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Table representation of search results timeline featuring number of search results per year.

Year Number of Results
2004 3
2005 1
2006 1
2007 2
2009 1
2012 1
2013 1
2016 1
2017 2
2020 1
2022 2
2023 2
2024 1

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16 results

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Page 1
IL-7: Comprehensive review.
Winer H, Rodrigues GOL, Hixon JA, Aiello FB, Hsu TC, Wachter BT, Li W, Durum SK. Winer H, et al. Cytokine. 2022 Dec;160:156049. doi: 10.1016/j.cyto.2022.156049. Epub 2022 Oct 3. Cytokine. 2022. PMID: 36201890 Review.
Human IL-7R: gene ID 3575 on ch 5; human IL2RG: gene ID 3561 on ch X; mouse IL-7R: gene ID 16,197 on ch 15; murine Il2rg gene ID 16,186 on ch X. Member of gammac family of receptors for cytokines IL-2, -4, -9, -15, and -21. ...
Human IL-7R: gene ID 3575 on ch 5; human IL2RG: gene ID 3561 on ch X; mouse IL-7R: gene ID 16,197 on ch 15; murine Il2rg gene ID 16,186 on c …
Inflammation and Organ Injury the Role of Substance P and Its Receptors.
Zhu Z, Bhatia M. Zhu Z, et al. Int J Mol Sci. 2023 Mar 24;24(7):6140. doi: 10.3390/ijms24076140. Int J Mol Sci. 2023. PMID: 37047113 Free PMC article. Review.
The proinflammatory effects of SP are achieved by activating its functional receptors, namely the neurokinin 1 receptor (NK1R) receptor and mas-related G protein-coupled receptors X member 2 (MRGPRX2) and its murine homolog MRGPRB2. Upon activation, the receptors fu …
The proinflammatory effects of SP are achieved by activating its functional receptors, namely the neurokinin 1 receptor (NK1R) receptor and …
DNA polymerase mu: An inflexible scaffold for substrate flexibility.
Kaminski AM, Bebenek K, Pedersen LC, Kunkel TA. Kaminski AM, et al. DNA Repair (Amst). 2020 Sep;93:102932. doi: 10.1016/j.dnarep.2020.102932. DNA Repair (Amst). 2020. PMID: 33087269 Free PMC article. Review.
DNA polymerase mu is a Family X member that participates in repair of DNA double strand breaks (DSBs) by non-homologous end joining. ...
DNA polymerase mu is a Family X member that participates in repair of DNA double strand breaks (DSBs) by non-homologous end jo …
MiRNA-29b and miRNA-497 Modulate the Expression of Carboxypeptidase X Member 2, a Candidate Gene Associated with Left Ventricular Hypertrophy.
Subrova J, Böhme K, Gillespie A, Orphal M, Plum C, Kreutz R, Eisenreich A. Subrova J, et al. Int J Mol Sci. 2022 Feb 18;23(4):2263. doi: 10.3390/ijms23042263. Int J Mol Sci. 2022. PMID: 35216380 Free PMC article.
Recently, a novel candidate gene encoding the carboxypeptidase X member 2 (CPXM2) was found to be associated with hypertension-induced LVH. ...
Recently, a novel candidate gene encoding the carboxypeptidase X member 2 (CPXM2) was found to be associated with hypertension …
CPXM1 correlates to poor prognosis and immune cell infiltration in gastric cancer.
Gu Q, Mi L, Lai C, Guan X, Lu N, Zhan T, Wang G, Lu C, Xu L, Gao X, Zhang J. Gu Q, et al. Heliyon. 2023 Nov 11;10(3):e21909. doi: 10.1016/j.heliyon.2023.e21909. eCollection 2024 Feb 15. Heliyon. 2023. PMID: 38314284 Free PMC article.
BACKGROUND: Gastric cancer (GC) is the fourth most common cause of cancer-related death and the fifth most frequent malignant cancer, especially advanced GC. Carboxypeptidase X member 1 (CPXM1) is an epigenetic factor involved in many physiological processes, includ …
BACKGROUND: Gastric cancer (GC) is the fourth most common cause of cancer-related death and the fifth most frequent malignant cancer, especi …
Structural accommodation of ribonucleotide incorporation by the DNA repair enzyme polymerase Mu.
Moon AF, Pryor JM, Ramsden DA, Kunkel TA, Bebenek K, Pedersen LC. Moon AF, et al. Nucleic Acids Res. 2017 Sep 6;45(15):9138-9148. doi: 10.1093/nar/gkx527. Nucleic Acids Res. 2017. PMID: 28911097 Free PMC article.
While most DNA polymerases discriminate against ribonucleotide triphosphate (rNTP) incorporation very effectively, the Family X member DNA polymerase mu (Pol mu) incorporates rNTPs almost as efficiently as deoxyribonucleotides. ...
While most DNA polymerases discriminate against ribonucleotide triphosphate (rNTP) incorporation very effectively, the Family X me
Ribonucleotides and manganese ions improve non-homologous end joining by human Polμ.
Martin MJ, Garcia-Ortiz MV, Esteban V, Blanco L. Martin MJ, et al. Nucleic Acids Res. 2013 Feb 1;41(4):2428-36. doi: 10.1093/nar/gks1444. Epub 2012 Dec 28. Nucleic Acids Res. 2013. PMID: 23275568 Free PMC article.
Human DNA polymerase mu (Polmu), a family X member involved in DNA repair, has both template-directed and terminal transferase (template-independent) activities. ...
Human DNA polymerase mu (Polmu), a family X member involved in DNA repair, has both template-directed and terminal transferase …
A closed conformation for the Pol lambda catalytic cycle.
Garcia-Diaz M, Bebenek K, Krahn JM, Kunkel TA, Pedersen LC. Garcia-Diaz M, et al. Nat Struct Mol Biol. 2005 Jan;12(1):97-8. doi: 10.1038/nsmb876. Epub 2004 Dec 19. Nat Struct Mol Biol. 2005. PMID: 15608652
Pol lambda is a family X member believed to fill short gaps during DNA repair. Here we report crystal structures of Pol lambda representing three steps in filling a single-nucleotide gap. ...
Pol lambda is a family X member believed to fill short gaps during DNA repair. Here we report crystal structures of Pol lambda …
A structural solution for the DNA polymerase lambda-dependent repair of DNA gaps with minimal homology.
Garcia-Diaz M, Bebenek K, Krahn JM, Blanco L, Kunkel TA, Pedersen LC. Garcia-Diaz M, et al. Mol Cell. 2004 Feb 27;13(4):561-72. doi: 10.1016/s1097-2765(04)00061-9. Mol Cell. 2004. PMID: 14992725 Free article.
Human DNA polymerase lambda (Pol lambda) is a family X member with low frameshift fidelity that has been suggested to perform gap-filling DNA synthesis during base excision repair and during repair of broken ends with limited homology. ...
Human DNA polymerase lambda (Pol lambda) is a family X member with low frameshift fidelity that has been suggested to perform …
Limited terminal transferase in human DNA polymerase mu defines the required balance between accuracy and efficiency in NHEJ.
Andrade P, Martín MJ, Juárez R, López de Saro F, Blanco L. Andrade P, et al. Proc Natl Acad Sci U S A. 2009 Sep 22;106(38):16203-8. doi: 10.1073/pnas.0908492106. Epub 2009 Sep 4. Proc Natl Acad Sci U S A. 2009. PMID: 19805281 Free PMC article.
DNA polymerase mu (Polmu) is a family X member implicated in DNA repair, with template-directed and terminal transferase (template-independent) activities. ...
DNA polymerase mu (Polmu) is a family X member implicated in DNA repair, with template-directed and terminal transferase (temp …
16 results