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Beschreibung:
Influenza A virus is a major public health threat. Novel influenza virus strains caused by genetic drift and viral recombination emerge periodically to which humans have little or no immunity, resulting in devastating pandemics. Influenza A can exist in a variety of animals; however it is in birds that all subtypes can be found. These subtypes are classified based on the combination of the virus coat glycoproteins hemagglutinin (HA) and neuraminidase (NA) subtypes. During 1997, an H5N1 avian influenza virus was determined to be the cause of death in 6 of 18 infected patients in Hong Kong. There was some evidence of human to human spread of this virus, but it is thought that the transmission efficiency was fairly low. HA interacts with cell surface proteins containing oligosaccharides with terminal sialyl residues. Virus isolated from a human infected with the H5N1 strain in 1997 could bind to oligosaccharides from human as well as avian sources, indicating its species jumping ability.
Beschreibung:
Influenza A virus is a major public health threat. Novel influenza virus strains caused by genetic drift and viral recombination emerge periodically to which humans have little or no immunity, resulting in devastating pandemics. Influenza A can exist in a variety of animals; however it is in birds that all subtypes can be found. These subtypes are classified based on the combination of the virus coat glycoproteins hemagglutinin (HA) and neuraminidase (NA) subtypes. During 1997, an H5N1 avian influenza virus was determined to be the cause of death in 6 of 18 infected patients in Hong Kong. There was some evidence of human to human spread of this virus, but it is thought that the transmission efficiency was fairly low. HA interacts with cell surface proteins containing oligosaccharides with terminal sialyl residues. Virus isolated from a human infected with the H5N1 strain in 1997 could bind to oligosaccharides from human as well as avian sources, indicating its species jumping ability.Influenza A Virus [A/California/04/2009(H1N1)]
Beschreibung:
AT-motif binding factor 1 (ATBF1) binds to the AT-rich core sequence element in the human a-fetoprotein enhancer (1). Alternative splicing generates the ATBF1-A and ATBF1-B (2,3). While ATBF1-A contains a 920-amino acid extension at the N-terminus, both ATBF1-A and ATBF1-B contain 4 DNA-binding homeobox domains (2,3). Additionally, ATBF1-A contains 23 zinc finger motifs while ATBF1-B contains 18 zinc finger motifs (1–3). The N-terminal extension unique to ATBF1-A has transcriptional repressor activity (4). In the small intestine, ATBF1-A inhibits expression of the brushborder enzyme aminopeptidase-N through direct binding to the AT motif element (5). Besides functioning in transcription regulation, ATBF1 also functions in ATPase activity (6). ATPase activity associated with ATBF1-A is DNA/RNA-dependent and requires both homeobox domains and zinc finger motifs (6). ATBF1 is highly expressed in spleen and brain tissues (7). The gene encoding human ATBF1 maps to chromosome 16q22.3-q23.1 (8).
Beschreibung:
AT-motif binding factor 1 (ATBF1) binds to the AT-rich core sequence element in the human a-fetoprotein enhancer. Alternative splicing generates the ATBF1-A and ATBF1-B. While ATBF1-A contains a 920-amino acid extension at the N-terminus, both ATBF1-A and ATBF1-B contain 4 DNA-binding homeobox domains. Additionally, ATBF1-A contains 23 zinc finger motifs while ATBF1-B contains 18 zinc finger motifs. The N-terminal extension unique to ATBF1-A has transcriptional repressor activity. In the small intestine, ATBF1-A inhibits expression of the brushborder enzyme aminopeptidase-N through direct binding to the AT motif element. Besides functioning in transcription regulation, ATBF1 also functions in ATPase activity. ATPase activity associated with ATBF1-A is DNA/RNA-dependent and requires both homeobox domains and zinc finger motifs. ATBF1 is highly expressed in spleen and brain tissues. The gene encoding human ATBF1 maps to chromosome 16q22.3-q23.1.
Beschreibung:
Influenza A virus is a major public health threat. Novel influenza virus strains caused by genetic drift and viral recombination emerge periodically to which humans have little or no immunity, resulting in devastating pandemics. Influenza A can exist in a variety of animals; however it is in birds that all subtypes can be found. These subtypes are classified based on the combination of the virus coat glycoproteins hemagglutinin (HA) and neuraminidase (NA) subtypes. During 1997, an H5N1 avian influenza virus was determined to be the cause of death in 6 of 18 infected patients in Hong Kong. There was some evidence of human to human spread of this virus, but it is thought that the transmission efficiency was fairly low. HA interacts with cell surface proteins containing oligosaccharides with terminal sialyl residues. Virus isolated from a human infected with the H5N1 strain in 1997 could bind to oligosaccharides from human as well as avian sources, indicating its species jumping ability. Influenza A Virus [A/California/04/2009(H1N1)]
Beschreibung:
Influenza A virus is a major public health threat. Novel influenza virus strains caused by genetic drift and viral recombination emerge periodically to which humans have little or no immunity, resulting in devastating pandemics. Influenza A can exist in a variety of animals; however it is in birds that all subtypes can be found. These subtypes are classified based on the combination of the virus coat glycoproteins hemagglutinin (HA) and neuraminidase (NA) subtypes. During 1997, an H5N1 avian influenza virus was determined to be the cause of death in 6 of 18 infected patients in Hong Kong. There was some evidence of human to human spread of this virus, but it is thought that the transmission efficiency was fairly low. HA interacts with cell surface proteins containing oligosaccharides with terminal sialyl residues. Virus isolated from a human infected with the H5N1 strain in 1997 could bind to oligosaccharides from human as well as avian sources, indicating its species jumping ability. Influenza A Virus [A/California/04/2009(H1N1)]
Beschreibung:
Members of the suppressor of cytokine signaling (SOCS) family of proteins contain C-terminal regions of homology called the SOCS box, which serves to couple SOCS proteins and their binding partners with the Elongin B and C complex. Several other families of proteins also contain SOCS boxes, but differ from the SOCS proteins in the type of domain they contain upstream of the SOCS box. The largest family of SOCS box-containing proteins is the ankyrin repeat and SOCS box-containing (ASB) protein family. Members of the ASB family include ASB-1 through ASB-18 and are involved in a variety of biological processes. ASB-17 is a 295 amino acid member of this family. ASB-17 contains one ankyrin repeat and one SOCS box domain. ASB-17 is thought to be a substrate-recognition subunit of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin protein ligase complex. This complex mediates the ubiquitination of target proteins and their subsequent proteasomal degradation.
Beschreibung:
Members of the suppressor of cytokine signaling (SOCS) family of proteins contain C-terminal regions of homology called the SOCS box, which serves to couple SOCS proteins and their binding partners with the Elongin B and C complex. Several other families of proteins also contain SOCS boxes, but differ from the SOCS proteins in the type of domain they contain upstream of the SOCS box. The largest family of SOCS box-containing proteins is the ankyrin repeat and SOCS box-containing (ASB) protein family. Members of the ASB family include ASB-1 through ASB-18 and are involved in a variety of biological processes. ASB-17 is a 295 amino acid member of this family. ASB-17 contains one ankyrin repeat and one SOCS box domain. ASB-17 is thought to be a substrate-recognition subunit of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin protein ligase complex. This complex mediates the ubiquitination of target proteins and their subsequent proteasomal degradation.
Beschreibung:
Nudel is important for normal cortical development. It is invovled in microtubule organization, nuclear translocation, and neuronal positioning in concert with various other factors (including Lis1, Pafah1b1, Pahfah1b2, dynein, dynorphin A and cdk5). Western blot analysis of mouse tissues shows abundant expression of Nudel in brain and testis, and much lower expression in heart, liver, kidney, and skeletal muscle. In fractionated rat brain, Nudel and Lis1 are both found in fractions enriched for postsynaptic density proteins. Immunostaining of embryonic day 18 mouse brain sections revealed staining of migrating neurons and thalamocortical axons of the intermediate zone of the developing cerebral cortex, as well as several other developing brain regions. The deduced protein contains 345 amino acids and has a calculated molecular mass of 38.4 kDa. It has a coiled coil motif (residues 19 to 201), followed by several potential phosphorylation sites for casein kinase II, protein kinase C or CDK5. Nudel shares about 50% identity with mouse and human NUDE proteins.
Beschreibung:
Nudel is important for normal cortical development. It is invovled in microtubule organization, nuclear translocation, and neuronal positioning in concert with various other factors (including Lis1, Pafah1b1, Pahfah1b2, dynein, dynorphin A and cdk5). Western blot analysis of mouse tissues shows abundant expression of Nudel in brain and testis, and much lower expression in heart, liver, kidney, and skeletal muscle. In fractionated rat brain, Nudel and Lis1 are both found in fractions enriched for postsynaptic density proteins. Immunostaining of embryonic day 18 mouse brain sections revealed staining of migrating neurons and thalamocortical axons of the intermediate zone of the developing cerebral cortex, as well as several other developing brain regions. The deduced protein contains 345 amino acids and has a calculated molecular mass of 38.4 kDa. It has a coiled coil motif (residues 19 to 201), followed by several potential phosphorylation sites for casein kinase II, protein kinase C or CDK5. Nudel shares about 50% identity with mouse and human NUDE proteins.
Beschreibung:
Midline-1 (Tripartite motif-containing protein 18, Putative transcription factor XPRF, RING finger protein 59) is a 667 amino acid protein encoded by the human gene MID1. Midline-1 belongs to the TRIM/RBCC family and contains two B box-type zinc fingers, one B30.2/SPRY domain, one COS domain, one fibronectin type-III domain and one RING-type zinc finger. Midline-1 is believed to have E3 ubiquitin ligase activity which targets the catalytic subunit of protein phosphatase 2 for degradation. It is a cytoplasmic protein found as a homodimer or heterodimer with Midline-2. It also interacts with IGBP1 (Lymphocyte signaling protein A4). Defects in MID1 are the cause of Opitz syndrome type I (OS-I). OS-I is an X-linked recessive disorder characterized by hypertelorism, genital-urinary defects such as hypospadias in males and splayed labia in females, lip-palate-laryngotracheal clefts, imperforate anus, developmental delay and congenital heart defects. OS-I mutations produce proteins with a decreased affinity for microtubules.
Beschreibung:
Nudel is important for normal cortical development. It is invovled in microtubule organization, nuclear translocation, and neuronal positioning in concert with various other factors (including Lis1, Pafah1b1, Pahfah1b2, dynein, dynorphin A and cdk5). Western blot analysis of mouse tissues shows abundant expression of Nudel in brain and testis, and much lower expression in heart, liver, kidney, and skeletal muscle. In fractionated rat brain, Nudel and Lis1 are both found in fractions enriched for postsynaptic density proteins. Immunostaining of embryonic day 18 mouse brain sections revealed staining of migrating neurons and thalamocortical axons of the intermediate zone of the developing cerebral cortex, as well as several other developing brain regions. The deduced protein contains 345 amino acids and has a calculated molecular mass of 38.4 kDa. It has a coiled coil motif (residues 19 to 201), followed by several potential phosphorylation sites for casein kinase II, protein kinase C or CDK5. Nudel shares about 50% identity with mouse and human NUDE proteins.
Beschreibung:
Nudel is important for normal cortical development. It is invovled in microtubule organization, nuclear translocation, and neuronal positioning in concert with various other factors (including Lis1, Pafah1b1, Pahfah1b2, dynein, dynorphin A and cdk5). Western blot analysis of mouse tissues shows abundant expression of Nudel in brain and testis, and much lower expression in heart, liver, kidney, and skeletal muscle. In fractionated rat brain, Nudel and Lis1 are both found in fractions enriched for postsynaptic density proteins. Immunostaining of embryonic day 18 mouse brain sections revealed staining of migrating neurons and thalamocortical axons of the intermediate zone of the developing cerebral cortex, as well as several other developing brain regions. The deduced protein contains 345 amino acids and has a calculated molecular mass of 38.4 kDa. It has a coiled coil motif (residues 19 to 201), followed by several potential phosphorylation sites for casein kinase II, protein kinase C or CDK5. Nudel shares about 50% identity with mouse and human NUDE proteins.
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