My NIH bibliography: https://www.ncbi.nlm.nih.gov/myncbi/1vQQppz6ku6swy/bibliography/public/
Publications
2024
17. Adolph, MB., Cortez D. (2024). Mechanisms and Regulation of Replication Fork Reversal. DNA repair. 2024 Sep:141:103731. PMID: 39089193
16. Balakrishnan, S., Adolph, MB., Tsai, MS., Gallagher, K., Cortez, D., Chazin, WJ. (2024). A structure based mechanism for the regulation of RAD51 by RADX. PNAS. 121 (12) e2316491121. PMID: 38466836
2023
15. Adolph, MB., Garje, AS., Balakrishnan, S., Morati, F., Modesti, M., Chazin WJ., Cortez D. (2023). CRISPR-dependent base editing screens identify separation of function mutants of RADX with altered RAD51 regulatory activity. J.Mol.Bio. 2023 Aug 10:168236. PMID: 37572935
2022
14. Mohamed, T., Adolph, MB., Modesti, M., Cortez D. (2022). RADX forms oligomers to maintain replication fork stability. J. Biol. Chem: 298(3):101672. PMID: 35120927.
2021
13. Krishnamoorthy, A., Jackson, J., Mohamed T., Adolph MB., Vindigni, A., Cortez, D, (2021). RADX prevents genome instability by confining replication fork reversal to stalled forks. Mol. Cell. 81(14): 3007-3017.e5. PMID: 34107305
12. Adolph, MB., Mohamed TM., Balakrishnan S., Xue C., Morati F., Modesti M., Greene EC., Chazin W.J., Cortez D. (2021). RADX controls RAD51 filament dynamics to regulate replication fork stability. Mol. Cell, 81(5):1074-1083. PMID: 33453169
2020
11. Conner KL., Shaik AN., Marshall KA., Floyd AM., Ekinci, E, Lindquist J, Sawant A, Lei W, Adolph MB, Chelico L, Siriwardena SU, Bhagwat A, Kim S, Cote ML, Patrick SM. (2020). APOBEC3 enzymes mediate efficacy of cisplatin and are epistatic with base excision repair and mismatch repair in platinum response. NAR Cancer, 2(4):zcaa033. PMID: 33196045
10. McDaniel, Y.Z., Wang, D., Love, RP., Adolph, MB., Mohammadzadeh N., Linda Chelico, L., Mansky, L.M. (2020). Deamination hotspots among APOBEC3 family members are defined by both target site sequence context and ssDNA secondary structure. Nucl. Acids Res., 48(3): 1353-1371. PMID: 31943071
2019
9. Adolph, MB., Ara, A., Chelico, L. (2019). APOBEC3 host restriction factors of HIV-1 can change the template switching frequency of reverse transcriptase. J.Mol. Biol. 431(7):1339-1352. PMID: 30797859
2018
8. Adolph, MB., Love RP., Chelico L. (2018). Biochemical basis of APOBEC3 deoxycytidine deaminase activity on diverse DNA substrates. ACS Infect. Dis., 4(3):224-238. PMID: 29347817
2017
7. Adolph, MB., Love, RP., Feng, Y., Chelico L. (2017). Enzyme cycling contributes to efficient induction of genome mutagenesis by the cytidine deaminase APOBEC3B. Nucl. Acids Res., 45(20): 11925-11940. PMID: 28981865
6. Adolph, MB., Ara, A., Feng, Y., Wittkopp, CJ., Emerman, M., Fraser, JS., Chelico L. (2017). Cytidine deaminase efficiency of the lentiviral viral restriction factor APOBEC3C correlates with dimerization. Nucl. Acids Res., 45(6): 3378-3394. PMID: 28158858
5. Ara, A., Love RP., Follack, TB., Ahmed, K., Adolph, MB., Chelico, L. (2017). Mechanism of enhanced HIV restriction by virion coencapsidated cytidine deaminases APOBEC3F and APOBEC3G. J. Virol., 91(3) e02230-16. PMID: 27881650
2016
4. Wittkopp, CJ., Adolph MB., Wu, LI., Chelico L., Emerman, M. (2016). A single nucleotide polymorphism in human APOBEC3C enhances restriction of lentivirus. PLoS Path., 12(10):e1005865. PMID: 27732658
3. Starrett, GJ., Luengas, EM., McCann, JL., Ebrahimi, D., Tezmiz NA., Lov, RP., Feng, Y., Adolph, MB., Chelico, L., Law, EK., Carpenter, MA., Harris, RS. (2016). The DNA cytosine deaminase APOBEC3H haplotype I likely contributes to breast and lung cancer mutagenesis. Nat. Commun., 7:12918. PMID: 27650891
2015
2. Feng, Y., Love, RP., Ara, A., Baig, TT., Adolph, MB., Chelico L. (2015). Natural polymorphisms and oligomerization of human APOBEC3H contribute to single-stranded DNA scanning ability. J. Biol. Chem., 290(45):27188-203. PMID: 26396192
2013
1. Adolph, M.B., Webb, J., and Chelico L. (2013) Retroviral Restriction Factor APOBEC3G Delays the Initiation of DNA Synthesis by HIV-1 Reverse Transcriptase. PLoS ONE, 8(5), e64196. PMID: 23717565