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PMID |
Sentence |
1 |
15155861
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The BBS6 gene is predicted to code for a protein with sequence similarity to the chaperonin family of proteins.
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2 |
15155861
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The predicted BBS1, BBS2, BBS4, BBS7, and BBS8 gene products do not seem to be molecular chaperones, on the basis of a lack of sequence similarity to the chaperonin family of proteins.
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3 |
15155861
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The identification of BBS8 suggests a possible role in cilia function for BBS gene products.
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4 |
15231740
|
Loss of C. elegans BBS-7 and BBS-8 protein function results in cilia defects and compromised intraflagellar transport.
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5 |
15231740
|
Here, we show that mutations in the Caenorhabditis elegans bbs-7 and bbs-8 genes cause structural and functional defects in cilia.
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6 |
15231740
|
Importantly, we demonstrate that BBS-7 and BBS-8 are required for the normal localization/motility of the IFT proteins OSM-5/Polaris and CHE-11, and to a notably lesser extent, CHE-2.
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7 |
15231740
|
Loss of C. elegans BBS-7 and BBS-8 protein function results in cilia defects and compromised intraflagellar transport.
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8 |
15231740
|
Here, we show that mutations in the Caenorhabditis elegans bbs-7 and bbs-8 genes cause structural and functional defects in cilia.
|
9 |
15231740
|
Importantly, we demonstrate that BBS-7 and BBS-8 are required for the normal localization/motility of the IFT proteins OSM-5/Polaris and CHE-11, and to a notably lesser extent, CHE-2.
|
10 |
15231740
|
Loss of C. elegans BBS-7 and BBS-8 protein function results in cilia defects and compromised intraflagellar transport.
|
11 |
15231740
|
Here, we show that mutations in the Caenorhabditis elegans bbs-7 and bbs-8 genes cause structural and functional defects in cilia.
|
12 |
15231740
|
Importantly, we demonstrate that BBS-7 and BBS-8 are required for the normal localization/motility of the IFT proteins OSM-5/Polaris and CHE-11, and to a notably lesser extent, CHE-2.
|
13 |
15666242
|
A mutation of the BBS1 gene on chromosome 11q13 is observed in 30%-40% of BBS cases.
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14 |
15666242
|
In six cases, we identified a recessive mutation in a BBS gene (three in BBS2, two in BBS4, and one in BBS6).
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15 |
15666242
|
No BBS1, BBS3, BBS5, BBS7, or BBS8 mutations were identified in our series.
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16 |
15666242
|
These results suggest that the antenatal presentation of BBS may mimic Meckel syndrome.
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17 |
22500027
|
To date, 16 BBS genes have been reported, seven of which (BBS1, 2, 4, 5, 7, 8, and 9) code for proteins that form a complex known as the BBSome.
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18 |
22500027
|
Three additional BBS genes (BBS6, BBS10, and BBS12) have homology to type II chaperonins and interact with CCT/TRiC proteins and BBS7 to form a complex termed the BBS-chaperonin complex.
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19 |
22500027
|
By characterizing BBSome assembly intermediates, we show that the BBS-chaperonin complex plays a role in BBS7 stability.
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20 |
22500027
|
BBS7 interacts with BBS2 and becomes part of a BBS7-BBS2-BBS9 assembly intermediate referred to as the BBSome core complex because it forms the core of the BBSome.
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21 |
22500027
|
BBS1, BBS5, BBS8, and finally BBS4 are added to the BBSome core to form the complete BBSome.
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22 |
22500027
|
To date, 16 BBS genes have been reported, seven of which (BBS1, 2, 4, 5, 7, 8, and 9) code for proteins that form a complex known as the BBSome.
|
23 |
22500027
|
Three additional BBS genes (BBS6, BBS10, and BBS12) have homology to type II chaperonins and interact with CCT/TRiC proteins and BBS7 to form a complex termed the BBS-chaperonin complex.
|
24 |
22500027
|
By characterizing BBSome assembly intermediates, we show that the BBS-chaperonin complex plays a role in BBS7 stability.
|
25 |
22500027
|
BBS7 interacts with BBS2 and becomes part of a BBS7-BBS2-BBS9 assembly intermediate referred to as the BBSome core complex because it forms the core of the BBSome.
|
26 |
22500027
|
BBS1, BBS5, BBS8, and finally BBS4 are added to the BBSome core to form the complete BBSome.
|
27 |
22500027
|
To date, 16 BBS genes have been reported, seven of which (BBS1, 2, 4, 5, 7, 8, and 9) code for proteins that form a complex known as the BBSome.
|
28 |
22500027
|
Three additional BBS genes (BBS6, BBS10, and BBS12) have homology to type II chaperonins and interact with CCT/TRiC proteins and BBS7 to form a complex termed the BBS-chaperonin complex.
|
29 |
22500027
|
By characterizing BBSome assembly intermediates, we show that the BBS-chaperonin complex plays a role in BBS7 stability.
|
30 |
22500027
|
BBS7 interacts with BBS2 and becomes part of a BBS7-BBS2-BBS9 assembly intermediate referred to as the BBSome core complex because it forms the core of the BBSome.
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31 |
22500027
|
BBS1, BBS5, BBS8, and finally BBS4 are added to the BBSome core to form the complete BBSome.
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