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2025
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2025
- Book : ()
- Pub. Date : 2025
- Page : pp.101785-101785
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2025
- Book : ()
- Pub. Date : 2025
- Page : pp.101712-101712
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2025
Using the color dipole picture for photon-nucleus interactions at small x together with the color glass condensate (CGC) effective theory, we demonstrate that the next-to-leading (NLO) order corrections to the cross section for the inclusive production of a pair of hard jets encode not only the Jalilian-Marian, Iancu, McLerran, Weigert, Leonidov and Kovner (JIMWLK) evolution with decreasing x, but also the Dokshitzer-Gribov-Lipatov-Altarelli-Parisi (DGLAP) evolution of the gluon distribution function and the Collins-Soper-Sterman (CSS) evolution of the gluon transverse momentum dependent (TMD) distribution. The emergent CSS equation takes the form of a rate equation describing the evolution of the dijet distribution in the transverse momentum imbalance K⊥ when increasing the dijet relative momentum P⊥. All three types of evolution become important when both P⊥ and K⊥ are much larger than the nuclear saturation momentum Qs(x) and we propose a framework which encompasses all of them. The solution to the JIMWLK equation provides the source term for the DGLAP evolution with increasing K⊥, which in turn generates the initial condition for the CSS evolution with increasing P⊥.
Published by the American Physical Society
2025
- Book : 111(7)
- Pub. Date : 2025
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2025
- Book : 124()
- Pub. Date : 2025
- Page : pp.104050-104050
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2025
- Book : 43()
- Pub. Date : 2025
- Page : pp.101923-101923
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2025
- Book : 4(03)
- Pub. Date : 2025
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2025
ABSTRACTHIV-1 exploits host cell post-translation modifications (PTMs) to facilitate production of infectious particles. These modifications include SUMOylation, a dynamically regulated PTM involving covalent attachment of small ubiquitin-like modifiers (SUMOs) to lysine (K) residues of target proteins. SUMOylation modulates the activity of thousands of proteins and multiple fundamental host cellular processes, including pathways hijacked by HIV-1 to promote infection and spread. The SUMOylation of several proteins during HIV-1 infection has been characterized. However, the broad effects of HIV-1 infection on the SUMOylation of the host cell proteome is largely unknown. To date, SUMOylation has not been explored by large-scale proteomics in the context of HIV infection, where many SUMO-regulated host dependency factors remain to be identified. In this study, we performed a proteome-wide, mass spectrometry (MS)-based screen to identify proteins that are SUMOylated during HIV-1 infection. Here, and in immunoprecipitation assays, infection with HIV-1 led to the widespread increased SUMOylation of heterogeneous nuclear ribonucleoprotein (HNRNP) A/B family members. We selected HNRNPA2B1 (A2/B1) and HNRNPA3 for further study. We find that infection with HIV-1 specifically induced the SUMOylation of both proteins by SUMO1 and SUMO2 paralogs in multiple biochemical assays and in multiple human cell lines. Current efforts include generating non-SUMOylatable HNRNPA2B1 and HNRNPA3 mutants to test the functional consequences of their SUMOylation on the splicing of HIV-1 mRNAs. Together, our data point to a novel mechanism involving HIV-1-induced SUMOylation of these host RNA splicing factors as a means to regulate HIV-1 splice variant production. Broadly, our findings suggest that infection with HIV-1 alters the SUMOylation of many unexplored host cellular proteins, and provides a proteomic resource for their future mechanistic study.- Book : ()
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2025
- Book : ()
- Pub. Date : 2025
- Page : pp.1-1
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2025
- Book : ()
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