Type |
Details |
Score |
Publication |
First Author: |
Resendez SL |
Year: |
2020 |
Journal: |
J Neurosci |
Title: |
Social Stimuli Induce Activation of Oxytocin Neurons Within the Paraventricular Nucleus of the Hypothalamus to Promote Social Behavior in Male Mice. |
Volume: |
40 |
Issue: |
11 |
Pages: |
2282-2295 |
|
•
•
•
•
•
|
Publication |
First Author: |
Ortiz-Guzman J |
Year: |
2024 |
Journal: |
eNeuro |
Title: |
Cholinergic Basal Forebrain Connectivity to the Basolateral Amygdala Modulates Food Intake. |
Volume: |
11 |
Issue: |
3 |
|
|
•
•
•
•
•
|
Publication |
First Author: |
Boitnott A |
Year: |
2021 |
Journal: |
Biol Psychiatry |
Title: |
Developmental and Behavioral Phenotypes in a Mouse Model of DDX3X Syndrome. |
Volume: |
90 |
Issue: |
11 |
Pages: |
742-755 |
|
•
•
•
•
•
|
Publication |
First Author: |
Jeanne M |
Year: |
2021 |
Journal: |
Hum Genet |
Title: |
Haploinsufficiency of the HIRA gene located in the 22q11 deletion syndrome region is associated with abnormal neurodevelopment and impaired dendritic outgrowth. |
Volume: |
140 |
Issue: |
6 |
Pages: |
885-896 |
|
•
•
•
•
•
|
Publication |
First Author: |
Rodriguez-Romaguera J |
Year: |
2020 |
Journal: |
Cell Rep |
Title: |
Prepronociceptin-Expressing Neurons in the Extended Amygdala Encode and Promote Rapid Arousal Responses to Motivationally Salient Stimuli. |
Volume: |
33 |
Issue: |
6 |
Pages: |
108362 |
|
•
•
•
•
•
|
Publication |
First Author: |
Kho I |
Year: |
2023 |
Journal: |
JCI Insight |
Title: |
Severe kidney dysfunction in sialidosis mice reveals an essential role for neuraminidase 1 in reabsorption. |
Volume: |
8 |
Issue: |
20 |
|
|
•
•
•
•
•
|
Publication |
First Author: |
Rosado CJ |
Year: |
2007 |
Journal: |
Science |
Title: |
A common fold mediates vertebrate defense and bacterial attack. |
Volume: |
317 |
Issue: |
5844 |
Pages: |
1548-51 |
|
•
•
•
•
•
|
Publication |
First Author: |
Feng WW |
Year: |
2019 |
Journal: |
Cell Rep |
Title: |
CD36-Mediated Metabolic Rewiring of Breast Cancer Cells Promotes Resistance to HER2-Targeted Therapies. |
Volume: |
29 |
Issue: |
11 |
Pages: |
3405-3420.e5 |
|
•
•
•
•
•
|
Publication |
First Author: |
Apicco DJ |
Year: |
2018 |
Journal: |
Nat Neurosci |
Title: |
Reducing the RNA binding protein TIA1 protects against tau-mediated neurodegeneration in vivo. |
Volume: |
21 |
Issue: |
1 |
Pages: |
72-80 |
|
•
•
•
•
•
|
Publication |
First Author: |
Tang CC |
Year: |
2021 |
Journal: |
Elife |
Title: |
Dual targeting of salt inducible kinases and CSF1R uncouples bone formation and bone resorption. |
Volume: |
10 |
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Visnes T |
Year: |
2009 |
Journal: |
Philos Trans R Soc Lond B Biol Sci |
Title: |
Uracil in DNA and its processing by different DNA glycosylases. |
Volume: |
364 |
Issue: |
1517 |
Pages: |
563-8 |
|
•
•
•
•
•
|
Publication |
First Author: |
Earl C |
Year: |
2018 |
Journal: |
Nucleic Acids Res |
Title: |
A structurally conserved motif in γ-herpesvirus uracil-DNA glycosylases elicits duplex nucleotide-flipping. |
Volume: |
46 |
Issue: |
8 |
Pages: |
4286-4300 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
Uracil-DNA glycosylase (UDG, UNG) []is a DNA repair enzyme that excises uracil residues from DNA by cleaving the N-glycosylic bond. Uracil in DNA can arise as a result of mis-incorporation of dUMP residues by DNA polymerase or deamination of cytosine. UDGs were classified into 4 families [, ].Family 1 enzymes are active against uracil in both ssDNA and dsDNA, and recognise uracil explicitly in an extrahelical conformation via a combination of protein and bound-water interactions []. Family 1 enzymes are present in Eubacteria, Eukarya and in some eukaryotic viruses. The sequence of uracil-DNA glycosylases is extremely well conserved []in bacteria and eukaryotes as well as in herpes viruses []. More distantly related uracil-DNA glycosylases are also found in poxviruses []. In eukaryotic cells, UNG activity is found in both the nucleus and the mitochondria. Human nuclear UNG2 and mitochondrial UNG1are both encoded by the UNG gene [, ]. The N-terminal 77 amino acids of UNG1 seem to be required for mitochondrial localisation []. The catalytic C-terminal domains of UNGs are highly conserved at both the sequence and structure level while the N-terminal domains are diverse and are thought to be involved in subcellular localisation and protein-protein interactions []. |
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•
•
•
•
•
|
Publication |
First Author: |
Sancar A |
Year: |
1988 |
Journal: |
Annu Rev Biochem |
Title: |
DNA repair enzymes. |
Volume: |
57 |
|
Pages: |
29-67 |
|
•
•
•
•
•
|
Publication |
First Author: |
Slupphaug G |
Year: |
1993 |
Journal: |
Nucleic Acids Res |
Title: |
Nuclear and mitochondrial forms of human uracil-DNA glycosylase are encoded by the same gene. |
Volume: |
21 |
Issue: |
11 |
Pages: |
2579-84 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
132
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
306
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
185
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Publication |
First Author: |
Nilsen H |
Year: |
2001 |
Journal: |
EMBO J |
Title: |
Excision of deaminated cytosine from the vertebrate genome: role of the SMUG1 uracil-DNA glycosylase. |
Volume: |
20 |
Issue: |
15 |
Pages: |
4278-86 |
|
•
•
•
•
•
|
Publication |
First Author: |
Lauritzen KH |
Year: |
2010 |
Journal: |
Mol Cell Biol |
Title: |
Mitochondrial DNA toxicity in forebrain neurons causes apoptosis, neurodegeneration, and impaired behavior. |
Volume: |
30 |
Issue: |
6 |
Pages: |
1357-67 |
|
•
•
•
•
•
|
Publication |
First Author: |
Green B |
Year: |
2018 |
Journal: |
Exp Hematol |
Title: |
Deficiency in the DNA glycosylases UNG1 and OGG1 does not potentiate c-Myc-induced B-cell lymphomagenesis. |
Volume: |
61 |
|
Pages: |
52-58 |
|
•
•
•
•
•
|
Publication |
First Author: |
Schärer OD |
Year: |
2001 |
Journal: |
Bioessays |
Title: |
Recent progress in the biology, chemistry and structural biology of DNA glycosylases. |
Volume: |
23 |
Issue: |
3 |
Pages: |
270-81 |
|
•
•
•
•
•
|
Publication |
First Author: |
Pearl LH |
Year: |
2000 |
Journal: |
Mutat Res |
Title: |
Structure and function in the uracil-DNA glycosylase superfamily. |
Volume: |
460 |
Issue: |
3-4 |
Pages: |
165-81 |
|
•
•
•
•
•
|
Publication |
First Author: |
Savva R |
Year: |
1995 |
Journal: |
Nature |
Title: |
The structural basis of specific base-excision repair by uracil-DNA glycosylase. |
Volume: |
373 |
Issue: |
6514 |
Pages: |
487-93 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Active_site |
Description: |
Uracil-DNA glycosylase (UNG) []is a DNA repair enzyme that excises uracil residues from DNA by cleaving the N-glycosylic bond. Uracil in DNA can arise as a result of mis-incorporation of dUMP residues by DNA polymerase or deamination of cytosine.The sequence of uracil-DNA glycosylase is extremely well conserved []in bacteria and eukaryotes as well as in herpes viruses. More distantly related uracil-DNA glycosylases are also found in poxviruses []. In eukaryotic cells, UNG activity is found in both the nucleus and the mitochondria. Human UNG1 protein is transported to both the mitochondria and the nucleus []. The N-terminal 77 amino acids of UNG1 seem to be required for mitochondrial localisation [], but the presence of a mitochondrial transitpeptide has not been directly demonstrated. The most N-terminal conserved region contains an aspartic acid residue which has been proposed, based on X-ray structures [, ]to act as a general base in the catalytic mechanism.This signature pattern covers the most N-terminal conserved region, which contains an aspartic acid residue that has been proposed, based on X-ray structures [, ]to act as a general base in the catalytic mechanism. |
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•
•
•
•
•
|
Publication |
First Author: |
Olsen LC |
Year: |
1989 |
Journal: |
EMBO J |
Title: |
Molecular cloning of human uracil-DNA glycosylase, a highly conserved DNA repair enzyme. |
Volume: |
8 |
Issue: |
10 |
Pages: |
3121-5 |
|
•
•
•
•
•
|
Publication |
First Author: |
Upton C |
Year: |
1993 |
Journal: |
Proc Natl Acad Sci U S A |
Title: |
Identification of a poxvirus gene encoding a uracil DNA glycosylase. |
Volume: |
90 |
Issue: |
10 |
Pages: |
4518-22 |
|
•
•
•
•
•
|
Publication |
First Author: |
Masaoka A |
Year: |
2003 |
Journal: |
Biochemistry |
Title: |
Mammalian 5-formyluracil-DNA glycosylase. 2. Role of SMUG1 uracil-DNA glycosylase in repair of 5-formyluracil and other oxidized and deaminated base lesions. |
Volume: |
42 |
Issue: |
17 |
Pages: |
5003-12 |
|
•
•
•
•
•
|
Publication |
First Author: |
Wu X |
Year: |
2007 |
Journal: |
J Exp Med |
Title: |
DNA polymerase beta is able to repair breaks in switch regions and plays an inhibitory role during immunoglobulin class switch recombination. |
Volume: |
204 |
Issue: |
7 |
Pages: |
1677-89 |
|
•
•
•
•
•
|
Publication |
First Author: |
Rogier M |
Year: |
2021 |
Journal: |
Nature |
Title: |
Fam72a enforces error-prone DNA repair during antibody diversification. |
Volume: |
600 |
Issue: |
7888 |
Pages: |
329-333 |
|
•
•
•
•
•
|
Publication |
First Author: |
Wu L |
Year: |
2022 |
Journal: |
Genes Dev |
Title: |
HMCES protects immunoglobulin genes specifically from deletions during somatic hypermutation. |
Volume: |
36 |
Issue: |
7-8 |
Pages: |
433-450 |
|
•
•
•
•
•
|
Publication |
First Author: |
Kadungure T |
Year: |
2015 |
Journal: |
PLoS One |
Title: |
Individual substitution mutations in the AID C terminus that ablate IgH class switch recombination. |
Volume: |
10 |
Issue: |
8 |
Pages: |
e0134397 |
|
•
•
•
•
•
|
Publication |
First Author: |
Mol CD |
Year: |
1995 |
Journal: |
Cell |
Title: |
Crystal structure and mutational analysis of human uracil-DNA glycosylase: structural basis for specificity and catalysis. |
Volume: |
80 |
Issue: |
6 |
Pages: |
869-78 |
|
•
•
•
•
•
|