Proteopedia - User contributions [en]

Zbtb7

2016-10-08T19:52:45Z

Rajesh Pal:

==Introduction==
Zbtb7 which was originally named as Pokemon (POK erythroid myeloid ontogenic factor) is a gene which plays a critical role in development, cellular differentiation and oncogenesis and has a crucial role in interacting with other POK family proteins.The gene was discovered in 2005 by the team of scientists from Memorial Sloan-Kettering Cancer Center, New York and Institute of Cancer Research, London. Scientists have reported the transcriptional repressor Pokemon as a critical factor in oncogenesis.[1] <Structure load='2NN2' size='350' frame='true' align='right' caption='BTB-zinc finger (BTB-ZF) proteins are transcription regulators with roles in development, differentiation, and oncogenesis. In these proteins, the BTB domain (also known as the POZ domain) is a protein-protein interaction motif that contains a dimerization interface, a possible oligomerization surface' scene='Insert optional scene name here' />
== Function ==
Pokemon functions as a transcription regulator with active roles in cell growth, differentiation and oncogenesis. Pokemon interferes with GC box recognition by Sp1 via interacting with the zinc finger DNA binding domain, resulting in the repression of ADH5/FDH transcription. Pokemon also affects the transcription of nuclear factor (NF)-κB-responsive genes by associating with the p65 subunit and inducing its nuclear import and stabilization. The target genes of Pokemon include extracellular matrix collagen types I, II, IX, X and XI; aggrecan; fibronectin; elastin; cartilage oligomeric matrix protein (COMP); alcohol dehydrogenase ADH5/FDH, ARF and Rb tumor suppressors; and c-fos and c-myc oncoproteins [2]

== Disease ==
Expression of Pokemon is proved to be required for normal growth, development and differentiation of cells although overexpression of this transcriptional factor has been found to be oncogenic as tested in mice both in vitro and in vivo.According to the research published in 2011 it was reported that Pokemon promotes breast cancer progression by upregulating survivin expression.[1,3]

== Structural highlights ==

Members of the POK family of proteins contain an amino-terminal POZ domain and a carboxy-terminal DNA-binding domain made of Kru¨ppel-type zinc fingers and can act as potent transcriptional repressors through the recruitment of histone deacetylases (HDACs) and subsequent chromatin remodelling.[1]

== References ==
[1] Takahiro Maeda1,2, Robin M. Hobbs1,2, Taha Merghoub1,2, Ilhem Guernah1,2, Arthur Zelent3, Carlos Cordon-Cardo2, Julie Teruya-Feldstein & Pier Paolo Pandolfi1,2. 1Cancer Biology and Genetics Program, 2Department of Pathology, Memorial Sloan-Kettering Cancer Center, Sloan-Kettering Institute, 1275 York Avenue, New York,New York 10021, USA Leukemia Research Fund Center at the Institute of Cancer Research, Chester Beatty Laboratories, Fulham Road, London SW3 6JB, UK

[2]Xuyu Zu, Jun Ma, Hongxia Liu, Feng Liu, Chunyan Tan, Lingling Yu, Jue Wang, Zhenhua Xie, Deliang Cao and Yuyang JiangEmail author
Breast Cancer Research201113:R26
DOI: 10.1186/bcr2843© Zu et al.; licensee BioMed Central Ltd. 2011

[3]https://books.google.co.in/books?id=d2_RCwAAQBAJ&pg=PA346&lpg=PA346&dq=Pokemon+protein+biology&source=bl&ots=84E--0aM7J&sig=thRXrH8HWN0eSewyt81bkD4biug&hl=en&sa=X&ved=0ahUKEwjX8de68MvPAhVLNo8KHTu1BzQQ6AEIQzAG#v=onepage&q=Pokemon%20protein%20biology&f=false

Zbtb7

2016-10-08T19:51:35Z

Rajesh Pal:

==Introduction==
Zbtb7 which was originally named as Pokemon (POK erythroid myeloid ontogenic factor) is a gene which plays a critical role in development, cellular differentiation and oncogenesis and has a crucial role in interacting with other POK family proteins.The gene was discovered in 2005 by the team of scientists from Memorial Sloan-Kettering Cancer Center, New York and Institute of Cancer Research, London. Scientists have reported the transcriptional repressor Pokemon as a critical factor in oncogenesis.[1] <Structure load='2NN2' size='350' frame='true' align='right'caption='BTB-zinc finger (BTB-ZF) proteins are transcription regulators with roles in development, differentiation, and oncogenesis. In these proteins, the BTB domain (also known as the POZ domain) is a protein-protein interaction motif that contains a dimerization interface, a possible oligomerization surface'

== Function ==
Pokemon functions as a transcription regulator with active roles in cell growth, differentiation and oncogenesis. Pokemon interferes with GC box recognition by Sp1 via interacting with the zinc finger DNA binding domain, resulting in the repression of ADH5/FDH transcription. Pokemon also affects the transcription of nuclear factor (NF)-κB-responsive genes by associating with the p65 subunit and inducing its nuclear import and stabilization. The target genes of Pokemon include extracellular matrix collagen types I, II, IX, X and XI; aggrecan; fibronectin; elastin; cartilage oligomeric matrix protein (COMP); alcohol dehydrogenase ADH5/FDH, ARF and Rb tumor suppressors; and c-fos and c-myc oncoproteins [2]

== Disease ==
Expression of Pokemon is proved to be required for normal growth, development and differentiation of cells although overexpression of this transcriptional factor has been found to be oncogenic as tested in mice both in vitro and in vivo.According to the research published in 2011 it was reported that Pokemon promotes breast cancer progression by upregulating survivin expression.[1,3]

== Structural highlights ==

Members of the POK family of proteins contain an amino-terminal POZ domain and a carboxy-terminal DNA-binding domain made of Kru¨ppel-type zinc fingers and can act as potent transcriptional repressors through the recruitment of histone deacetylases (HDACs) and subsequent chromatin remodelling.[1]

== References ==
[1] Takahiro Maeda1,2, Robin M. Hobbs1,2, Taha Merghoub1,2, Ilhem Guernah1,2, Arthur Zelent3, Carlos Cordon-Cardo2, Julie Teruya-Feldstein & Pier Paolo Pandolfi1,2. 1Cancer Biology and Genetics Program, 2Department of Pathology, Memorial Sloan-Kettering Cancer Center, Sloan-Kettering Institute, 1275 York Avenue, New York,New York 10021, USA Leukemia Research Fund Center at the Institute of Cancer Research, Chester Beatty Laboratories, Fulham Road, London SW3 6JB, UK

[2]Xuyu Zu, Jun Ma, Hongxia Liu, Feng Liu, Chunyan Tan, Lingling Yu, Jue Wang, Zhenhua Xie, Deliang Cao and Yuyang JiangEmail author
Breast Cancer Research201113:R26
DOI: 10.1186/bcr2843© Zu et al.; licensee BioMed Central Ltd. 2011

[3]https://books.google.co.in/books?id=d2_RCwAAQBAJ&pg=PA346&lpg=PA346&dq=Pokemon+protein+biology&source=bl&ots=84E--0aM7J&sig=thRXrH8HWN0eSewyt81bkD4biug&hl=en&sa=X&ved=0ahUKEwjX8de68MvPAhVLNo8KHTu1BzQQ6AEIQzAG#v=onepage&q=Pokemon%20protein%20biology&f=false

Zbtb7

2016-10-08T19:49:35Z

Rajesh Pal:

==Introduction==
Zbtb7 which was originally named as Pokemon (POK erythroid myeloid ontogenic factor) is a gene which plays a critical role in development, cellular differentiation and oncogenesis and has a crucial role in interacting with other POK family proteins.The gene was discovered in 2005 by the team of scientists from Memorial Sloan-Kettering Cancer Center, New York and Institute of Cancer Research, London. Scientists have reported the transcriptional repressor Pokemon as a critical factor in oncogenesis.[1] <Structure load='2NN2' size='350' frame='true' align='right' caption='BTB-zinc finger (BTB-ZF) proteins are transcription regulators with roles in development, differentiation, and oncogenesis. In these proteins, the BTB domain (also known as the POZ domain) is a protein-protein interaction motif that contains a dimerization interface, a possible oligomerization surface' scene='<scene name='74/744121/2nn2/1'>TextToBeDisplayed</scene>' />

== Function ==
Pokemon functions as a transcription regulator with active roles in cell growth, differentiation and oncogenesis. Pokemon interferes with GC box recognition by Sp1 via interacting with the zinc finger DNA binding domain, resulting in the repression of ADH5/FDH transcription. Pokemon also affects the transcription of nuclear factor (NF)-κB-responsive genes by associating with the p65 subunit and inducing its nuclear import and stabilization. The target genes of Pokemon include extracellular matrix collagen types I, II, IX, X and XI; aggrecan; fibronectin; elastin; cartilage oligomeric matrix protein (COMP); alcohol dehydrogenase ADH5/FDH, ARF and Rb tumor suppressors; and c-fos and c-myc oncoproteins [2]

== Disease ==
Expression of Pokemon is proved to be required for normal growth, development and differentiation of cells although overexpression of this transcriptional factor has been found to be oncogenic as tested in mice both in vitro and in vivo.According to the research published in 2011 it was reported that Pokemon promotes breast cancer progression by upregulating survivin expression.[1,3]

== Structural highlights ==

Members of the POK family of proteins contain an amino-terminal POZ domain and a carboxy-terminal DNA-binding domain made of Kru¨ppel-type zinc fingers and can act as potent transcriptional repressors through the recruitment of histone deacetylases (HDACs) and subsequent chromatin remodelling.[1]

== References ==
[1] Takahiro Maeda1,2, Robin M. Hobbs1,2, Taha Merghoub1,2, Ilhem Guernah1,2, Arthur Zelent3, Carlos Cordon-Cardo2, Julie Teruya-Feldstein & Pier Paolo Pandolfi1,2. 1Cancer Biology and Genetics Program, 2Department of Pathology, Memorial Sloan-Kettering Cancer Center, Sloan-Kettering Institute, 1275 York Avenue, New York,New York 10021, USA Leukemia Research Fund Center at the Institute of Cancer Research, Chester Beatty Laboratories, Fulham Road, London SW3 6JB, UK

[2]Xuyu Zu, Jun Ma, Hongxia Liu, Feng Liu, Chunyan Tan, Lingling Yu, Jue Wang, Zhenhua Xie, Deliang Cao and Yuyang JiangEmail author
Breast Cancer Research201113:R26
DOI: 10.1186/bcr2843© Zu et al.; licensee BioMed Central Ltd. 2011

[3]https://books.google.co.in/books?id=d2_RCwAAQBAJ&pg=PA346&lpg=PA346&dq=Pokemon+protein+biology&source=bl&ots=84E--0aM7J&sig=thRXrH8HWN0eSewyt81bkD4biug&hl=en&sa=X&ved=0ahUKEwjX8de68MvPAhVLNo8KHTu1BzQQ6AEIQzAG#v=onepage&q=Pokemon%20protein%20biology&f=false

Zbtb7

2016-10-08T19:44:55Z

Rajesh Pal:

==Introduction==
Zbtb7 which was originally named as Pokemon (POK erythroid myeloid ontogenic factor) is a gene which plays a critical role in development, cellular differentiation and oncogenesis and has a crucial role in interacting with other POK family proteins.The gene was discovered in 2005 by the team of scientists from Memorial Sloan-Kettering Cancer Center, New York and Institute of Cancer Research, London. Scientists have reported the transcriptional repressor Pokemon as a critical factor in oncogenesis.[1] <Structure load='2NN2' size='350' frame='true' align='right' caption='BTB-zinc finger (BTB-ZF) proteins are transcription regulators with roles in development, differentiation, and oncogenesis. In these proteins, the BTB domain (also known as the POZ domain) is a protein-protein interaction motif that contains a dimerization interface, a possible oligomerization surface' scene='Insert optional scene name here' />

== Function ==
Pokemon functions as a transcription regulator with active roles in cell growth, differentiation and oncogenesis. Pokemon interferes with GC box recognition by Sp1 via interacting with the zinc finger DNA binding domain, resulting in the repression of ADH5/FDH transcription. Pokemon also affects the transcription of nuclear factor (NF)-κB-responsive genes by associating with the p65 subunit and inducing its nuclear import and stabilization. The target genes of Pokemon include extracellular matrix collagen types I, II, IX, X and XI; aggrecan; fibronectin; elastin; cartilage oligomeric matrix protein (COMP); alcohol dehydrogenase ADH5/FDH, ARF and Rb tumor suppressors; and c-fos and c-myc oncoproteins [2]

== Disease ==
Expression of Pokemon is proved to be required for normal growth, development and differentiation of cells although overexpression of this transcriptional factor has been found to be oncogenic as tested in mice both in vitro and in vivo.According to the research published in 2011 it was reported that Pokemon promotes breast cancer progression by upregulating survivin expression.[1,3]

== Structural highlights ==

Members of the POK family of proteins contain an amino-terminal POZ domain and a carboxy-terminal DNA-binding domain made of Kru¨ppel-type zinc fingers and can act as potent transcriptional repressors through the recruitment of histone deacetylases (HDACs) and subsequent chromatin remodelling.[1]

==References=
[1] Takahiro Maeda1,2, Robin M. Hobbs1,2, Taha Merghoub1,2, Ilhem Guernah1,2, Arthur Zelent3, Carlos Cordon-Cardo2, Julie Teruya-Feldstein & Pier Paolo Pandolfi1,2. 1Cancer Biology and Genetics Program, 2Department of Pathology, Memorial Sloan-Kettering Cancer Center, Sloan-Kettering Institute, 1275 York Avenue, New York,New York 10021, USA Leukemia Research Fund Center at the Institute of Cancer Research, Chester Beatty Laboratories, Fulham Road, London SW3 6JB, UK

[2]Xuyu Zu, Jun Ma, Hongxia Liu, Feng Liu, Chunyan Tan, Lingling Yu, Jue Wang, Zhenhua Xie, Deliang Cao and Yuyang JiangEmail author
Breast Cancer Research201113:R26
DOI: 10.1186/bcr2843© Zu et al.; licensee BioMed Central Ltd. 2011

[3]https://books.google.co.in/books?id=d2_RCwAAQBAJ&pg=PA346&lpg=PA346&dq=Pokemon+protein+biology&source=bl&ots=84E--0aM7J&sig=thRXrH8HWN0eSewyt81bkD4biug&hl=en&sa=X&ved=0ahUKEwjX8de68MvPAhVLNo8KHTu1BzQQ6AEIQzAG#v=onepage&q=Pokemon%20protein%20biology&f=false

Zbtb7

2016-10-08T19:44:19Z

Rajesh Pal:

==Introduction==
Zbtb7 which was originally named as Pokemon (POK erythroid myeloid ontogenic factor) is a gene which plays a critical role in development, cellular differentiation and oncogenesis and has a crucial role in interacting with other POK family proteins.The gene was discovered in 2005 by the team of scientists from Memorial Sloan-Kettering Cancer Center, New York and Institute of Cancer Research, London. Scientists have reported the transcriptional repressor Pokemon as a critical factor in oncogenesis.[1] <Structure load='2NN2' size='350' frame='true' align='right' caption='BTB-zinc finger (BTB-ZF) proteins are transcription regulators with roles in development, differentiation, and oncogenesis. In these proteins, the BTB domain (also known as the POZ domain) is a protein-protein interaction motif that contains a dimerization interface, a possible oligomerization surface' scene='Insert optional scene name here' />

== Function ==
Pokemon functions as a transcription regulator with active roles in cell growth, differentiation and oncogenesis. Pokemon interferes with GC box recognition by Sp1 via interacting with the zinc finger DNA binding domain, resulting in the repression of ADH5/FDH transcription. Pokemon also affects the transcription of nuclear factor (NF)-κB-responsive genes by associating with the p65 subunit and inducing its nuclear import and stabilization. The target genes of Pokemon include extracellular matrix collagen types I, II, IX, X and XI; aggrecan; fibronectin; elastin; cartilage oligomeric matrix protein (COMP); alcohol dehydrogenase ADH5/FDH, ARF and Rb tumor suppressors; and c-fos and c-myc oncoproteins [2]

== Disease ==
Expression of Pokemon is proved to be required for normal growth, development and differentiation of cells although overexpression of this transcriptional factor has been found to be oncogenic as tested in mice both in vitro and in vivo.According to the research published in 2011 it was reported that Pokemon promotes breast cancer progression by upregulating survivin expression.[1,3]

== Structural highlights ==

Members of the POK family of proteins contain an amino-terminal POZ domain and a carboxy-terminal DNA-binding domain made of Kru¨ppel-type zinc fingers and can act as potent transcriptional repressors through the recruitment of histone deacetylases (HDACs) and subsequent chromatin remodelling.[1]

==References=
[1] Takahiro Maeda1,2, Robin M. Hobbs1,2, Taha Merghoub1,2, Ilhem Guernah1,2, Arthur Zelent3, Carlos Cordon-Cardo2, Julie Teruya-Feldstein & Pier Paolo Pandolfi1,2. 1Cancer Biology and Genetics Program, 2Department of Pathology, Memorial Sloan-Kettering Cancer Center, Sloan-Kettering Institute, 1275 York Avenue, New York,New York 10021, USA Leukemia Research Fund Center at the Institute of Cancer Research, Chester Beatty Laboratories, Fulham Road, London SW3 6JB, UK
[2]Xuyu Zu, Jun Ma, Hongxia Liu, Feng Liu, Chunyan Tan, Lingling Yu, Jue Wang, Zhenhua Xie, Deliang Cao and Yuyang JiangEmail author
Breast Cancer Research201113:R26
DOI: 10.1186/bcr2843© Zu et al.; licensee BioMed Central Ltd. 2011
[3]https://books.google.co.in/books?id=d2_RCwAAQBAJ&pg=PA346&lpg=PA346&dq=Pokemon+protein+biology&source=bl&ots=84E--0aM7J&sig=thRXrH8HWN0eSewyt81bkD4biug&hl=en&sa=X&ved=0ahUKEwjX8de68MvPAhVLNo8KHTu1BzQQ6AEIQzAG#v=onepage&q=Pokemon%20protein%20biology&f=false

Zbtb7

2016-10-08T19:31:40Z

Rajesh Pal: New page: ==Introduction== Zbtb7 which was originally named as Pokemon (POK erythroid myeloid ontogenic factor) is a gene which plays a critical role in development, cellular differentiation and onc...

Pikachurin

2016-10-08T05:40:08Z

Rajesh Pal:

==Introduction==
Synapse formation is very important for mammalian CNS to function properly. Information is transferred from photoreceptors present in the eye to bipolar and horizontal cells at the specialized synapse known as ribbon synapse.Pikachurin is an extracellular retinal protein which helps in precise interaction and signal transmission between ribbon synapse and bipolar dendrites.

== Function ==

Pikachurin protein has a dual function of photoreceptor visual synapse formation and visual perception.

== Disease ==

Visual impairments were seen in mice with deleted pikachurin gene. Congenital muscular dystrophies (CMD) such as muscle-eye-brain disease caused by defective glycosylation of α-dystroglycan (α-DG) exhibit defective photoreceptor synaptic function.

== References ==

1) Hu H, Li J, Zhang Z, Yu M . "Pikachurin interaction with dystroglycan is diminished by defective O-mannosyl glycosylation in congenital muscular dystrophy models and rescued by LARGE overexpression". Neurosci. Lett. 489 (1): 10–5.

2)http://www.uniprot.org/uniprot/Q63HQ2

3)Sato S1, Omori Y, Katoh K, Kondo M, Kanagawa M, Miyata K, Funabiki K, Koyasu T, Kajimura N, Miyoshi T, Sawai H, Kobayashi K, Tani A, Toda T, Usukura J, Tano Y, Fujikado T, Furukawa T.Pikachurin, a dystroglycan ligand, is essential for photoreceptor ribbon synapse formation.Nat Neurosci. 2008 Aug;11(8):923-31. doi: 10.1038/nn.2160. Epub 2008 Jul 20.

Pikachurin

2016-10-08T05:35:41Z

Rajesh Pal:

==Introduction==
Synapse formation is very important for mammalian CNS to function properly. Information is transferred from photoreceptors present in the eye to bipolar and horizontal cells at the specialized synapse known as ribbon synapse.Pikachurin is an extracellular retinal protein which helps in precise interaction and signal transmission between ribbon synapse and bipolar dendrites.

== Function ==

Pikachurin protein has a dual function of photoreceptor visual synapse formation and visual perception.

== Disease ==

Visual impairments were seen in mice with deleted pikachurin gene. Congenital muscular dystrophies (CMD) such as muscle-eye-brain disease caused by defective glycosylation of α-dystroglycan (α-DG) exhibit defective photoreceptor synaptic function.

== References ==
1) Hu H, Li J, Zhang Z, Yu M . "Pikachurin interaction with dystroglycan is diminished by defective O-mannosyl glycosylation in congenital muscular dystrophy models and rescued by LARGE overexpression". Neurosci. Lett. 489 (1): 10–5.

2)http://www.uniprot.org/uniprot/Q63HQ2

3)Sato S1, Omori Y, Katoh K, Kondo M, Kanagawa M, Miyata K, Funabiki K, Koyasu T, Kajimura N, Miyoshi T, Sawai H, Kobayashi K, Tani A, Toda T, Usukura J, Tano Y, Fujikado T, Furukawa T.Pikachurin, a dystroglycan ligand, is essential for photoreceptor ribbon synapse formation.Nat Neurosci. 2008 Aug;11(8):923-31. doi: 10.1038/nn.2160. Epub 2008 Jul 20.

Pikachurin

2016-10-08T05:34:31Z

Rajesh Pal:

==Introduction==
Synapse formation is very important for mammalian CNS to function properly. Information is transferred from photoreceptors present in the eye to bipolar and horizontal cells at the specialized synapse known as ribbon synapse.Pikachurin is an extracellular retinal protein which helps in precise interaction and signal transmission between ribbon synapse and bipolar dendrites.

== Function ==

Pikachurin protein has a dual function of photoreceptor visual synapse formation and visual perception.
[[Image:nn0808-857-F1.jpg]]

== Disease ==

Visual impairments were seen in mice with deleted pikachurin gene. Congenital muscular dystrophies (CMD) such as muscle-eye-brain disease caused by defective glycosylation of α-dystroglycan (α-DG) exhibit defective photoreceptor synaptic function.

== References ==
1)Hu H, Li J, Zhang Z, Yu M (February 2011). "Pikachurin interaction with dystroglycan is diminished by defective O-mannosyl glycosylation in congenital muscular dystrophy models and rescued by LARGE overexpression". Neurosci. Lett. 489 (1): 10–5.

2)http://www.uniprot.org/uniprot/Q63HQ2
<references/>

3)Sato S1, Omori Y, Katoh K, Kondo M, Kanagawa M, Miyata K, Funabiki K, Koyasu T, Kajimura N, Miyoshi T, Sawai H, Kobayashi K, Tani A, Toda T, Usukura J, Tano Y, Fujikado T, Furukawa T.Pikachurin, a dystroglycan ligand, is essential for photoreceptor ribbon synapse formation.Nat Neurosci. 2008 Aug;11(8):923-31. doi: 10.1038/nn.2160. Epub 2008 Jul 20.

Pikachurin

2016-10-07T21:53:31Z

Rajesh Pal:

== Function ==

Has a dual function of photoreceptor visual synapse formation and visual perception.

== Disease ==

Visual impairments were seen in mice with deleted pikachurin gene. Congenital muscular dystrophies (CMD) such as muscle-eye-brain disease caused by defective glycosylation of α-dystroglycan (α-DG) exhibit defective photoreceptor synaptic function.

== References ==
1)Hu H, Li J, Zhang Z, Yu M (February 2011). "Pikachurin interaction with dystroglycan is diminished by defective O-mannosyl glycosylation in congenital muscular dystrophy models and rescued by LARGE overexpression". Neurosci. Lett. 489 (1): 10–5.

2)http://www.uniprot.org/uniprot/Q63HQ2
<references/>

Pikachurin

2016-10-07T21:51:37Z

Rajesh Pal:

== Function ==

Has a dual function of photoreceptor visual synapse formation and visual perception

== Disease ==

Visual impairments were seen in mice with deleted pikachurin gene. Congenital muscular dystrophies (CMD) such as muscle-eye-brain disease caused by defective glycosylation of α-dystroglycan (α-DG) exhibit defective photoreceptor synaptic function.

== References ==
1)Hu H, Li J, Zhang Z, Yu M (February 2011). "Pikachurin interaction with dystroglycan is diminished by defective O-mannosyl glycosylation in congenital muscular dystrophy models and rescued by LARGE overexpression". Neurosci. Lett. 489 (1): 10–5.

2)http://www.uniprot.org/uniprot/Q63HQ2
<references/>

Pikachurin

2016-10-07T21:51:04Z

Rajesh Pal:

== Function ==

Has a Dual function of photoreceptor visual synapse formation and visual perception

== Disease ==

Visual Impairments were seen in mice with deleted pikachurin gene. Congenital muscular dystrophies (CMD) such as muscle-eye-brain disease caused by defective glycosylation of α-dystroglycan (α-DG) exhibit defective photoreceptor synaptic function.

== References ==
1)Hu H, Li J, Zhang Z, Yu M (February 2011). "Pikachurin interaction with dystroglycan is diminished by defective O-mannosyl glycosylation in congenital muscular dystrophy models and rescued by LARGE overexpression". Neurosci. Lett. 489 (1): 10–5.

2)http://www.uniprot.org/uniprot/Q63HQ2
<references/>

Pikachurin

2016-10-07T21:50:20Z

Rajesh Pal:

==PIKACHURIN==

== Function ==

Has a Dual function of photoreceptor visual synapse formation and visual perception

== Disease ==

Visual Impairments were seen in mice with deleted pikachurin gene. Congenital muscular dystrophies (CMD) such as muscle-eye-brain disease caused by defective glycosylation of α-dystroglycan (α-DG) exhibit defective photoreceptor synaptic function.

== References ==
1)Hu H, Li J, Zhang Z, Yu M (February 2011). "Pikachurin interaction with dystroglycan is diminished by defective O-mannosyl glycosylation in congenital muscular dystrophy models and rescued by LARGE overexpression". Neurosci. Lett. 489 (1): 10–5.
2)http://www.uniprot.org/uniprot/Q63HQ2
<references/>

Pikachurin

2016-10-07T21:48:18Z

Rajesh Pal:

==PIKACHURIN GENE==

== Function ==Has a Dual function of photoreceptor visual synapse formation and visual perception

== Disease ==Visual Impairments were seen in mice with deleted pikachurin gene. Congenital muscular dystrophies (CMD) such as muscle-eye-brain disease caused by defective glycosylation of α-dystroglycan (α-DG) exhibit defective photoreceptor synaptic function.

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
1)Hu H, Li J, Zhang Z, Yu M (February 2011). "Pikachurin interaction with dystroglycan is diminished by defective O-mannosyl glycosylation in congenital muscular dystrophy models and rescued by LARGE overexpression". Neurosci. Lett. 489 (1): 10–5.
2)http://www.uniprot.org/uniprot/Q63HQ2
<references/>

Pikachurin

2016-10-07T21:46:11Z

Rajesh Pal:

==PIKACHURIN GENE==

This is a default text for your page '''Pikachurin'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: Hu H, Li J, Zhang Z, Yu M (February 2011). "Pikachurin interaction with dystroglycan is diminished by defective O-mannosyl glycosylation in congenital muscular dystrophy models and rescued by LARGE overexpression". Neurosci. Lett. 489 (1): 10–5.
http://www.uniprot.org/uniprot/Q63HQ2.

== Function ==Has a Dual function of photoreceptor visual synapse formation and visual perception

== Disease ==Visual Impairments were seen in mice with deleted pikachurin gene. Congenital muscular dystrophies (CMD) such as muscle-eye-brain disease caused by defective glycosylation of α-dystroglycan (α-DG) exhibit defective photoreceptor synaptic function.

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>

Pikachurin

2016-10-07T21:44:54Z

Rajesh Pal:

==PIKACHURIN GENE== 0
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page '''Pikachurin'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: Hu H, Li J, Zhang Z, Yu M (February 2011). "Pikachurin interaction with dystroglycan is diminished by defective O-mannosyl glycosylation in congenital muscular dystrophy models and rescued by LARGE overexpression". Neurosci. Lett. 489 (1): 10–5.
http://www.uniprot.org/uniprot/Q63HQ2.

== Function ==Has a Dual function of photoreceptor visual synapse formation and visual perception

== Disease ==Visual Impairments were seen in mice with deleted pikachurin gene. Congenital muscular dystrophies (CMD) such as muscle-eye-brain disease caused by defective glycosylation of α-dystroglycan (α-DG) exhibit defective photoreceptor synaptic function.

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>

Pikachurin

2016-10-07T21:36:44Z

Rajesh Pal: New page: ==Your Heading Here (maybe something like 'Structure')== 0 <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> This is a default text for y...

==Your Heading Here (maybe something like 'Structure')== 0
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page '''Pikachurin'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

== Function ==Has a Dual function of photoreceptor visual synapse formation and visual perception

== Disease ==Visual Impairments were seen in mice with deleted pikachurin gene. Pikachurin also plays very role in congenital muscular dystrophies(CMD) because any defect in the function can cause Muscle-eye-brain disease.

== Relevance ==

== Structural highlights ==

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>
== References ==
<references/>