mutations in 11 MODY probands, 28 type 2 diabetic patients with nephropathy, and 46 type 2 diabetic patients with an impaired beta-cell function by combined single-strand conformation polymorphism (SSCP) and heteroduplex analysis.
3	11668623	In conclusion, mutations in HNF-1beta and DCoH are not a major cause of MODY or late onset type 2 diabetes in Danish Caucasian subjects.
4	11668623	Studies of the variability of the hepatocyte nuclear factor-1beta (HNF-1beta / TCF2) and the dimerization cofactor of HNF-1 (DcoH / PCBD) genes in relation to type 2 diabetes mellitus and beta-cell function.
5	11668623	To investigate whether mutations in HNF-1 are implicated in the pathogenesis of MODY or late-onset diabetes with and without nephropathy in Danish Caucasians we examined the HNF-1beta (TCF2) and the dimerization cofactor of HNF-1 (DCoH, PCBD) genes for mutations in 11 MODY probands, 28 type 2 diabetic patients with nephropathy, and 46 type 2 diabetic patients with an impaired beta-cell function by combined single-strand conformation polymorphism (SSCP) and heteroduplex analysis.
6	11668623	In conclusion, mutations in HNF-1beta and DCoH are not a major cause of MODY or late onset type 2 diabetes in Danish Caucasian subjects.
7	11668623	Studies of the variability of the hepatocyte nuclear factor-1beta (HNF-1beta / TCF2) and the dimerization cofactor of HNF-1 (DcoH / PCBD) genes in relation to type 2 diabetes mellitus and beta-cell function.
8	11668623	To investigate whether mutations in HNF-1 are implicated in the pathogenesis of MODY or late-onset diabetes with and without nephropathy in Danish Caucasians we examined the HNF-1beta (TCF2) and the dimerization cofactor of HNF-1 (DCoH, PCBD) genes for mutations in 11 MODY probands, 28 type 2 diabetic patients with nephropathy, and 46 type 2 diabetic patients with an impaired beta-cell function by combined single-strand conformation polymorphism (SSCP) and heteroduplex analysis.
9	11668623	In conclusion, mutations in HNF-1beta and DCoH are not a major cause of MODY or late onset type 2 diabetes in Danish Caucasian subjects.
10	12011081	The bifunctional protein DCoH (Dimerizing Cofactor for HNF1) acts as an enzyme in intermediary metabolism and as a binding partner of the HNF1 family of transcriptional activators.
11	12011081	DCoH acts as a cofactor for HNF1 that stabilizes the dimeric HNF1 complex.
12	12011081	Surprisingly, HNF1 function in DCoH null mice is only slightly impaired, and mice are mildly glucose-intolerant in contrast to HNF1alpha null mice, which are diabetic.
13	12011081	DCoH function as it pertains to HNF1 activity appears to be partially complemented by a newly identified homolog, DCoH2.
14	12011081	The bifunctional protein DCoH (Dimerizing Cofactor for HNF1) acts as an enzyme in intermediary metabolism and as a binding partner of the HNF1 family of transcriptional activators.
15	12011081	DCoH acts as a cofactor for HNF1 that stabilizes the dimeric HNF1 complex.
16	12011081	Surprisingly, HNF1 function in DCoH null mice is only slightly impaired, and mice are mildly glucose-intolerant in contrast to HNF1alpha null mice, which are diabetic.
17	12011081	DCoH function as it pertains to HNF1 activity appears to be partially complemented by a newly identified homolog, DCoH2.
18	12011081	The bifunctional protein DCoH (Dimerizing Cofactor for HNF1) acts as an enzyme in intermediary metabolism and as a binding partner of the HNF1 family of transcriptional activators.
19	12011081	DCoH acts as a cofactor for HNF1 that stabilizes the dimeric HNF1 complex.
20	12011081	Surprisingly, HNF1 function in DCoH null mice is only slightly impaired, and mice are mildly glucose-intolerant in contrast to HNF1alpha null mice, which are diabetic.
21	12011081	DCoH function as it pertains to HNF1 activity appears to be partially complemented by a newly identified homolog, DCoH2.
22	12011081	The bifunctional protein DCoH (Dimerizing Cofactor for HNF1) acts as an enzyme in intermediary metabolism and as a binding partner of the HNF1 family of transcriptional activators.
23	12011081	DCoH acts as a cofactor for HNF1 that stabilizes the dimeric HNF1 complex.
24	12011081	Surprisingly, HNF1 function in DCoH null mice is only slightly impaired, and mice are mildly glucose-intolerant in contrast to HNF1alpha null mice, which are diabetic.
25	12011081	DCoH function as it pertains to HNF1 activity appears to be partially complemented by a newly identified homolog, DCoH2.
26	12618086	Mutations in the HNF1-alpha gene cause maturity-onset diabetes of the young (MODY), but the exact mechanism is not known.
27	12618086	These were 92bp upstream of SLC3A1, 52bp upstream of PCBD (DCOH), and 42202bp upstream of TCF2(HNF1-beta).
28	15182178	Biochemical and structural basis for partially redundant enzymatic and transcriptional functions of DCoH and DCoH2.
29	15182178	Transcription by HNF1alpha is stimulated by the bifunctional coactivator DCoH (dimerization cofactor of HNF1).
30	15182178	Strikingly, an HNF1alpha deletion in mice causes more severe phenotypes than a DCoH deletion.
31	15182178	It has been hypothesized that a DCoH homolog, DCoH2, partially complements the DCoH deletion.
32	15182178	Like DCoH, DCoH2 forms a tetramer, displays pterin-4alpha-carbinolamine dehydratase activity, and binds HNF1alpha in vivo and in vitro.
33	15182178	DCoH and DCoH2 adopt identical folds with structural differences confined largely to the protein surfaces and the tetramer interface.
34	15182178	In contrast to the hyperstable DCoH tetramer, DCoH2 readily disproportionates and forms a 2:2 complex with HNF1 in vitro.
35	15182178	Phylogenetic analysis reveals six major subfamilies of DCoH proteins, including unique DCoH and DCoH2 branches in metazoans.
36	15182178	These results suggest distinct roles for DCoH and DCoH2.
37	15182178	We propose that HNF1alpha binding kinetics may distinguish regulation by DCoH2, under thermodynamic control, from regulation by DCoH, under kinetic control.
38	15182178	Biochemical and structural basis for partially redundant enzymatic and transcriptional functions of DCoH and DCoH2.
39	15182178	Transcription by HNF1alpha is stimulated by the bifunctional coactivator DCoH (dimerization cofactor of HNF1).
40	15182178	Strikingly, an HNF1alpha deletion in mice causes more severe phenotypes than a DCoH deletion.
41	15182178	It has been hypothesized that a DCoH homolog, DCoH2, partially complements the DCoH deletion.
42	15182178	Like DCoH, DCoH2 forms a tetramer, displays pterin-4alpha-carbinolamine dehydratase activity, and binds HNF1alpha in vivo and in vitro.
43	15182178	DCoH and DCoH2 adopt identical folds with structural differences confined largely to the protein surfaces and the tetramer interface.
44	15182178	In contrast to the hyperstable DCoH tetramer, DCoH2 readily disproportionates and forms a 2:2 complex with HNF1 in vitro.
45	15182178	Phylogenetic analysis reveals six major subfamilies of DCoH proteins, including unique DCoH and DCoH2 branches in metazoans.
46	15182178	These results suggest distinct roles for DCoH and DCoH2.
47	15182178	We propose that HNF1alpha binding kinetics may distinguish regulation by DCoH2, under thermodynamic control, from regulation by DCoH, under kinetic control.
48	15182178	Biochemical and structural basis for partially redundant enzymatic and transcriptional functions of DCoH and DCoH2.
49	15182178	Transcription by HNF1alpha is stimulated by the bifunctional coactivator DCoH (dimerization cofactor of HNF1).
50	15182178	Strikingly, an HNF1alpha deletion in mice causes more severe phenotypes than a DCoH deletion.
51	15182178	It has been hypothesized that a DCoH homolog, DCoH2, partially complements the DCoH deletion.
52	15182178	Like DCoH, DCoH2 forms a tetramer, displays pterin-4alpha-carbinolamine dehydratase activity, and binds HNF1alpha in vivo and in vitro.
53	15182178	DCoH and DCoH2 adopt identical folds with structural differences confined largely to the protein surfaces and the tetramer interface.
54	15182178	In contrast to the hyperstable DCoH tetramer, DCoH2 readily disproportionates and forms a 2:2 complex with HNF1 in vitro.
55	15182178	Phylogenetic analysis reveals six major subfamilies of DCoH proteins, including unique DCoH and DCoH2 branches in metazoans.
56	15182178	These results suggest distinct roles for DCoH and DCoH2.
57	15182178	We propose that HNF1alpha binding kinetics may distinguish regulation by DCoH2, under thermodynamic control, from regulation by DCoH, under kinetic control.
58	15182178	Biochemical and structural basis for partially redundant enzymatic and transcriptional functions of DCoH and DCoH2.
59	15182178	Transcription by HNF1alpha is stimulated by the bifunctional coactivator DCoH (dimerization cofactor of HNF1).
60	15182178	Strikingly, an HNF1alpha deletion in mice causes more severe phenotypes than a DCoH deletion.
61	15182178	It has been hypothesized that a DCoH homolog, DCoH2, partially complements the DCoH deletion.
62	15182178	Like DCoH, DCoH2 forms a tetramer, displays pterin-4alpha-carbinolamine dehydratase activity, and binds HNF1alpha in vivo and in vitro.
63	15182178	DCoH and DCoH2 adopt identical folds with structural differences confined largely to the protein surfaces and the tetramer interface.
64	15182178	In contrast to the hyperstable DCoH tetramer, DCoH2 readily disproportionates and forms a 2:2 complex with HNF1 in vitro.
65	15182178	Phylogenetic analysis reveals six major subfamilies of DCoH proteins, including unique DCoH and DCoH2 branches in metazoans.
66	15182178	These results suggest distinct roles for DCoH and DCoH2.
67	15182178	We propose that HNF1alpha binding kinetics may distinguish regulation by DCoH2, under thermodynamic control, from regulation by DCoH, under kinetic control.
68	15182178	Biochemical and structural basis for partially redundant enzymatic and transcriptional functions of DCoH and DCoH2.
69	15182178	Transcription by HNF1alpha is stimulated by the bifunctional coactivator DCoH (dimerization cofactor of HNF1).
70	15182178	Strikingly, an HNF1alpha deletion in mice causes more severe phenotypes than a DCoH deletion.
71	15182178	It has been hypothesized that a DCoH homolog, DCoH2, partially complements the DCoH deletion.
72	15182178	Like DCoH, DCoH2 forms a tetramer, displays pterin-4alpha-carbinolamine dehydratase activity, and binds HNF1alpha in vivo and in vitro.
73	15182178	DCoH and DCoH2 adopt identical folds with structural differences confined largely to the protein surfaces and the tetramer interface.
74	15182178	In contrast to the hyperstable DCoH tetramer, DCoH2 readily disproportionates and forms a 2:2 complex with HNF1 in vitro.
75	15182178	Phylogenetic analysis reveals six major subfamilies of DCoH proteins, including unique DCoH and DCoH2 branches in metazoans.
76	15182178	These results suggest distinct roles for DCoH and DCoH2.
77	15182178	We propose that HNF1alpha binding kinetics may distinguish regulation by DCoH2, under thermodynamic control, from regulation by DCoH, under kinetic control.
78	15182178	Biochemical and structural basis for partially redundant enzymatic and transcriptional functions of DCoH and DCoH2.
79	15182178	Transcription by HNF1alpha is stimulated by the bifunctional coactivator DCoH (dimerization cofactor of HNF1).
80	15182178	Strikingly, an HNF1alpha deletion in mice causes more severe phenotypes than a DCoH deletion.
81	15182178	It has been hypothesized that a DCoH homolog, DCoH2, partially complements the DCoH deletion.
82	15182178	Like DCoH, DCoH2 forms a tetramer, displays pterin-4alpha-carbinolamine dehydratase activity, and binds HNF1alpha in vivo and in vitro.
83	15182178	DCoH and DCoH2 adopt identical folds with structural differences confined largely to the protein surfaces and the tetramer interface.
84	15182178	In contrast to the hyperstable DCoH tetramer, DCoH2 readily disproportionates and forms a 2:2 complex with HNF1 in vitro.
85	15182178	Phylogenetic analysis reveals six major subfamilies of DCoH proteins, including unique DCoH and DCoH2 branches in metazoans.
86	15182178	These results suggest distinct roles for DCoH and DCoH2.
87	15182178	We propose that HNF1alpha binding kinetics may distinguish regulation by DCoH2, under thermodynamic control, from regulation by DCoH, under kinetic control.
88	15182178	Biochemical and structural basis for partially redundant enzymatic and transcriptional functions of DCoH and DCoH2.
89	15182178	Transcription by HNF1alpha is stimulated by the bifunctional coactivator DCoH (dimerization cofactor of HNF1).
90	15182178	Strikingly, an HNF1alpha deletion in mice causes more severe phenotypes than a DCoH deletion.
91	15182178	It has been hypothesized that a DCoH homolog, DCoH2, partially complements the DCoH deletion.
92	15182178	Like DCoH, DCoH2 forms a tetramer, displays pterin-4alpha-carbinolamine dehydratase activity, and binds HNF1alpha in vivo and in vitro.
93	15182178	DCoH and DCoH2 adopt identical folds with structural differences confined largely to the protein surfaces and the tetramer interface.
94	15182178	In contrast to the hyperstable DCoH tetramer, DCoH2 readily disproportionates and forms a 2:2 complex with HNF1 in vitro.
95	15182178	Phylogenetic analysis reveals six major subfamilies of DCoH proteins, including unique DCoH and DCoH2 branches in metazoans.
96	15182178	These results suggest distinct roles for DCoH and DCoH2.
97	15182178	We propose that HNF1alpha binding kinetics may distinguish regulation by DCoH2, under thermodynamic control, from regulation by DCoH, under kinetic control.
98	15182178	Biochemical and structural basis for partially redundant enzymatic and transcriptional functions of DCoH and DCoH2.
99	15182178	Transcription by HNF1alpha is stimulated by the bifunctional coactivator DCoH (dimerization cofactor of HNF1).
100	15182178	Strikingly, an HNF1alpha deletion in mice causes more severe phenotypes than a DCoH deletion.
101	15182178	It has been hypothesized that a DCoH homolog, DCoH2, partially complements the DCoH deletion.
102	15182178	Like DCoH, DCoH2 forms a tetramer, displays pterin-4alpha-carbinolamine dehydratase activity, and binds HNF1alpha in vivo and in vitro.
103	15182178	DCoH and DCoH2 adopt identical folds with structural differences confined largely to the protein surfaces and the tetramer interface.
104	15182178	In contrast to the hyperstable DCoH tetramer, DCoH2 readily disproportionates and forms a 2:2 complex with HNF1 in vitro.
105	15182178	Phylogenetic analysis reveals six major subfamilies of DCoH proteins, including unique DCoH and DCoH2 branches in metazoans.
106	15182178	These results suggest distinct roles for DCoH and DCoH2.
107	15182178	We propose that HNF1alpha binding kinetics may distinguish regulation by DCoH2, under thermodynamic control, from regulation by DCoH, under kinetic control.
108	15182178	Biochemical and structural basis for partially redundant enzymatic and transcriptional functions of DCoH and DCoH2.
109	15182178	Transcription by HNF1alpha is stimulated by the bifunctional coactivator DCoH (dimerization cofactor of HNF1).
110	15182178	Strikingly, an HNF1alpha deletion in mice causes more severe phenotypes than a DCoH deletion.
111	15182178	It has been hypothesized that a DCoH homolog, DCoH2, partially complements the DCoH deletion.
112	15182178	Like DCoH, DCoH2 forms a tetramer, displays pterin-4alpha-carbinolamine dehydratase activity, and binds HNF1alpha in vivo and in vitro.
113	15182178	DCoH and DCoH2 adopt identical folds with structural differences confined largely to the protein surfaces and the tetramer interface.
114	15182178	In contrast to the hyperstable DCoH tetramer, DCoH2 readily disproportionates and forms a 2:2 complex with HNF1 in vitro.
115	15182178	Phylogenetic analysis reveals six major subfamilies of DCoH proteins, including unique DCoH and DCoH2 branches in metazoans.
116	15182178	These results suggest distinct roles for DCoH and DCoH2.
117	15182178	We propose that HNF1alpha binding kinetics may distinguish regulation by DCoH2, under thermodynamic control, from regulation by DCoH, under kinetic control.
118	15182178	Biochemical and structural basis for partially redundant enzymatic and transcriptional functions of DCoH and DCoH2.
119	15182178	Transcription by HNF1alpha is stimulated by the bifunctional coactivator DCoH (dimerization cofactor of HNF1).
120	15182178	Strikingly, an HNF1alpha deletion in mice causes more severe phenotypes than a DCoH deletion.
121	15182178	It has been hypothesized that a DCoH homolog, DCoH2, partially complements the DCoH deletion.
122	15182178	Like DCoH, DCoH2 forms a tetramer, displays pterin-4alpha-carbinolamine dehydratase activity, and binds HNF1alpha in vivo and in vitro.
123	15182178	DCoH and DCoH2 adopt identical folds with structural differences confined largely to the protein surfaces and the tetramer interface.
124	15182178	In contrast to the hyperstable DCoH tetramer, DCoH2 readily disproportionates and forms a 2:2 complex with HNF1 in vitro.
125	15182178	Phylogenetic analysis reveals six major subfamilies of DCoH proteins, including unique DCoH and DCoH2 branches in metazoans.
126	15182178	These results suggest distinct roles for DCoH and DCoH2.
127	15182178	We propose that HNF1alpha binding kinetics may distinguish regulation by DCoH2, under thermodynamic control, from regulation by DCoH, under kinetic control.
128	21047120	The two disparate functions of DCoH1 (dimerization cofactor of HNF-1)/PCD (pterin-4a-carbinolamine dehydratase) are associated with a change in oligomeric state.