Biological Sciences / Biochemistry -- New results matching your topic search. https://www.pnas.org/action/doSearch?af=R Proceedings of the National Academy of Sciences: Biochemistry Proceedings of the National Academy of Sciences en-US http://www.atypon.com/images/atypon_logo_small.gif http://www.atypon.com https://www.pnas.org/doi/abs/10.1073/pnas.2513997123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. <br/>SignificanceRecluse spider venoms carry a unique toxin that is not found in other spider venoms and triggers a medical syndrome called loxoscelism, which can involve severe localized skin and tissue damage as well as systemic effects. The toxin is an ... Spider venom phospholipase D toxin structure: Interfacial binding site, mechanism, activation, and head group preference doi:10.1073/pnas.2513997123 2026-04-06T07:00:00Z Alexandra K. SundmanGreta J. BinfordWilliam R. MontfortMatthew H. J. CordesaDepartment of Chemistry and Biochemistry, University of Arizona, Tucson, AZ 85701bDepartment of Biology, Lewis & Clark College, Portland, OR 97219 Proceedings of the National Academy of Sciences 123 15 2026-04-14T07:00:00Z 2026-04-14T07:00:00Z 10.1073/pnas.2513997123 https://www.pnas.org/doi/abs/10.1073/pnas.2513997123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2526136123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. <br/>SignificanceHeat shock proteins 70 (Hsp70) are central hubs of cellular proteostasis networks. Their biological functions are enabled by the large conformational changes these chaperones undergo as they hydrolyze ATP in their nucleotide-binding domain and ... mtHsp70 chaperone converts mitochondrial proteostasis stress into impaired protein import doi:10.1073/pnas.2526136123 2026-04-09T07:00:00Z Rupa BanerjeeVanessa TrauschkeNils BertramIna AretzChristof OsmanDon C. LambDejana MokranjacaBiomedical Center, Physiological Chemistry, Ludwig-Maximilians-Universität München, Martinsried 82152, GermanybPhysical Chemistry, Department of Chemistry and Center for NanoScience, Ludwig-Maximilians-Universität München, Munich 81377, GermanycBiozentrum, Cell Biology, Ludwig-Maximilians-Universität München, Martinsried 82152, Germany Proceedings of the National Academy of Sciences 123 15 2026-04-14T07:00:00Z 2026-04-14T07:00:00Z 10.1073/pnas.2526136123 https://www.pnas.org/doi/abs/10.1073/pnas.2526136123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2526665123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. <br/>SignificanceProtein-based marine adhesives produced by biological organisms are an important source of inspiration for design of underwater and biomedical glues. However, this requires a deep understanding of relationships between their composition, ... Nanocondensate bioadhesive delivery via metal–halogenated catechol coordination in tunicate rhizoid holdfasts doi:10.1073/pnas.2526665123 2026-04-08T07:00:00Z Hyungbin KimSeunghyeon LeeSamantha JeeGeonho SongDorian SchoenaersJérôme DelroissePatrick FlammangMatthew J. HarringtonDong Soo HwangaSchool of Interdisciplinary Bioscience and Bioengineering, Pohang University of Science and Technology, Pohang 37673, Republic of KoreabDivision of Environmental Science and Engineering, Pohang University of Science and Technology, Pohang 37673, Republic of KoreacDepartment of Chemistry, McGill University, Montreal, QC H3A 0B8, CanadadDepartment of Chemical Engineering, Pohang University of Science and Technology, Pohang 37673, Republic of KoreaeDepartment of Biomaterials, Max Planck Institute of Colloids and Interfaces, Potsdam14424, GermanyfBiology of Marine Organisms and Biomimetics Unit, Research Institute for Biosciences, University of Mons, Mons 7000, Belgium Proceedings of the National Academy of Sciences 123 15 2026-04-14T07:00:00Z 2026-04-14T07:00:00Z 10.1073/pnas.2526665123 https://www.pnas.org/doi/abs/10.1073/pnas.2526665123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2605594123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 15, April 2026. <br/>SignificanceThe Arg/N-degron pathway of the yeastSaccharomyces cerevisiaetargets proteins for degradation via its targeting complex that contains the Ubr1/Ufd4 E3 ubiquitin ligases. Ubr1 E3 recognizes destabilizing N-terminal residues (N-degrons) of ... A C-degron regulates Chk1 kinase by allowing stability of inactive Chk1 and by making it short- lived upon activation doi:10.1073/pnas.2605594123 2026-04-07T07:00:00Z Jang-Hyun OhJu-Yeon HyunShun-Jia ChenAlexander VarshavskyaDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA 91125 Proceedings of the National Academy of Sciences 123 15 2026-04-14T07:00:00Z 2026-04-14T07:00:00Z 10.1073/pnas.2605594123 https://www.pnas.org/doi/abs/10.1073/pnas.2605594123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2528216123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 14, April 2026. <br/>SignificanceMisfolding of cystic fibrosis transmembrane conductance regulator (CFTR) underlies cystic fibrosis, and its complex, multidomain architecture makes it an ideal model for understanding how membrane proteins fold and how small molecules can ... Single-molecule dissection of CFTR folding defects and pharmacological rescue doi:10.1073/pnas.2528216123 2026-03-31T07:00:00Z Sang Ah KimJesper LevringJue ChenTae-Young YoonaSchool of Biological Sciences and Institute for Molecular Biology and Genetics, Seoul National University, Seoul 08826, South KoreabLaboratory of Membrane Biology and Biophysics, The Rockefeller University, New York, NY 10065cHHMI, Chevy Chase, MD 20815 Proceedings of the National Academy of Sciences 123 14 2026-04-07T07:00:00Z 2026-04-07T07:00:00Z 10.1073/pnas.2528216123 https://www.pnas.org/doi/abs/10.1073/pnas.2528216123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2532672123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 14, April 2026. <br/>SignificanceRibosomally synthesized and posttranslationally modified peptides (RiPPs) are a superfamily of natural products that display antibiotic, antifungal, anticancer, and metal-binding activities. Their biosynthesis typically follows a common logic ... Co-opting the bacterial lipoprotein pathway for the biosynthesis of lipidated macrocyclic peptides doi:10.1073/pnas.2532672123 2026-03-30T07:00:00Z Jeff Y. ChenLingyang ZhuKevin Y. ZhangDeborah A. BertholdWilfred A. van der DonkaDepartment of Chemistry and HHMI, University of Illinois at Urbana−Champaign, Urbana, IL 61801bCarl R. Woese Institute for Genomic Biology, University of Illinois at Urbana-Champaign, Urbana, IL 61801cSchool of Chemical Sciences, Nuclear Magnetic Resonance Laboratory, University of Illinois at Urbana-Champaign, Urbana, IL 61801 Proceedings of the National Academy of Sciences 123 14 2026-04-07T07:00:00Z 2026-04-07T07:00:00Z 10.1073/pnas.2532672123 https://www.pnas.org/doi/abs/10.1073/pnas.2532672123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2534936123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 14, April 2026. <br/>SignificanceThe outer membrane of Gram-negative bacteria contains a wide variety of integral β-barrel proteins. Here, we study the conserved β-barrel assembly machine which is responsible for folding and inserting these membrane β-barrels. By determining ... Structures of folding intermediates on BAM show diverse substrates fold by a conserved mechanism doi:10.1073/pnas.2534936123 2026-04-02T07:00:00Z Benjamin D. ThomsonMelissa D. MarquezShaun RawsonThiago M. A. dos SantosStephen C. HarrisonDaniel KahneaDepartment of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138bDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115cHHMI, Boston, MA 02115 Proceedings of the National Academy of Sciences 123 14 2026-04-07T07:00:00Z 2026-04-07T07:00:00Z 10.1073/pnas.2534936123 https://www.pnas.org/doi/abs/10.1073/pnas.2534936123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2504045123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. <br/>SignificanceInfluenza remains a major global health threat. We introduce oseltamivir-based aziridines that unite transition-state mimicry for tight binding with aziridine-enabled covalent capture of the catalytic tyrosine. This dual function yields potent,... Oseltamivir aziridines are potent influenza neuraminidase inhibitors and imaging agents doi:10.1073/pnas.2504045123 2026-03-23T07:00:00Z Merijn B. L. VriendsElisha MoranMartín CalveloThomas HansenIsabelle B. PicklesXincheng XinMarieke BiezenoZachary W. B. ArmstrongMaria J. FerrazLei LiAlice LilleyRuth HarveyDmitri V. FilippovQinghua LiaoSybrin P. SchröderGijsbert A. van der MarelMarta ArtolaJohannes M. F. G. AertsJames N. BlazaJeroen D. C. CodéeCarme RoviraHerman S. OverkleeftGideon J. DaviesaDepartment of Bio-organic Synthesis, Leiden Institute of Chemistry, Leiden University, Leiden 2300 RA, The NetherlandsbDepartment of Chemistry, University of York Heslington, York YO10 5DD, United KingdomcDepartament de Química Inorgaǹica i Orgaǹica (Seccióde Química Orgaǹica) and Institut de Química TeorÌica I Computacional, Universitat de Barcelona, Barcelona 08028, SpaindFundació Catalana de Recerca i Estudis Avancats, Barcelona 08010, SpaineDepartment of Medical Biochemistry, Leiden Institute of Chemistry, Leiden University, Leiden 2300 RA, The NetherlandsfWorldwide Influenza Centre, The Francis Crick Institute, London NW1 1AT, United Kingdom Proceedings of the National Academy of Sciences 123 13 2026-03-31T07:00:00Z 2026-03-31T07:00:00Z 10.1073/pnas.2504045123 https://www.pnas.org/doi/abs/10.1073/pnas.2504045123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2514681123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. <br/>SignificanceThis study establishes an integrated workflow from the identification of a high-affinity aptamer (CW06) to the identification of its target, SLC25A24. We further reveal a therapeutic mechanism wherein the aptamer exerts antitumor effects by ... Identifying a cancer therapeutic target: Cell-SELEX identifies a membrane protein for aptamer-mediated growth suppression doi:10.1073/pnas.2514681123 2026-03-23T07:00:00Z Wei CuiHang XiaoXiaohong WenChen LiSuxia BaoJiahao ZengYangbing LiYan QiaoKemin WangHonghui WangJin HuangQiuping GuoaState Key Laboratory of Chemo and Biosensing, Hunan University, Changsha 410082, People’s Republic of ChinabCollege of Biology, Hunan University, Changsha 410082, People’s Republic of ChinacKey Laboratory for Bio-Nanotechnology and Molecular Engineering of Hunan Province, Hunan University, Changsha 410082, People’s Republic of ChinadCollege of Chemistry and Chemical Engineering, Hunan University, Changsha 410082, People’s Republic of ChinaeDepartment of Pathophysiology, School of Basic Medical Sciences, Zhengzhou University, Zhengzhou 450001, People’s Republic of ChinafHunan Research Center of the Basic Discipline for Cell Signaling, Hunan University, Changsha 410082, People’s Republic of China Proceedings of the National Academy of Sciences 123 13 2026-03-31T07:00:00Z 2026-03-31T07:00:00Z 10.1073/pnas.2514681123 https://www.pnas.org/doi/abs/10.1073/pnas.2514681123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2523453123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. <br/>SignificanceBacterial ribosomal RNA (rRNA) methylations are important for ribosome function and antibiotic sensitivity, but little is known about how they are incorporated during ribosome biogenesis. Using single-particle cryo-EM and complementary ... Mechanism of 30S subunit recognition and modification by the conserved bacterial ribosomal RNA methyltransferase RsmI doi:10.1073/pnas.2523453123 2026-03-24T07:00:00Z Mohamed I. BarmadaErin N. McGinitySuparno NandiDebayan DeyNatalia ZelinskayaGeorge M. HarrisLindsay R. ComstockChristine M. DunhamGraeme L. ConnaDepartment of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322bGraduate Program in Biochemistry, Cell and Developmental Biology, Graduate Division of Biological and Biomedical Sciences, Emory University, Atlanta, GA 30322cDepartment of Chemistry, Wake Forest University, Winston-Salem, NC 27106dDepartment of Chemistry, Emory University, Atlanta, GA 30322 Proceedings of the National Academy of Sciences 123 13 2026-03-31T07:00:00Z 2026-03-31T07:00:00Z 10.1073/pnas.2523453123 https://www.pnas.org/doi/abs/10.1073/pnas.2523453123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2529493123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. <br/>SignificanceThis study describes “Inside-Out” (I-O) proteins, a class of intracellular proteins that translocate to the cell surface under stress or disease conditions through a mechanism distinct from conventional secretion pathways. I-O proteins are ... Dynamic translocation of Inside-Out proteins to the cell surface underlies cellular adaptation to cancer-induced stress doi:10.1073/pnas.2529493123 2026-03-24T07:00:00Z Tomasz SlezakKelly M. O’LearyTanya Guevara AvellaNatalia MusialJinyang LiAnna AndrzejczakElizabeth F. ScottDuc Anh LeAnthony A. KossiakoffaDepartment of Biochemistry and Molecular Biology, The University of Chicago, Chicago, IL 60637bIntercollegiate Faculty of Biotechnology, University of Gdansk and Medical University of Gdansk, Gdańsk 80-307, PolandcDepartment of Experimental Therapy, Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Wrocław 53-114, PolanddInstitute for Biophysical Dynamics, The University of Chicago, Chicago, IL 60637 Proceedings of the National Academy of Sciences 123 13 2026-03-31T07:00:00Z 2026-03-31T07:00:00Z 10.1073/pnas.2529493123 https://www.pnas.org/doi/abs/10.1073/pnas.2529493123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2535016123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. <br/>SignificanceLegionella pneumophilaremodels host membrane trafficking to establish a replication-permissive niche, yet the molecular basis of this process is not fully understood. Here, we elucidate the structural basis by which the effector SetA couples ... Structural insights into SetA-mediated Rab1 glucosylation and PI3P-guided localization during early Legionella infection doi:10.1073/pnas.2535016123 2026-03-27T07:00:00Z Ha Na ImYeon LeeYunju SongHyunggu HahnHyerry JeonDonghyuk ShinSangho LeeKyung-Hee KimKyung-Tae KimSe Won SuhDong Man JangHyoun Sook KimaResearch Institute, National Cancer Center, Goyang 10408, Republic of KoreabDepartment of Chemistry, College of Natural Sciences, Seoul National University, Seoul 08826, Republic of KoreacDepartment of Biomedical Sciences, Seoul National University, Seoul 03080, Republic of KoreadDepartment of Systems Biology, College of Life Science and Biotechnology, Yonsei University, Seoul 03722, Republic of KoreaeDepartment of Biological Sciences, Sungkyunkwan University, Suwon 16419, Republic of KoreafDepartment of Applied Chemistry, School of Science and Technology, Kookmin University, Seoul 02707, Republic of KoreagDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115 Proceedings of the National Academy of Sciences 123 13 2026-03-31T07:00:00Z 2026-03-31T07:00:00Z 10.1073/pnas.2535016123 https://www.pnas.org/doi/abs/10.1073/pnas.2535016123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2603894123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 13, March 2026. <br/> Alternative splicing rewires banana aroma biosynthesis doi:10.1073/pnas.2603894123 2026-03-23T07:00:00Z Adam JozwiakaDepartment of Botany and Plant Sciences, University of California Riverside, Riverside, CA 92521bInstitute for Integrative Genome Biology, University of California Riverside, Riverside, CA 92521 Proceedings of the National Academy of Sciences 123 13 2026-03-31T07:00:00Z 2026-03-31T07:00:00Z 10.1073/pnas.2603894123 https://www.pnas.org/doi/abs/10.1073/pnas.2603894123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2520070123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 12, March 2026. <br/>SignificanceWhile nature has evolved enzymes to carry out a vast array of chemical transformations, selecting the ideal protein to initiate an enzyme engineering campaign often presents a significant challenge, slowing progress across biocatalysis and ... Dual-encoder contrastive learning accelerates enzyme discovery doi:10.1073/pnas.2520070123 2026-03-17T07:00:00Z Jason W. RocksDat P. TruongDmitrij RappoportSamuel Maddrell-ManderDaniel A. Martin-AlarconToni M. LeeSteven CrossanJoshua E. GoldfordaDayhoff Labs, Inc., Cambridge, MA 02140 Proceedings of the National Academy of Sciences 123 12 2026-03-24T07:00:00Z 2026-03-24T07:00:00Z 10.1073/pnas.2520070123 https://www.pnas.org/doi/abs/10.1073/pnas.2520070123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2520462123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 12, March 2026. <br/>SignificanceHuntingtin is a large, essential protein with conserved roles in development, intracellular trafficking, and protein homeostasis, yet its precise molecular functions remain incompletely defined. Here, we report high-affinity, selective, and ... High-affinity, structure-validated and selective macrocyclic peptide tools for chemical biology studies of Huntingtin doi:10.1073/pnas.2520462123 2026-03-16T07:00:00Z Rebeka FantiEsther WolfTatsuya IkenoueJustin C. DemeSwati BalakrishnanBrandon A. KeithMatthew G. AlteenRenu ChandrasekaranManisha YadavRitika BhajiawalaSuzanne AcklooJia FengMahmoud A. PouladiAled M. EdwardsDerek J. WilsonSusan M. LeaHiroaki SugaRachel J. HardingaStructural Genomics Consortium, University Health Network, Toronto, ON M5G 1L7, CanadabDepartment of Molecular Genetics, Faculty of Medicine, University of Toronto, Toronto, ON M5S 1A8, CanadacLeslie Dan Faculty of Pharmacy, University of Toronto, Toronto, ON M5S 3M2, CanadadDepartment of Chemistry, Graduate School of Science, The University of Tokyo, Tokyo 113-0033, JapaneCenter for Structural Biology, Center for Cancer Research, National Cancer Institute, Frederick, MD 21702fDepartment of Medical Biophysics, University of Toronto, Toronto, ON M5G1L7, CanadagDepartment of Medical Genetics, Vancouver, BC V5Z 4H4, CanadahCentre for Molecular Medicine and Therapeutics, Vancouver, BC V5Z 4H4, CanadaiDjavad Mowafaghian Centre for Brain Health, University of British Columbia, Vancouver, BC V6T 1Z3, CanadajEdwin S.H Leong Centre for Healthy Aging, University of British Columbia, Vancouver, BC V6T 1Z3, CanadakBC Children’s Hospital Research Institute, Vancouver, BC V5Z 4H4, CanadalDepartment of Chemistry, York University, Toronto, ON M3J 1P3, CanadamDepartment of Pharmacology and Toxicology, Faculty of Medicine, University of Toronto, Toronto, ON M5S 1A8, CanadanPrincess Margaret Cancer Centre, Toronto, ON M5G 2C4, Canada Proceedings of the National Academy of Sciences 123 12 2026-03-24T07:00:00Z 2026-03-24T07:00:00Z 10.1073/pnas.2520462123 https://www.pnas.org/doi/abs/10.1073/pnas.2520462123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2527162123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 12, March 2026. <br/>SignificanceThe hepatic JUN NH2-terminal kinase (JNK) exhibits mutually exclusive alternative pre-mRNA splicing that results in the expression of JNK spliceoforms. We show that the hepatic adaptive response to the consumption of a high fat diet requires ... Mutually exclusive alternative pre-mRNA splicing promotes adaptive metabolic stress signaling by JNK doi:10.1073/pnas.2527162123 2026-03-17T07:00:00Z Alexandra LeeAutumn GentzlerDeclan FitzpatrickSithara Raju PonnyOzkan AydemirMyoung Sook HanCaroline A. LewisGuangping GaoRoger J. DavisaProgram in Molecular Medicine, University of Massachusetts Chan Medical School, Worcester, MA 01605bHorae Gene Therapy Center, Department of Genetic and Cellular Medicine, University of Massachusetts Chan Medical School, Worcester, MA 01605 Proceedings of the National Academy of Sciences 123 12 2026-03-24T07:00:00Z 2026-03-24T07:00:00Z 10.1073/pnas.2527162123 https://www.pnas.org/doi/abs/10.1073/pnas.2527162123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2529780123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 12, March 2026. <br/>SignificancePeptides synthesized at the ribosome and then posttranslationally modified by enzymes constitute an important class of natural products with antibiotic and antiviral properties. An important type of posttranslational modification is the ... The radical SAM enzyme EpeE exhibits distinct site reactivity during the biosynthesis of the RiPP natural product epipeptide doi:10.1073/pnas.2529780123 2026-03-18T07:00:00Z William G. WallsHao YangMadeline B. HoWilliam E. BroderickBrian M. HoffmanJoan B. BroderickaDepartment of Chemistry & Biochemistry, Montana State University, Bozeman, MT 59717bDeparment of Chemistry, Northwestern University, Evanston, IL 60208 Proceedings of the National Academy of Sciences 123 12 2026-03-24T07:00:00Z 2026-03-24T07:00:00Z 10.1073/pnas.2529780123 https://www.pnas.org/doi/abs/10.1073/pnas.2529780123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2530575123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 12, March 2026. <br/>SignificanceMycobacterium tuberculosisand related pathogens possess an unusual cell wall, rich in mycolic acid, that protects them from antibiotics and the host immune system. This study presents the structure of the mycobacterial long-chain acyl-CoA ... Structural basis for substrate specificity and MSMEG_0435-0436 binding by the mycobacterial long-chain acyl-CoA carboxylase complex doi:10.1073/pnas.2530575123 2026-03-17T07:00:00Z Yingke LiangStephanie A. BuelerJohn L. RubinsteinaMolecular Medicine Program, The Hospital for Sick Children, Toronto, ON M5G 0A4, CanadabDepartment of Biochemistry, The University of Toronto, Toronto, ON M5S 1A8, CanadacDepartment of Medical Biophysics, The University of Toronto, Toronto, ON M5G 2C4, Canada Proceedings of the National Academy of Sciences 123 12 2026-03-24T07:00:00Z 2026-03-24T07:00:00Z 10.1073/pnas.2530575123 https://www.pnas.org/doi/abs/10.1073/pnas.2530575123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2530653123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 12, March 2026. <br/>SignificanceAntibody-based therapies rely not only on antigen binding but also on effector functions such as antibody-dependent cellular cytotoxicity (ADCC) and complement-dependent cellular phagocytosis (CDCP), both of which are strongly shaped by the ... Selective fluorination of Fc glycans enhances antibody-mediated effector functions doi:10.1073/pnas.2530653123 2026-03-18T07:00:00Z Xianyang WangMargaryta GomozkovaSiqi LiBiswarup BanerjeeGuanghui ZongDominique MissiakasLai-Xi WangaDepartment of Chemistry and Biochemistry, University of Maryland, College Park, MD 20742bDepartment of Microbiology, The University of Chicago, Chicago, IL 60637 Proceedings of the National Academy of Sciences 123 12 2026-03-24T07:00:00Z 2026-03-24T07:00:00Z 10.1073/pnas.2530653123 https://www.pnas.org/doi/abs/10.1073/pnas.2530653123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2607090123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 12, March 2026. <br/> Correction for Guo et al., A ribosomally synthesized and posttranslationally modified peptide with ADP-ribosylation doi:10.1073/pnas.2607090123 2026-03-16T07:00:00Z Proceedings of the National Academy of Sciences 123 12 2026-03-24T07:00:00Z 2026-03-24T07:00:00Z 10.1073/pnas.2607090123 https://www.pnas.org/doi/abs/10.1073/pnas.2607090123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2515301123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 11, March 2026. <br/>SignificanceDuring banana fruit ripening, the two feedback-inhibited, rate-limiting enzymes of the valine and leucine biosynthetic pathway are simultaneously alternatively spliced, effectively losing their feedback regulation and promoting carbon flux ... Banana aroma is a result of acetohydroxyacid synthase and isopropylmalate synthase alternative isoforms that bypass feedback inhibition doi:10.1073/pnas.2515301123 2026-03-09T07:00:00Z Philip EngelgauRandolph M. BeaudryaDepartment of Horticulture, Michigan State University, East Lansing, MI 48824 Proceedings of the National Academy of Sciences 123 11 2026-03-17T07:00:00Z 2026-03-17T07:00:00Z 10.1073/pnas.2515301123 https://www.pnas.org/doi/abs/10.1073/pnas.2515301123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2515348123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 11, March 2026. <br/>SignificanceAerobic respiration in bacteria is a versatile and highly adaptable process, with many species encoding multiple terminal oxidases catalyzing the reduction of oxygen to water. Terminal oxidases belong to two major families: the heme-copper ... The Mycobacterium smegmatis bd-II terminal oxidase employs a carboxylate shift mechanism doi:10.1073/pnas.2515348123 2026-03-10T07:00:00Z Terezia KovalovaMateusz JanczakAna P. Gamiz-HernandezDaniel LundinSoni SharmaJohanna VilhjálmsdóttirDan SjöstrandVille R. I. KailaMartin HögbomPia ÄdelrothaDepartment of Biochemistry and Biophysics, Stockholm University, Stockholm 116 91, Sweden Proceedings of the National Academy of Sciences 123 11 2026-03-17T07:00:00Z 2026-03-17T07:00:00Z 10.1073/pnas.2515348123 https://www.pnas.org/doi/abs/10.1073/pnas.2515348123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2533320123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 11, March 2026. <br/> Cryo-EM maps of human DNA polymerase ε should be reevaluated in light of its unexpected behavior in vitro doi:10.1073/pnas.2533320123 2026-03-06T08:00:00Z Johann J. RoskeJoseph T. P. YeelesaMedical Research Council, Protein and Nucleic Acid Chemistry Division Division, Laboratory of Molecular Biology, Cambridge CB2 0QH, United Kingdom Proceedings of the National Academy of Sciences 123 11 2026-03-17T07:00:00Z 2026-03-17T07:00:00Z 10.1073/pnas.2533320123 https://www.pnas.org/doi/abs/10.1073/pnas.2533320123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2535727123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 11, March 2026. <br/> Reply to Roske and Yeeles: Mismatch correction by a replicative polymerase constrained on DNA by a ring doi:10.1073/pnas.2535727123 2026-03-06T08:00:00Z Feng WangQing HeMichael E. O’DonnellHuilin LiaDepartment of Structural Biology, Van Andel Institute, Grand Rapids, MI 49503bLaboratory of DNA Replication, The Rockefeller University, New York, NY 10065cHHMI, The Rockefeller University, New York, NY 10065 Proceedings of the National Academy of Sciences 123 11 2026-03-17T07:00:00Z 2026-03-17T07:00:00Z 10.1073/pnas.2535727123 https://www.pnas.org/doi/abs/10.1073/pnas.2535727123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2537453123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 11, March 2026. <br/>SignificanceWhile many aquatic organisms evolved strategies to adhere to surfaces underwater, current synthetic biocompatible adhesives lack reliable strength in aqueous conditions. Investigating freshwater mussel adhesive proteins expands the current ... Identification and characterization of a wet adhesive protein extracted from Dreissena bugensis, the freshwater quagga mussel doi:10.1073/pnas.2537453123 2026-03-09T07:00:00Z Angelico R. ObilleRida HasanDavid J. ReesJudith NgZhi Yi WangRaunaq BagchiKeryn LianKarina M. M. CarneiroEli D. SoneaInstitute of Biomedical Engineering, University of Toronto, Toronto, ON M5S 3G9, CanadabDepartment of Materials Science & Engineering, University of Toronto, Toronto, ON M5S 3E4, CanadacFaculty of Dentistry, University of Toronto, Toronto, ON M5G 1G6, Canada Proceedings of the National Academy of Sciences 123 11 2026-03-17T07:00:00Z 2026-03-17T07:00:00Z 10.1073/pnas.2537453123 https://www.pnas.org/doi/abs/10.1073/pnas.2537453123?af=R https://www.pnas.org/doi/abs/10.1073/pnas.2606204123?af=R Proceedings of the National Academy of Sciences, Volume 123, Issue 11, March 2026. <br/> Correction for Jaen Maisonet et al., Small-molecule allosteric activator of ubiquitin-specific protease 7 (USP7) doi:10.1073/pnas.2606204123 2026-03-11T07:00:00Z Proceedings of the National Academy of Sciences 123 11 2026-03-17T07:00:00Z 2026-03-17T07:00:00Z 10.1073/pnas.2606204123 https://www.pnas.org/doi/abs/10.1073/pnas.2606204123?af=R