Loss of Bardet-Biedl syndrome proteins alters the morphology and function of motile cilia in airway epithelia (Q24317556)

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3 January 2020

title

Loss of Bardet-Biedl syndrome proteins alters the morphology and function of motile cilia in airway epithelia (English)

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3 January 2020

main subject

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Bardet-Biedl syndrome 4 protein, putative (fragment)

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Bardet-Biedl syndrome 4

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Bardet-Biedl syndrome 2

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Bardet-Biedl syndrome 1 (human)

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Bardet-Biedl syndrome 2 (human)

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Bardet-Biedl syndrome 4 (human)

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McKusick-Kaufman syndrome

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Bardet-Biedl syndrome

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10

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3 January 2020

Val C. Sheffield

11

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3 January 2020

author name string

Alok S Shah

1

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3 January 2020

Sara L Farmen

2

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3 January 2020

Thomas O Moninger

3

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3 January 2020

Thomas R Businga

4

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3 January 2020

Michael P Andrews

5

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3 January 2020

Kevin Bugge

6

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Charles C Searby

7

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Darryl Nishimura

8

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3 January 2020

Kim A Brogden

9

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Michael J Welsh

12

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language of work or name

English

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publication date

25 February 2008

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number of pages

6

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Proceedings of the National Academy of Sciences of the United States of America

inferred from page(s)

published in

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volume

105

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issue

9

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3 January 2020

page(s)

3380-3385

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describes a project that uses

3 January 2020

ImageJ

1 reference

11 June 2022

https://www.ebi.ac.uk/europepmc/webservices/rest/PMC2265193/fullTextXML

inferred from PubMed Central ID database lookup

cites work

A core complex of BBS proteins cooperates with the GTPase Rab8 to promote ciliary membrane biogenesis

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Bardet-Biedl syndrome genes are important in retrograde intracellular trafficking and Kupffer's vesicle cilia function

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Pericentrin forms a complex with intraflagellar transport proteins and polycystin-2 and is required for primary cilia assembly

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Comparative genomic analysis identifies an ADP-ribosylation factor-like gene as the cause of Bardet-Biedl syndrome (BBS3)

19 March 2017

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Loss of C. elegans BBS-7 and BBS-8 protein function results in cilia defects and compromised intraflagellar transport

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The Bardet-Biedl protein BBS4 targets cargo to the pericentriolar region and is required for microtubule anchoring and cell cycle progression

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The autosomal recessive polycystic kidney disease protein is localized to primary cilia, with concentration in the basal body area

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A knockin mouse model of the Bardet-Biedl syndrome 1 M390R mutation has cilia defects, ventriculomegaly, retinopathy, and obesity

19 March 2017

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Gene expression analysis of photoreceptor cell loss in bbs4-knockout mice reveals an early stress gene response and photoreceptor cell damage

19 March 2017

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Phenotypic characterization of Bbs4 null mice reveals age-dependent penetrance and variable expressivity

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Evolution of intraflagellar transport from coated vesicles and autogenous origin of the eukaryotic cilium.

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Mkks-null mice have a phenotype resembling Bardet-Biedl syndrome

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Bbs2-null mice have neurosensory deficits, a defect in social dominance, and retinopathy associated with mislocalization of rhodopsin

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Loss of BBS proteins causes anosmia in humans and defects in olfactory cilia structure and function in the mouse

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A dynein light intermediate chain, D1bLIC, is required for retrograde intraflagellar transport

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Bardet-Biedl syndrome type 4 (BBS4)-null mice implicate Bbs4 in flagella formation but not global cilia assembly

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Crossref

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21 January 2018

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12 December 2020

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Identifiers

DOI

10.1073/PNAS.0712327105

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18299575 AND SRC:MED&resulttype=core&format=json

3 January 2020

0 references

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18299575 AND SRC:MED&resulttype=core&format=json

3 January 2020

PubMed publication ID

18299575

1 reference