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Search results 1001 to 1067 out of 1067 for Afp

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Type Details Score
Publication
17931875 | J:130640
First Author: Castaneda JA
Year: 2008
Journal: Neurobiol Dis
Title: Identification of alpha-fetoprotein as an autoantigen in juvenile Batten disease.
Volume: 29
Issue: 1
Pages: 92-102
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Publication
9705820 | J:49677
First Author: Tomizawa M
Year: 1998
Journal: Biochem Biophys Res Commun
Title: Hepatocytes deficient in CCAAT/enhancer binding protein alpha (C/EBP alpha) exhibit both hepatocyte and biliary epithelial cell character.
Volume: 249
Issue: 1
Pages: 1-5
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Publication
18212064 | J:136812
First Author: Wilkinson DS
Year: 2008
Journal: Mol Cell Biol
Title: Chromatin-bound p53 anchors activated Smads and the mSin3A corepressor to confer transforming-growth-factor-beta-mediated transcription repression.
Volume: 28
Issue: 6
Pages: 1988-98
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Publication
15657445 | J:96056
First Author: Wilkinson DS
Year: 2005
Journal: Mol Cell Biol
Title: A direct intersection between p53 and transforming growth factor beta pathways targets chromatin modification and transcription repression of the alpha-fetoprotein gene.
Volume: 25
Issue: 3
Pages: 1200-12
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Publication
10673330 | J:60690
First Author: Peyton DK
Year: 2000
Journal: Genomics
Title: The alpha-fetoprotein promoter is the target of Afr1-mediated postnatal repression.
Volume: 63
Issue: 2
Pages: 173-80
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Publication
1370712 | J:754
First Author: Vacher J
Year: 1992
Journal: Mol Cell Biol
Title: raf regulates the postnatal repression of the mouse alpha-fetoprotein gene at the posttranscriptional level.
Volume: 12
Issue: 2
Pages: 856-64
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Publication
22684007 | J:187000
First Author: Zheng Y
Year: 2012
Journal: FEBS Lett
Title: miR-376a suppresses proliferation and induces apoptosis in hepatocellular carcinoma.
Volume: 586
Issue: 16
Pages: 2396-403
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Publication
27178213 | J:235766
First Author: Gebert C
Year: 2016
Journal: Biochem Biophys Res Commun
Title: H19ICR mediated transcriptional silencing does not require target promoter methylation.
Volume: 476
Issue: 3
Pages: 121-6
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Genotype
Genotype
Symbol: Gt(ROSA)26Sor/Gt(ROSA)26Sor<+> Tg(Alb-cre/ERT2)#Nor/?
Background: involves: 129S1/Sv * 129X1/SvJ
Zygosity: cn
Has Mutant Allele: true
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Publication
10917536 | -
First Author: Liou YC
Year: 2000
Journal: Nature
Title: Mimicry of ice structure by surface hydroxyls and water of a beta-helix antifreeze protein.
Volume: 406
Issue: 6793
Pages: 322-4
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Publication
12015145 | -
First Author: Leinala EK
Year: 2002
Journal: Structure
Title: Crystal structure of beta-helical antifreeze protein points to a general ice binding model.
Volume: 10
Issue: 5
Pages: 619-27
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Protein
Q3V0I3
Organism: Mus musculus/domesticus
Length: 230  
Fragment?: false
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Publication
15291806 | -
First Author: Graether SP
Year: 2004
Journal: Eur J Biochem
Title: Cold survival in freeze-intolerant insects: the structure and function of beta-helical antifreeze proteins.
Volume: 271
Issue: 16
Pages: 3285-96
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Protein Domain
IPR016133 | Insect_cyst_antifreeze_prot
Type: Homologous_superfamily
Description: Antifreeze proteins (AFPs) are a class of proteins that are able to bind to and inhibit the growth of macromolecular ice, thereby permitting an organism to survive subzero temperatures by decreasing the probability of ice nucleation in their bodies []. These proteins have been characterised from a variety of organisms, including fish, plants, bacteria, fungi and arthropods. This entry represents insect AFPs of the type found in Tenebrio molitor iridescent virus and in Dendroides canadensis (Pyrochroid beetle).The structure of these AFPs consists of a right-handed β-helix with 12 residues per coil. The β-helices of insect AFPs present a highly rigid array of threonine residues and bound water molecules that can effectively mimic the ice lattice. As such, β-helical AFPs provide a more effective coverage of the ice surface compared to the α-helical fish AFPs [].A second insect antifreeze from Choristoneura fumiferana (Spruce budworm) () also consists of β-helices, however in these proteins the helices form a left-handed twist; these proteins show no sequence homology to the current entry, but may act by a similar mechanism. The β-helix motif may be used as an AFP structural motif in non-homologous proteins from other (non-fish) organisms as well.
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Protein Domain
IPR036732 | AFP_Neu5c_C_sf
Type: Homologous_superfamily
Description: Antifreeze proteins (AFPs) are defined by their ability to bind ice and prevent it from growing. In this way they function inboth freeze-resistance and freeze-tolerance strategies of organisms that live at sub-zero temperatures and require protection from ice growth. In fish, five AFP types have been described that are remarkably diverse in their 3D structures. They have completely dissimilar folds and no sequence homology. Type III AFPs found in eelpouts are 65-residue proteins with a compact globular fold formed from short β-strands, which presents a flat ice binding surface. These proteins are homologous to the C-terminal region of mammalian and prokaryotic sialic acid synthase (SAS; gene neuB), which has been called AFP-like domain []. The similarity is greatest in the protein core and the flat ice-binding region. SAS is involved in the condensation of phosphoenolpyruvate with N-acetylmannosamine derivatives to generate N-acetylneuraminic acid, an intermediate used for the sialylation of glycoconjugates. The function of the AFP-like domain, which is a β-clip fold [], in SAS is not known, but it has been proposed that it could be involved in sugar binding.
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Protein Domain
IPR036668 | Antifreeze_sf
Type: Homologous_superfamily
Description: Antifreeze proteins (AFPs) are a class of proteins that are able to bind to and inhibit the growth of macromolecular ice, thereby permitting an organism to survive subzero temperatures by decreasing the probability of ice nucleation in their bodies []. These proteins have been characterised from a variety of organisms, including fish, plants, bacteria, fungi and arthropods. This entry represents insect AFPs of the type found in spruce budworm, Choristoneura fumiferana.The structure of these AFPs consists of a left-handed β-helix with 15 residues per coil []. The β-helices of insect AFPs present a highly rigid array of threonine residues and bound water molecules that can effectively mimic the ice lattice. As such, β-helical AFPs provide a more effective coverage of the ice surface compared to the α-helical fish AFPs.A second insect antifreeze from Tenebrio molitor () also consists of β-helices, however in these proteins the helices form a right-handed twist; these proteins show no sequence homology to the current entry, but may act by a similar mechanism. The β-helix motif may be used as an AFP structural motif in non-homologous proteins from other (non-fish) organisms as well.
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Protein Domain
IPR020857 | Serum_albumin_CS
Type: Conserved_site
Description: A number of serum transport proteins are known to be evolutionarily related, including albumin, alpha-fetoprotein, vitamin D-binding protein and afamin [, , ]. Albumin is the main protein of plasma; it binds water, cations (such as Ca2+, Na+and K+), fatty acids, hormones, bilirubin and drugs - its main function is to regulate the colloidal osmotic pressure of blood. Alphafeto- protein (alpha-fetoglobulin) is a foetal plasma protein that binds various cations, fatty acids and bilirubin. Vitamin D-binding protein binds to vitamin D and its metabolites, as well as to fatty acids. The biological role of afamin (alpha-albumin) has not yet been characterised. The 3D structure of human serum albumin has been determined by X-ray crystallography to a resolution of 2.8A []. It comprises three homologous domains that assemble to form a heart-shaped molecule []. Each domain is a product of two subdomains that possess common structural motifs []. The principal regions of ligand binding to human serum albumin are located in hydrophobic cavities in subdomains IIA and IIIA, which exhibit similar chemistry. Structurally, the serum albumins are similar, each domain containing five or six internal disulphide bonds, as shown schematically below:+---+ +----+ +-----+| | | | | |xxCxxxxxxxxxxxxxxxxCCxxCxxxxCxxxxxCCxxxCxxxxxxxxxCxxxxxxxxxxxxxxCCxxxxCxxxx| | | | | |+-----------------+ +-----+ +---------------+This entry represents a conserved site that covers the three conserved cysteines at the end of the Serum albumin domain. It is built in such a way that it can detect all 3 repeats in albumin and human afamin, the first two in AFP and the first one in VDB and rat afamin.
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Protein Domain
IPR007928 | Antifreeze_CF
Type: Family
Description: Antifreeze proteins (AFPs) are a class of proteins that are able to bind to and inhibit the growth of macromolecular ice, thereby permitting an organism to survive subzero temperatures by decreasing the probability of ice nucleation in their bodies []. These proteins have been characterised from a variety of organisms, including fish, plants, bacteria, fungi and arthropods. This entry represents insect AFPs of the type found in spruce budworm, Choristoneura fumiferana.The structure of these AFPs consists of a left-handed β-helix with 15 residues per coil []. The β-helices of insect AFPs present a highly rigid array of threonine residues and bound water molecules that can effectively mimic the ice lattice. As such, β-helical AFPs provide a more effective coverage of the ice surface compared to the α-helical fish AFPs.A second insect antifreeze from Tenebrio molitor () also consists of β-helices, however in these proteins the helices form a right-handed twist; these proteins show no sequence homology to the current entry, but may act by a similar mechanism. The β-helix motif may be used as an AFP structural motif in non-homologous proteins from other (non-fish) organisms as well.
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Protein Domain
IPR003460 | Insect_antifreeze_prot_motif
Type: Repeat
Description: Antifreeze proteins (AFPs) are a class of proteins that are able to bind to and inhibit the growth of macromolecular ice, thereby permitting an organism to survive subzero temperatures by decreasing the probability of ice nucleation in their bodies []. These proteins have been characterised from a variety of organisms, including fish, plants, bacteria, fungi and arthropods. This entry represents insect AFPs of the type found in Tenebrio molitor (Yellow mealworm) and in Dendroides canadensis (Pyrochroid beetle).The structure of these AFPs consists of a right-handed β-helix with 12 residues per coil. Each 12 residue-repeat contains two cys residues that form a disulphide bridge. The β-helices of insect AFPs present a highly rigid array of threonine residues and bound water molecules that can effectively mimic the ice lattice. As such, β-helical AFPs provide a more effective coverage of the ice surface compared to the α-helical fish AFPs [].A second insect antifreeze from Choristoneura fumiferana (Spruce budworm) () also consists of β-helices, however in these proteins the helices form a left-handed twist; these proteins show no sequence homology to the current entry, but may act by a similar mechanism. The β-helix motif may be used as an AFP structural motif in non-homologous proteins from other (non-fish) organisms as well.
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Protein Domain
IPR006190 | AFP_Neu5c_C
Type: Domain
Description: Antifreeze proteins (AFPs) are defined by their ability to bind ice and prevent it from growing. In this way they function in both freeze-resistance and freeze-tolerance strategies of organisms that live at sub-zero temperatures and require protection from ice growth. In fish, five AFP types have been described that are remarkably diverse in their 3D structures. They have completely dissimilar folds and no sequence homology. Type III AFPs found in eelpouts are 65-residue proteins with a compact globular fold formed from short β-strands, which presents a flat ice binding surface. These proteins are homologous to the C-terminal region of mammalian and prokaryotic sialic acid synthase (SAS; gene neuB), which has been called AFP-like domain []. The similarity is greatest in the protein core and the flat ice-binding region. SAS is involved in the condensation of phosphoenolpyruvate with N-acetylmannosamine derivatives to generate N-acetylneuraminic acid, an intermediate used for the sialylation of glycoconjugates. The function of the AFP-like domain, which is a β-clip fold [], in SAS is not known, but it has been proposed that it could be involved in sugar binding.
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Publication
25266280 | J:317522
First Author: Ohrnberger S
Year: 2015
Journal: Hepatology
Title: Dysregulated serum response factor triggers formation of hepatocellular carcinoma.
Volume: 61
Issue: 3
Pages: 979-89
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Publication
15146494 | -
First Author: Iyer LM
Year: 2004
Journal: Proteins
Title: The emergence of catalytic and structural diversity within the beta-clip fold.
Volume: 55
Issue: 4
Pages: 977-91
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Publication
20360743 | -
First Author: Pauwels L
Year: 2010
Journal: Nature
Title: NINJA connects the co-repressor TOPLESS to jasmonate signalling.
Volume: 464
Issue: 7289
Pages: 788-91
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Publication
1696927 | J:10683
First Author: Yang F
Year: 1990
Journal: Genomics
Title: Mapping and conservation of the group-specific component gene in mouse.
Volume: 7
Issue: 4
Pages: 509-16
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Publication
11106437 | J:66270
First Author: Miao M
Year: 2000
Journal: Eur J Biochem
Title: The rat ortholog of the presumptive flounder antifreeze enhancer-binding protein is a helicase domain-containing protein.
Volume: 267
Issue: 24
Pages: 7237-46
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Publication
20658536 | J:170792
First Author: Marquardt JU
Year: 2011
Journal: Int J Cancer
Title: Neighbor of Punc E11, a novel oncofetal marker for hepatocellular carcinoma.
Volume: 128
Issue: 10
Pages: 2353-63
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Publication
15466196 | J:93646
First Author: Cavin LG
Year: 2004
Journal: Cancer Res
Title: Regulation of alpha-fetoprotein by nuclear factor-kappaB protects hepatocytes from tumor necrosis factor-alpha cytotoxicity during fetal liver development and hepatic oncogenesis.
Volume: 64
Issue: 19
Pages: 7030-8
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Publication
25727848 | J:258802
First Author: Nukaya D
Year: 2015
Journal: Genes Cells
Title: Preferential gene expression and epigenetic memory of induced pluripotent stem cells derived from mouse pancreas.
Volume: 20
Issue: 5
Pages: 367-81
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Publication
16581029 | J:111141
First Author: Langlois C
Year: 2006
Journal: Biochem Pharmacol
Title: Evaluation of dichloroacetate treatment in a murine model of hereditary tyrosinemia type 1.
Volume: 71
Issue: 11
Pages: 1648-61
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Publication
22617046 | J:190486
First Author: Nuño-Ayala M
Year: 2012
Journal: Physiol Genomics
Title: Cystathionine β-synthase deficiency causes infertility by impairing decidualization and gene expression networks in uterus implantation sites.
Volume: 44
Issue: 14
Pages: 702-16
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Publication
21442721 | J:166734
First Author: Viotti M
Year: 2011
Journal: Genesis
Title: Afp::mCherry, a red fluorescent transgenic reporter of the mouse visceral endoderm.
Volume: 49
Issue: 3
Pages: 124-33
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Publication
7489990 | J:239810
First Author: Arbuthnot P
Year: 1995
Journal: Hepatology
Title: Hepatoma cell-specific expression of a retrovirally transferred gene is achieved by alpha-fetoprotein but not insulinlike growth factor II regulatory sequences.
Volume: 22
Issue: 6
Pages: 1788-96
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Publication
11058961 | J:242552
First Author: Bois-Joyeux B
Year: 2000
Journal: DNA Cell Biol
Title: Modulation of the far-upstream enhancer of the rat alpha-fetoprotein gene by members of the ROR alpha, Rev-erb alpha, and Rev-erb beta groups of monomeric orphan nuclear receptors.
Volume: 19
Issue: 10
Pages: 589-99
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Publication
11714029 | J:73005
First Author: Sakairi T
Year: 2001
Journal: J Vet Med Sci
Title: Immunohistochemical characterization of hepatoblastomas in B6C3F1 mice treated with diethylnitrosamine and sodium phenobarbital.
Volume: 63
Issue: 10
Pages: 1121-5
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Publication
1691009 | J:27819
First Author: Adinolfi M
Year: 1990
Journal: Exp Clin Immunogenet
Title: Alpha-fetoprotein levels in different strains of mice during development.
Volume: 7
Issue: 2
Pages: 123-8
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Publication
8374795 | J:13585
First Author: Neumann PE
Year: 1993
Journal: Brain Res
Title: Genetic analysis of cerebellar folial pattern in crosses of C57BL/6J and DBA/2J inbred mice.
Volume: 619
Issue: 1-2
Pages: 81-8
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Publication
7692743 | J:14806
First Author: Serfas MS
Year: 1993
Journal: Am J Physiol
Title: HNF-1 alpha and HNF-1 beta expression in mouse intestinal crypts.
Volume: 265
Issue: 3 Pt 1
Pages: G506-13
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Publication
7544436 | J:28183
First Author: Ramesh TM
Year: 1995
Journal: Mol Cell Biol
Title: Individual mouse alpha-fetoprotein enhancer elements exhibit different patterns of tissue-specific and hepatic position-dependent activities.
Volume: 15
Issue: 9
Pages: 4947-55
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Publication
7557431 | J:41430
First Author: Nishio H
Year: 1995
Journal: Gene
Title: The chimpanzee alpha-fetoprotein-encoding gene shows structural similarity to that of gorilla but distinct differences from that of human.
Volume: 162
Issue: 2
Pages: 213-20
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Publication
9671753 | J:91046
First Author: Jin DK
Year: 1998
Journal: Proc Natl Acad Sci U S A
Title: alpha-Fetoprotein gene sequences mediating Afr2 regulation during liver regeneration.
Volume: 95
Issue: 15
Pages: 8767-72
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Publication
15743813 | J:97510
First Author: Nguyen TT
Year: 2005
Journal: Mol Cell Biol
Title: Transcription factor interactions and chromatin modifications associated with p53-mediated, developmental repression of the alpha-fetoprotein gene.
Volume: 25
Issue: 6
Pages: 2147-57
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Publication
18573881 | J:139743
First Author: Tsai WW
Year: 2008
Journal: Mol Cell Biol
Title: p53-targeted LSD1 functions in repression of chromatin structure and transcription in vivo.
Volume: 28
Issue: 17
Pages: 5139-46
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Publication
28614380 | J:248361
First Author: Cheng ST
Year: 2017
Journal: PLoS One
Title: Interleukin-34 inhibits hepatitis B virus replication in vitro and in vivo.
Volume: 12
Issue: 6
Pages: e0179605
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Publication
26426686 | J:305986
 
First Author: Kessler SM
Year: 2015
Journal: Cell Death Dis
Title: IMP2/p62 induces genomic instability and an aggressive hepatocellular carcinoma phenotype.
Volume: 6
Pages: e1894
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Publication
22563169 | J:321129
First Author: Zhou XJ
Year: 2012
Journal: World J Gastroenterol
Title: Over-expression of uPA increases risk of liver injury in pAAV-HBV transfected mice.
Volume: 18
Issue: 16
Pages: 1892-902
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Publication
21354236 | J:325938
First Author: Lu X
Year: 2011
Journal: J Hepatol
Title: Alpha-fetoprotein-thymidine kinase-luciferase knockin mice: a novel model for dual modality longitudinal imaging of tumorigenesis in liver.
Volume: 55
Issue: 1
Pages: 96-102
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Publication
29944670 | J:262925
First Author: Hwang A
Year: 2018
Journal: PLoS One
Title: Supervised learning reveals circulating biomarker levels diagnostic of hepatocellular carcinoma in a clinically relevant model of non-alcoholic steatohepatitis; An OAD to NASH.
Volume: 13
Issue: 6
Pages: e0198937
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Publication
23188673 | J:194680
First Author: Sun Y
Year: 2013
Journal: Carcinogenesis
Title: Annexin A2 is a discriminative serological candidate in early hepatocellular carcinoma.
Volume: 34
Issue: 3
Pages: 595-604
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Publication
8898244 | J:36696
First Author: Wu JX
Year: 1996
Journal: Development
Title: Kinase-negative mutant epidermal growth factor receptor (EGFR) expression during embryonal stem cell differentiation favours EGFR-independent lineages.
Volume: 122
Issue: 10
Pages: 3331-42
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Publication
16894545 | J:115997
First Author: Bagis H
Year: 2006
Journal: Mol Reprod Dev
Title: Stable transmission and transcription of newfoundland ocean pout type III fish antifreeze protein (AFP) gene in transgenic mice and hypothermic storage of transgenic ovary and testis.
Volume: 73
Issue: 11
Pages: 1404-11
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Protein
Q99J77
Organism: Mus musculus/domesticus
Length: 359  
Fragment?: false
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Publication
12171656 | -
First Author: Davies PL
Year: 2002
Journal: Philos Trans R Soc Lond B Biol Sci
Title: Structure and function of antifreeze proteins.
Volume: 357
Issue: 1423
Pages: 927-35
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Publication
9918916 | J:53627
First Author: Sakamoto T
Year: 1999
Journal: Hepatology
Title: Mitosis and apoptosis in the liver of interleukin-6-deficient mice after partial hepatectomy.
Volume: 29
Issue: 2
Pages: 403-11
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Protein
A0A0J9YV75
Organism: Mus musculus/domesticus
Length: 355  
Fragment?: false
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Protein
O89020
Organism: Mus musculus/domesticus
Length: 608  
Fragment?: false
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Protein
P07724
Organism: Mus musculus/domesticus
Length: 608  
Fragment?: false
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Protein
P02772
Organism: Mus musculus/domesticus
Length: 605  
Fragment?: false
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Protein
P21614
Organism: Mus musculus/domesticus
Length: 476  
Fragment?: false
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Protein
Q546G4
Organism: Mus musculus/domesticus
Length: 608  
Fragment?: false
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Protein
Q8BK65
Organism: Mus musculus/domesticus
Length: 605  
Fragment?: false
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Protein
Q8BK56
Organism: Mus musculus/domesticus
Length: 605  
Fragment?: false
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Protein
Q3TGA3
Organism: Mus musculus/domesticus
Length: 578  
Fragment?: true
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Protein
F8VQ07
Organism: Mus musculus/domesticus
Length: 620  
Fragment?: false
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Publication
2423133 | -
First Author: Schoentgen F
Year: 1986
Journal: Biochim Biophys Acta
Title: Complete amino acid sequence of human vitamin D-binding protein (group-specific component): evidence of a three-fold internal homology as in serum albumin and alpha-fetoprotein.
Volume: 871
Issue: 2
Pages: 189-98
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Publication
7517938 | J:18959
First Author: Lichenstein HS
Year: 1994
Journal: J Biol Chem
Title: Afamin is a new member of the albumin, alpha-fetoprotein, and vitamin D-binding protein gene family.
Volume: 269
Issue: 27
Pages: 18149-54
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Publication
2481749 | -
First Author: Haefliger DN
Year: 1989
Journal: J Mol Evol
Title: Amphibian albumins as members of the albumin, alpha-fetoprotein, vitamin D-binding protein multigene family.
Volume: 29
Issue: 4
Pages: 344-54
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Publication
1630489 | -
First Author: He XM
Year: 1992
Journal: Nature
Title: Atomic structure and chemistry of human serum albumin.
Volume: 358
Issue: 6383
Pages: 209-15
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MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

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