User:Schm6041/PXDC1: Difference between revisions – Wikipedia

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=== Common Aliases ===

=== Common Aliases ===

PXDC1 is also known as c6orf145.<ref name=”:0″ /> should show up in gene box, if so can remove.

PXDC1 is also known as c6orf145.<ref name=”:0″ />

=== Number of Exons ===

=== Number of Exons ===

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=== Span of Gene ===

=== Span of Gene ===

The gene is found on [[chromosome 6]] (6p25.2) in the minus strand and the resulting mRNA has 8 exons, with 5 of them in the coding sequence. It is the longest transcript at 1,878 bp and encodes the longest [[Protein isoform|isoform]] PXDC1 which is 231 amino acids long.<ref name=”:1″ /> The mass of the protein is ~27 kDa and it has a pI of 4.67. Its 3D structure can be seen in Figure 1. It is predicted to be involved in enabling [[phosphatidylinositol]] binding activity and it is expressed in 26 tissues.

should be in gene box?

== mRNA ==

== mRNA ==

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=== Conceptual Translation ===

=== Conceptual Translation ===

[[File:Conceptual translation1.png|left|thumb|463x463px|Part 1 of conceptual translation of human PXDC1.]]

[[File: .png|left|thumb||Part 1 of conceptual translation of human PXDC1.]]

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== Protein ==

== Protein ==

=== Known Isoforms ===

=== Known Isoforms ===

Transcript variants are shown in previous mRNA heading. These encode two isoforms:

Transcript variants are shown in previous mRNA heading. These encode two isoforms:

* PXDC1 isoform 1: 231 amino acids

* PXDC1 isoform 1: 231 amino acids

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=== MW, pI, Amino Acid Composition ===

=== MW, pI, Amino Acid Composition ===

The mass of the protein is ~27 kDa and it has a pI of 4.67.<ref>{{Cite web |title=PXDC1 Gene |url=https://www.genecards.org/cgi-bin/carddisp.pl?gene=PXDC1 |access-date=2025-09-19 |website=GeneCards}}</ref><ref>{{Cite web |title=Ensembl Genome Browser |url=https://grch37.ensembl.org/index.html |access-date=2025-10-20 |website=grch37.ensembl.org}}</ref> The composition of amino acids is comparable to that of a typical human protein, however the difference between the number of lysine and arginine residues compared to that of glutamate and aspartate is negative compared to the average human protein.<ref>{{Cite web |last=EMBL-EBI |last2=Institute |first2=European Bioinformatics |title=Job Dispatcher homepage {{!}} EMBL-EBI |url=https://www.ebi.ac.uk/jdispatcher/ |access-date=2025-12-04 |website=www.ebi.ac.uk |language=en}}</ref> This is consistent with the observed pI, which indicates acidity.

Molecular weight of the protein is 26,560 Da.<ref>{{Cite web |title=PXDC1 Gene |url=https://www.genecards.org/cgi-bin/carddisp.pl?gene=PXDC1 |access-date=2025-09-19 |website=GeneCards}}</ref>

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pI is 4.67.<ref>{{Cite web |title=Ensembl Genome Browser |url=https://grch37.ensembl.org/index.html |access-date=2025-10-20 |website=grch37.ensembl.org}}</ref>

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[[File:Compositional analysis of pxdc1.png|thumb|592x592px|Compositional analysis of human PXDC1 protein.<ref>{{Cite web |last=EMBL-EBI |last2=Institute |first2=European Bioinformatics |title=Job Dispatcher homepage {{!}} EMBL-EBI |url=https://www.ebi.ac.uk/jdispatcher/ |access-date=2025-12-04 |website=www.ebi.ac.uk |language=en}}</ref>|none]]

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=== Post-Translational Modifications ===

=== Post-Translational Modifications ===

{| class=”wikitable mw-collapsible”

{| class=”wikitable mw-collapsible”

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Phosphorylation sites in PXDC1 protein.<ref>Sequence- and structure-based prediction of eukaryotic protein phosphorylation sites. ”Blom, N., Gammeltoft, S., and Brunak, S.” Journal of Molecular Biology: 294(5): 1351-1362, 1999.</ref>

Phosphorylation sites in PXDC1 protein.<ref>Sequence- and structure-based prediction of eukaryotic protein phosphorylation sites. ”Blom, N., Gammeltoft, S., and Brunak, S.” Journal of Molecular Biology: 294(5): 1351-1362, 1999.</ref>

Residue S147 is also predicted to be O-GalNAc (mucin type) glycosylated.<ref>”’Precision mapping of the human O-GalNAc glycoproteome through SimpleCell technology.”’

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[[File:2nd structure part1.png|thumb|501x501px|Part 1 of conceptual translation to highlight secondary structure in human PXDC1.<ref>ITASSER server <nowiki>[https://aideepmed.com/I-TASSER/]</nowiki>.</ref>|none]][[File:Part 2 secondary structure.png|thumb|495x495px|Part 2 of conceptual translation to highlight secondary structure in human PXDC1.<ref>ITASSER server <nowiki>[https://aideepmed.com/I-TASSER/]</nowiki>.</ref>|none]]

”Steentoft C, Vakhrushev SY, Joshi HJ, Kong Y, Vester-Christensen MB, Schjoldager KT, Lavrsen K, Dabelsteen S, Pedersen NB, Marcos-Silva L, Gupta R, Bennett EP, Mandel U, Brunak S, Wandall HH, Levery SB, Clausen H.”

[[File:Key conceptual translation.png|thumb|423x423px|Key for conceptual translation.|none]]

=== Tertiary Structure ===

”’EMBO J”’, 32(10):1478-88, May 15, ”’2013”’.

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(doi: 10.1038/emboj.2013.79. Epub 2013 Apr 12)</ref>

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=== Subcellular Localization ===

=== Subcellular Localization ===

Localized to the cytosolic face of the plasma membrane, and is associated peripherally.<ref>PSORT II Server <nowiki>[https://psort.hgc.jp/cgi-bin/runpsort.pl]</nowiki>.</ref><ref>{{Cite web |title=PXDC1 protein expression summary – The Human Protein Atlas |url=https://www.proteinatlas.org/ENSG00000168994-PXDC1 |access-date=2025-12-04 |website=www.proteinatlas.org}}</ref>

Localized to the cytosolic face of the plasma membrane, and is associated peripherally.<ref>PSORT II Server <nowiki>[https://psort.hgc.jp/cgi-bin/runpsort.pl]</nowiki>.</ref><ref>{{Cite web |title=PXDC1 protein expression summary – The Human Protein Atlas |url=https://www.proteinatlas.org/ENSG00000168994-PXDC1 |access-date=2025-12-04 |website=www.proteinatlas.org}}</ref>

=== Protein Interactions ===

=== Protein Interactions ===

section and table.

{| class=”wikitable”

{| class=”wikitable”

| valign=”top” |”’Interactor”’

| valign=”top” |Interactor

| valign=”top” |”’Confidence”’

| valign=”top” |

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|Score

|-

|-

| valign=”top” |LIN7C

| valign=”top” |LIN7C

| valign=”top” |0.53

| valign=”top” |

| valign=”top” |Plays a role in establishing/maintaining the asymmetric distribution of channels/receptors at the plasma membrane of polarized cells.

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|-

|-

| valign=”top” |APBA1

| valign=”top” |

| valign=”top” |0.35

| valign=”top” |

| valign=”top” |GTP-hydrolysis activating protein (GAP) for small GTPase RAB22A. Plays a role in endocytosis and intracellular protein transport.

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|-

|-

| valign=”top” |CASK

| valign=”top” |

| valign=”top” |0.35

| valign=”top” |

| valign=”top” |Plays a role in establishing/maintaining the asymmetric distribution of channels/receptors at the plasma membrane of polarized cells.

|-

| valign=”top” |LIN7A

| valign=”top” |

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|-

| valign=”top” |LIN7B

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|-

| valign=”top” |RABGAP1L

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|}

|}

Results from IMEx and IntAct protein interaction searches with human PXDC1.<ref>EMBL-EBI IMEx <nowiki>[https://www.ebi.ac.uk/intact/imex/home.xhtml]</nowiki>.</ref><ref>{{Cite web |title=IntAct Portal |url=https://www.ebi.ac.uk/intact/home |access-date=2025-12-04 |website=www.ebi.ac.uk}}</ref>

with PXDC1.<ref>EMBL-EBI IMEx <nowiki>[https://www.ebi.ac.uk/intact/imex/home.xhtml]</nowiki>.</ref><ref>{{Cite web |title=IntAct Portal |url=https://www.ebi.ac.uk/intact/home |access-date=2025-12-04 |website=www.ebi.ac.uk}}</ref>

== Homology ==

== Homology ==

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==== Evolution Speed ====

==== Evolution Speed ====

PXDC1 has a slow evolution rate compared to that of the fibrinogen alpha chain. It has a speed more similar to that of cytochrome c.<ref name=”:1″ /><ref>{{Cite web |last=EMBL-EBI |last2=Institute |first2=European Bioinformatics |title=Job Dispatcher homepage {{!}} EMBL-EBI |url=https://www.ebi.ac.uk/jdispatcher/ |access-date=2025-12-04 |website=www.ebi.ac.uk |language=en}}</ref>

PXDC1 has a slow evolution rate compared to that of the fibrinogen alpha chain. It has a speed similar to that of cytochrome c.<ref name=”:1″ /><ref>{{Cite web |last=EMBL-EBI |last2=Institute |first2=European Bioinformatics |title=Job Dispatcher homepage {{!}} EMBL-EBI |url=https://www.ebi.ac.uk/jdispatcher/ |access-date=2025-12-04 |website=www.ebi.ac.uk |language=en}}</ref>

[[File:Graphpxdc1evol.png|none|thumb|464x464px|Graph of relative evolution of PXDC1 compared to that of cytochrome c and the fibrinogen alpha chain. All 20 orthologs were used to construct the PXDC1 line. 5 organisms that were already used had their corrected sequence divergence (m) calculated for the other proteins.]]

[[File:Graphpxdc1evol.png|none|thumb||Graph of relative evolution of PXDC1 compared to that of cytochrome c and the fibrinogen alpha chain. All 20 orthologs were used to construct the PXDC1 line.]]

=== Paralogs ===

=== Paralogs ===

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== Clinical Significance ==

== Clinical Significance ==

say specific changes/associations (text-based PS1), do not say SNPs, only eQTLs if you have them

TCDD-sensitive mice had PXDC1 expression in the liver significantly repressed after exposure, PXDC1 may have a role in sensitivity to this toxin.<ref>{{Cite journal |last=Prokopec |first=Stephenie D. |last2=Lu |first2=Aileen |last3=Lee |first3=Sandy Che-Eun S. |last4=Yao |first4=Cindy Q. |last5=Sun |first5=Ren X. |last6=Watson |first6=John D. |last7=Soliymani |first7=Rabah |last8=de Borja |first8=Richard |last9=Wong |first9=Ada |last10=Sam |first10=Michelle |last11=Zuzarte |first11=Philip |last12=McPherson |first12=John D. |last13=Okey |first13=Allan B. |last14=Pohjanvirta |first14=Raimo |last15=Boutros |first15=Paul C. |date=2019-10-01 |title=Comparative toxicoproteogenomics of mouse and rat liver identifies TCDD-resistance genes |url=https://doi.org/10.1007/s00204-019-02560-0 |journal=Archives of Toxicology |language=en |volume=93 |issue=10 |pages=2961–2978 |doi=10.1007/s00204-019-02560-0 |issn=1432-0738}}</ref>

TCDD-sensitive mice had PXDC1 expression in the liver significantly repressed after exposure, PXDC1 may have a role in sensitivity to this toxin.<ref>{{Cite journal |last=Prokopec |first=Stephenie D. |last2=Lu |first2=Aileen |last3=Lee |first3=Sandy Che-Eun S. |last4=Yao |first4=Cindy Q. |last5=Sun |first5=Ren X. |last6=Watson |first6=John D. |last7=Soliymani |first7=Rabah |last8=de Borja |first8=Richard |last9=Wong |first9=Ada |last10=Sam |first10=Michelle |last11=Zuzarte |first11=Philip |last12=McPherson |first12=John D. |last13=Okey |first13=Allan B. |last14=Pohjanvirta |first14=Raimo |last15=Boutros |first15=Paul C. |date=2019-10-01 |title=Comparative toxicoproteogenomics of mouse and rat liver identifies TCDD-resistance genes |url=https://doi.org/10.1007/s00204-019-02560-0 |journal=Archives of Toxicology |language=en |volume=93 |issue=10 |pages=2961–2978 |doi=10.1007/s00204-019-02560-0 |issn=1432-0738}}</ref>

Predicted tertiary structure of PXDC1 human protein. Coloring is red for N terminus and purple for C terminus with progression through rainbow colors.[5][6]

The PX (Phox homology) domain-containing 1, also known as PXDC1 and C6orf145, is a protein which in humans is encoded by the protein coding gene PXDC1 which is 29,095 bp long. The gene is found on chromosome 6 (6p25.2) in the minus strand and the resulting mRNA has 8 exons, with 5 of them in the coding sequence. It is the longest transcript at 1,878 bp and encodes the longest isoform PXDC1 which is 231 amino acids long.[7] The mass of the protein is ~27 kDa and it has a pI of 4.67. Its 3D structure can be seen in Figure 1. It is predicted to be involved in enabling phosphatidylinositol binding activity and it is expressed in 26 tissues. The areas with the highest expression include the liver, placenta, and the gall bladder.[8] Add key info here!! fix headings.

Gene

Common Aliases

PXDC1 is also known as c6orf145.[8]

Number of Exons

Human protein contains 8 exons, with 5 of them in the coding sequence.[7]

Span of Gene

The gene is found on chromosome 6 (6p25.2) in the minus strand and the resulting mRNA has 8 exons, with 5 of them in the coding sequence. It is the longest transcript at 1,878 bp and encodes the longest isoform PXDC1 which is 231 amino acids long.[7] The mass of the protein is ~27 kDa and it has a pI of 4.67. Its 3D structure can be seen in Figure 1. It is predicted to be involved in enabling phosphatidylinositol binding activity and it is expressed in 26 tissues.

mRNA

Transcript Variants

Transcript variant Accession # Length (nt) Exons Protein isoform Accession # Length (aa) Molecular Weight (kDa)
Variant 1 NM_183373.4 1878 1-5 1 NP_899229.2 231 231
Variant X2 XM_011514393.4 1718 2-5 X1 XP_011512695.1 170 170

Transcript variants of PXDC1 gene.[7][9][10]

Expression Pattern

Expression is ubiquitous and variable across tissues. (add fold numbers).

  • Ubiquitous or tissue-specific?
  • High, moderate, low mRNA abundance
  • NCBI GEO profile across tissues, if really interesting
  • In situ hybridization data

Conceptual Translation

Part 1 of conceptual translation of human PXDC1.
Part 2 and key of conceptual translation of human PXDC1.

Protein

Known Isoforms

Transcript variants are shown in previous mRNA heading. These encode two isoforms:[7]

  • PXDC1 isoform 1: 231 amino acids
  • PXDC1 isoform X1: 170 amino acids

MW, pI, Amino Acid Composition

The mass of the protein is ~27 kDa and it has a pI of 4.67.[11][12] The composition of amino acids is comparable to that of a typical human protein, however the difference between the number of lysine and arginine residues compared to that of glutamate and aspartate is negative compared to the average human protein.[13] This is consistent with the observed pI, which indicates acidity.

Domains and Motifs

Protein diagram for human PXDC1 highlighting domains, exon boundaries, and predicted post-translational modifications.[14]

Post-Translational Modifications

Location Kinase Full name
S3 cdc2 Cyclin-dependent kinase 1
T109 PKC Protein Kinase C
S118 unsp –
S130 unsp –
S150 cdk5 Cyclin-dependent kinase 5
S176 unsp –
S202 unsp –
Y213 unsp –
T215 PKG Protein Kinase G
S218 DNAPK DNA-dependent protein kinase
T227 CKII Casein Kinase 2

Phosphorylation sites in PXDC1 protein.[15]

Residue S147 is also predicted to be O-GalNAc (mucin type) glycosylated.[16]

Structure

Predicted secondary and tertiary structure of PXDC1 human protein. Coloring is red for N terminus and purple for C terminus with progression through rainbow colors.[17][18]

Subcellular Localization

Localized to the cytosolic face of the plasma membrane, and is associated peripherally.[19][20]

Protein Interactions

Interactor Full Name Description Score
LIN7C Protein lin-7 homolog C Plays a role in establishing/maintaining the asymmetric distribution of channels/receptors at the plasma membrane of polarized cells. 0.731
RABGAP1L Rab GTPase-activating protein 1-like GTP-hydrolysis activating protein (GAP) for small GTPase RAB22A. Plays a role in endocytosis and intracellular protein transport. 0.623
LIN7B Protein lin-7 homolog B Plays a role in establishing/maintaining the asymmetric distribution of channels/receptors at the plasma membrane of polarized cells. 0.610

Table 4. Common interactors that were found with PXDC1.[21][22][23][24]

Homology

Orthologs

Class Genus and Species Common Name Taxonomic Group Median Date of Divergence from humans (MYA) Accession # Sequence Length (aa) Identity (%) Similarity (%)
Mammalia Homo sapiens Human Primates 0 NP_899229.2 231 100 100
Mammalia Mus musculus Mouse Rodents 87 NP_080107.3 231 92 94
Mammalia Phascolarctos cinereus Koala Marsupials 160 XP_020829466.1 231 90 94
Mammalia Notamacropus eugenii Tammar wallaby Marsupials 160 XP_072459796.1 231 89 94
Mammalia Ornithorhynchus anatinus Platypus Monotremes 180 XP_001508393.1 231 87 92
Aves Gallus gallus Chicken Fowl 319 XP_040520929.1 231 84 92
Reptilia Pogona vitticeps Central bearded dragon Squamata 319 XP_020645452.1 231 86 92
Reptilia Mauremys mutica Yellowpond turtle Turtles 319 XP_044863675.1 231 86 92
Amphibia Ambystoma mexicanum Axolotl Salamanders 352 XP_069469606.1 231 86 92
Amphibia Microcaecilia unicolor Tiny cayenne caecilian Caecilians 352 XP_030064485.1 230 85 92
Amphibia Rhinatrema bivittatum Two-lined caecilian Caecilians 352 XP_029446414.1 230 85 91
Fish Protopterus annectens West African lungfish Lobe-finned fish 408 XP_043937493.1 231 73 87
Fish Acipenser oxyrinchus Atlantic sturgeon Ray-finned fish 429 KAK1173668.1 232 80 90
Fish Seriola dumerili Greater amberjack Ray-finned fish 429 XP_022604539.1 233 73 86
Fish Liparis tanakae Tanaka’s snailfish Ray-finned fish 429 TNN44386.1 230 73 86
Fish Carcharodon carcharias Great white shark Sharks 462 XP_041039133.1 228 76 89
Fish Pristiophorus japonicus Japanese sawshark Sawsharks 462 XP_070735904.1 228 76 88
Fish Callorhinchus milii Elephant shark Chimaeras 462 XP_007900829.1 230 74 86
Fish Leucoraja erinaceus Little skate Skates 462 XP_055509634.1 227 62 76
Fish Myxine glutinosa Atlantic hagfish Hagfish 563 XP_067972370.1 263 36 48

Table of Orthologs to PXDC1.[25][26]

Evolution Speed

PXDC1 has a slow evolution rate compared to that of the fibrinogen alpha chain. It has a speed similar to that of cytochrome c.[7][27]

Graph of relative evolution of PXDC1 compared to that of cytochrome c and the fibrinogen alpha chain. All 20 orthologs were used to construct the PXDC1 line.

Paralogs

There are no direct paralogs of PXDC1, however, there are 49 proteins in humans that also contain the PX domain.[28]

Clinical Significance

TCDD-sensitive mice had PXDC1 expression in the liver significantly repressed after exposure, PXDC1 may have a role in sensitivity to this toxin.[29]

In the process of differentiation of dental pulp stem cells, PXDC1 was one of the genes whose expression was significantly altered. Suggests it may have a role in osteo/odontoblast differentiation.[30]

Study showed that PXDC1 had a parent-of-origin expression bias, favored paternal allele. Also, less that 100 kB away from a known imprinted gene FAM50B.[31]

Found that PXDC1 had a 2:1 paternal expression bias in lymphoblastoid cell lines and whole blood.[32]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000168994 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000021411 – Ensembl, May 2017
  3. ^ “Human PubMed Reference:”. National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ “Mouse PubMed Reference:”. National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ ITASSER server [https://aideepmed.com/I-TASSER/].
  6. ^ “iCn3D: Web-based 3D Structure Viewer”. www.ncbi.nlm.nih.gov. Retrieved 2025-12-04.
  7. ^ a b c d e f “NCBI Gene – PXDC1”. NCBI. Retrieved 2025-09-25.
  8. ^ a b “PXDC1 PX domain containing 1 [Homo sapiens (human)] – Gene – NCBI”. www.ncbi.nlm.nih.gov. Retrieved 2025-09-19.
  9. ^ “PX domain-containing protein 1 [Homo sapiens] – Protein – NCBI”. www.ncbi.nlm.nih.gov. Retrieved 2025-10-20.
  10. ^ “NCBI Nucleotide”.
  11. ^ “PXDC1 Gene”. GeneCards. Retrieved 2025-09-19.
  12. ^ “Ensembl Genome Browser”. grch37.ensembl.org. Retrieved 2025-10-20.
  13. ^ EMBL-EBI; Institute, European Bioinformatics. “Job Dispatcher homepage | EMBL-EBI”. www.ebi.ac.uk. Retrieved 2025-12-04.
  14. ^ IBS 2.0: an upgraded illustrator for the visualization of biological sequences. Nucleic Acids Research, 2022. DOI: 10.1093/nar/gkac373.
  15. ^ Sequence- and structure-based prediction of eukaryotic protein phosphorylation sites. Blom, N., Gammeltoft, S., and Brunak, S. Journal of Molecular Biology: 294(5): 1351-1362, 1999.
  16. ^ Precision mapping of the human O-GalNAc glycoproteome through SimpleCell technology.

    Steentoft C, Vakhrushev SY, Joshi HJ, Kong Y, Vester-Christensen MB, Schjoldager KT, Lavrsen K, Dabelsteen S, Pedersen NB, Marcos-Silva L, Gupta R, Bennett EP, Mandel U, Brunak S, Wandall HH, Levery SB, Clausen H.

    EMBO J, 32(10):1478-88, May 15, 2013.

    (doi: 10.1038/emboj.2013.79. Epub 2013 Apr 12)

  17. ^ ITASSER server [https://aideepmed.com/I-TASSER/].
  18. ^ “iCn3D: Web-based 3D Structure Viewer”. www.ncbi.nlm.nih.gov. Retrieved 2025-12-04.
  19. ^ PSORT II Server [https://psort.hgc.jp/cgi-bin/runpsort.pl].
  20. ^ “PXDC1 protein expression summary – The Human Protein Atlas”. www.proteinatlas.org. Retrieved 2025-12-04.
  21. ^ EMBL-EBI IMEx [https://www.ebi.ac.uk/intact/imex/home.xhtml].
  22. ^ “IntAct Portal”. www.ebi.ac.uk. Retrieved 2025-12-04.
  23. ^ “BioGRID | Database of Protein, Chemical, and Genetic Interactions”. thebiogrid.org. Retrieved 2025-12-12.
  24. ^ “PXDC1 protein (human) – STRING interaction network”. string-db.org. Retrieved 2025-12-12.
  25. ^ “BLAST: Basic Local Alignment Search Tool”. blast.ncbi.nlm.nih.gov. Retrieved 2025-10-20.
  26. ^ “TimeTree :: The Timescale of Life”. timetree.org. Retrieved 2025-10-20.
  27. ^ EMBL-EBI; Institute, European Bioinformatics. “Job Dispatcher homepage | EMBL-EBI”. www.ebi.ac.uk. Retrieved 2025-12-04.
  28. ^ Chandra, Mintu; Collins, Brett M. (2019), Atassi, M. Zouhair (ed.), “The Phox Homology (PX) Domain”, Protein Reviews – Purinergic Receptors: Volume 20, Cham: Springer International Publishing, pp. 1–17, doi:10.1007/5584_2018_185, ISBN 978-3-030-14339-8, retrieved 2025-12-04
  29. ^ Prokopec, Stephenie D.; Lu, Aileen; Lee, Sandy Che-Eun S.; Yao, Cindy Q.; Sun, Ren X.; Watson, John D.; Soliymani, Rabah; de Borja, Richard; Wong, Ada; Sam, Michelle; Zuzarte, Philip; McPherson, John D.; Okey, Allan B.; Pohjanvirta, Raimo; Boutros, Paul C. (2019-10-01). “Comparative toxicoproteogenomics of mouse and rat liver identifies TCDD-resistance genes”. Archives of Toxicology. 93 (10): 2961–2978. doi:10.1007/s00204-019-02560-0. ISSN 1432-0738.
  30. ^ Liu, Zhongjun; Xu, Shuaimei; Dao, Junfeng; Gan, Zekun; Zeng, Xiongqun (2020-04). “Differential expression of lncRNA/miRNA/mRNA and their related functional networks during the osteogenic/odontogenic differentiation of dental pulp stem cells”. Journal of Cellular Physiology. 235 (4): 3350–3361. doi:10.1002/jcp.29223. ISSN 0021-9541.
  31. ^ Mozaffari, Sahar V.; Stein, Michelle M.; Magnaye, Kevin M.; Nicolae, Dan L.; Ober, Carole (2018-09-11). “Parent of origin gene expression in a founder population identifies two new candidate imprinted genes at known imprinted regions”. PLOS ONE. 13 (9): e0203906. doi:10.1371/journal.pone.0203906. ISSN 1932-6203. PMC 6133383. PMID 30204804.{{cite journal}}: CS1 maint: article number as page number (link) CS1 maint: unflagged free DOI (link)
  32. ^ GoNL Consortium; BIOS Consortium; Jadhav, Bharati; Monajemi, Ramin; Gagalova, Kristina K.; Ho, Daniel; Draisma, Harmen H. M.; van de Wiel, Mark A.; Franke, Lude; Heijmans, Bastiaan T.; van Meurs, Joyce; Jansen, Rick; ‘t Hoen, Peter A. C.; Sharp, Andrew J.; KieÅ‚basa, Szymon M. (2019-12). “RNA-Seq in 296 phased trios provides a high-resolution map of genomic imprinting”. BMC Biology. 17 (1). doi:10.1186/s12915-019-0674-0. ISSN 1741-7007. PMC 6589892. PMID 31234833. CS1 maint: unflagged free DOI (link)

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