Type |
Details |
Score |
Genotype |
Symbol: |
Ldlr/Ldlr |
Background: |
involves: 129S7/SvEvBrd * C57BL/6J |
Zygosity: |
hm |
Has Mutant Allele: |
true |
|
•
•
•
•
•
|
Genotype |
Symbol: |
Rr92/Rr92 |
Background: |
involves: 129S1/Sv * 129X1/SvJ * C3H |
Zygosity: |
hm |
Has Mutant Allele: |
true |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
This entry represents the Ninja family of proteins, which play a role in stress-related and growth-related signalling cascades []. In Arabidopsis thaliana, Ninja (also known as AFP homologue 2, At4g28910) is a negative regulator of jasmonate responses. Through protein Ninja, Jasmonate ZIM-domain (JAZ) repressor proteins recruit the Groucho/Tup1-type co-repressor TOPLESS (TPL) and TPL-related proteins (TPRs) []. Ninja-family proteins AFP1 and AFP4 have been shown to act as negative regulators of the abscisic acid (ABA) response []. |
|
•
•
•
•
•
|
Publication |
First Author: |
Li K |
Year: |
2002 |
Journal: |
Hum Mol Genet |
Title: |
A gene fusion method to screen for regulatory effects on gene expression: application to the LDL receptor. |
Volume: |
11 |
Issue: |
26 |
Pages: |
3257-65 |
|
•
•
•
•
•
|
Publication |
First Author: |
Pollard DR |
Year: |
1982 |
Journal: |
Can J Genet Cytol |
Title: |
Strain and sex differences in serum alpha-fetoprotein levels in Mus musculus. |
Volume: |
24 |
Issue: |
3 |
Pages: |
343-6 |
|
•
•
•
•
•
|
Publication |
First Author: |
Garcia ME |
Year: |
2008 |
Journal: |
Plant Mol Biol |
Title: |
A small plant-specific protein family of ABI five binding proteins (AFPs) regulates stress response in germinating Arabidopsis seeds and seedlings. |
Volume: |
67 |
Issue: |
6 |
Pages: |
643-58 |
|
•
•
•
•
•
|
Publication |
First Author: |
Park JH |
Year: |
2011 |
Journal: |
Cancer Lett |
Title: |
Non-invasive monitoring of hepatocellular carcinoma in transgenic mouse with bioluminescent imaging. |
Volume: |
310 |
Issue: |
1 |
Pages: |
53-60 |
|
•
•
•
•
•
|
Publication |
First Author: |
Freitas I |
Year: |
2003 |
Journal: |
Anticancer Res |
Title: |
Stem cell recruitment and liver de-differentiation in MMTV-neu (ErbB-2) transgenic mice. |
Volume: |
23 |
Issue: |
5A |
Pages: |
3783-94 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
230
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Protein Domain |
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. |
|
•
•
•
•
•
|
Protein Domain |
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. |
|
•
•
•
•
•
|
Protein Domain |
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. |
|
•
•
•
•
•
|
Protein Domain |
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. |
|
•
•
•
•
•
|
Protein Domain |
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. |
|
•
•
•
•
•
|
Protein Domain |
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. |
|
•
•
•
•
•
|
Protein Domain |
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. |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
First Author: |
Schmithals C |
Year: |
2024 |
Journal: |
EBioMedicine |
Title: |
Tumour-specific activation of a tumour-blood transport improves the diagnostic accuracy of blood tumour markers in mice. |
Volume: |
105 |
|
Pages: |
105178 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
|
•
•
•
•
•
|
Publication |
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 |
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 |
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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•
•
•
•
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
359
 |
Fragment?: |
false |
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•
•
•
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Publication |
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 |
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 |
Organism: |
Mus musculus/domesticus |
Length: |
355
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
608
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
608
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
605
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
476
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
608
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
605
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
605
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
578
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
620
 |
Fragment?: |
false |
|
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•
•
•
•
|
Publication |
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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•
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Publication |
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 |
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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•
•
•
•
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Publication |
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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