PUBS | noinajlab

PUBLICATIONS

2023

Srinivasan, K, Erramilli, SK, Chakravarthy, S, Gonzalez, A, Kossiakoff, A, Noinaj N. Characterization of synthetic antigen binding fragments targeting Toc75 for the isolation of TOC in A. thaliana and P. sativum. Structure. S0969-2126(23)00078-3. doi: 10.1016/j.str.2023.03.002.

Cottom, CO, Stephenson, R, Wilson, L, and Noinaj, N. (2023). Targeting BAM for Novel Therapeutics against Pathogenic Gram-Negative Bacteria. Antibiotics. 12(4), 679; DOI: 10.3390/antibiotics12040679

Zhang, C, Zhao, J, Lu, B, Seeman, N, Sha, R, Noinaj, N, and Mao C. (2023). Engineering DNA Crystals toward Studying DNA-Guest Molecule Interactions. J Am Chem Soc. 145(8):4853-4859. doi: 10.1021/jacs.3c00081

Deng, Y, Dong, G, Meng, Y, Noinaj, N, and Huang, R. (2023). Structure-Activity Relationship Studies of Venglustat on NTMT1 Inhibition. Journal of Med. Chem. 66(2):1601-1615. DOI: 10.1021/acs.jmedchem.2c01854

2022

Greenawalt, A, Stoudenmire, J, Lundquist, K, Noinaj, N, Gumbart, J, and Cornelissen, C. (2022). Point Mutations in TbpA Abrogate Human Transferrin Binding in Neisseria gonorrhoeae. Infection and Immunity. 90(11):e0041422. DOI: 10.1128/iai.00414-2.

He, R, Wang, J, Yu, Z, Moyer, J, Dodson, M, Durham, T, Cramer, J, Qian, Y, Lin, A, Wu, L, Noinaj, N, Barrett, D, and Zhang, Z. (2022). Structure-Based Design of Active-Site-Directed, Highly Potent, Selective, and Orally Bioavailable Low-Molecular-Weight Protein Tyrosine Phosphatase Inhibitors. Journal of Med Chem. 65(20):13892-13909. DOI: 10.1021/acs.jmedchem.2c01143

Mukherjee, I, Gabel, C, Noinaj, N, Bondy-Denomy, J, and Chang, L. (2022). Structural basis of AcrIF24 as an anti-CRISPR protein and transcriptional suppressor. Nature Chemical Biology. 18(12):1417-1424. DOI: 10.1038/s41589-022-01137-w

Dong, G, Deng, Y, Yasgar, A, Yadav, R, Talley, D, Zakharov, A, Jain, S, Rai, G, Noinaj, N, Simneonov, A, and Huang, R. (2023). Venglustat Inhibits Protein N-Terminal Methyltransferase in a Substrate-Competitve Manner. Journal of Med. Chem. 65(18):12334-12345. DOI: 10.1021/acs.jmedchem.2c01050

Iyuma, ID, Vilseck, JZ, Yadav, R, Noinaj, N, and Huang, R. (2022). Exploring Unconvetional SAM Analogues to Build Cell-Potent Bisubstrate Inhibitors for Nicotinamide N- methyltransfarase. Angew Chem Int Ed Engl. 61(16):e202114813. DOI: 10.1002/anie.202114813

Bera, AK, Wu, R, Harrison, S, Cornelissen, CN, Chazin, WJ, and Noinaj, N. (2022). TdfH selectively binds metal-loaded tetrameric calprotectin for zinc import. Communications Biology. 5(1), 103. DOI: 10.1038/s42003-022-03039-y

2021

Wu, R, Bakelar, JW, Lunquist, K, Zhang, Z, Kuo, KM, Ryoo, D, Pang, YT, Sun C, White, T, Klose, T, Jiang W, Gumbart, JC, and Noinaj, N. (2021). Plasiticty in the barrel doamin of BamA mediates a hybird-barrel mechanism by BAM. Nature Communications. 12(1) 7131 DOI: 10.1038/s41467-021-27449-4

Yadav, R, Govindan, S, Daczkowski, C, Mesecar, A, Chakravarthy, S, and Noinaj, N. (2021). Structural Insight into the dual function of LbpB in mediating Neisserial pathogenesis. eLife. 10:e71683. DOI: 10.7554/eLife.71683

Chen, D, Meng, Y, Yu, D, Noinaj, N, Cheng, X, and Huang, R. (2021). Chemoproteomic Study Uncovers Hemk2/KMT9 As a New Target for NTMT1 Bi substrate Inhibitors. ACS Chem Biol. 16(7), 1234-1242. DOI: 10.1021/acschembio.1c00279

Billings, E, Lundquist, K, Overly, C, Srinivasan, K, and Noinaj, N. (2021). Structure Determination of Membrane Proteins Using X-ray Crystallography. Methods in Molecular Biology. 2302, 101-136. DOI: 10.1007/978-1-0716-1394-8_7

Chen, D, Dong, G, Deng, Y, Noinaj, N, and Huang, R. (2021). Structure-based Discovery of Cell-Potent Peptidomimetic Inhibitors for Protein N-Terminal Methyltransfrerase 1. ACS Med. Chem. Letters. 12(3), 485-493. DOI: 10.1021/acsmedchemlett.1c00012

Lundquist, K, Billings, E, Bi, M, Wellnitz, J, Noinaj, N. (2021). The assembly of beta-barrel membrane proteins by BAM and SAM. Molecular Microbiology. 115(3), 425-435. DOI: 10.1111/mmi.14666

2020

Mackie, B, Chen, D, Dong, D, Dong, C, Parker, H, Tooley, C, Noinaj, N, Min, Jinrong, and Huang, R. (2020). Selective Peptidomimetic Inhibitors of NTMT1/2: Rational Design, Synthesis, Characterization, and Crystallographic Studies. J. Med. Chem. 63(17), 9512-9522. DOI: 10.1021/acs.jmedchem.0c00689

Chen, D, Dong, C, Dong, G, Srinivasan, K, Min, J, Noinaj, N, and Huang R. (2020). Probing the Plasticity in the Active Site of Protein N-terminal Methyltransferase 1 Using Bisubstrate Analogues. J. Med. Chem. 63(15), 8419-8431. DOI: 10.1021/acs.jmedchem.0c00770

Kammerman, M, Bera, A, Wu, R, Harrison, S, Maxwell, N, Lundquist, K, Noinaj, N, Chazin, W, and Cornelissen, C. (2020). Molecular Insight Into TdfH-Mediated Zinc Piracy From Human Calprotectin by Neisseria Gonorrhoeae. mBio. 11(3). e00949-20. DOI: 10.1128/mBio.00949-20

Yadav, R, Noinaj, N, Ostan, N, Moraes, T, Stoudenmore, J, Maurakis, S, & Cornelissen, CN. (2020). Structural Basis for Evasion of Nutritional Immunity by the Pathogenic Neisseriae. Front Microbiol, 10(2981). DOI: 10.3389/fmicb.2019.02981

Celia, H, Noinaj, N, and Buchanon, SK. (2020). Structure and Stoichiometry of the Ton Molecular Motor. Int Jmol Sci, 21(2), E375. DOI: 10.3390/ijms21020375

2019

Chen, D, Linjie, L, Diaz, K, Iyamu, Iredia, D. Yadav, R. Noinaj N, Huang, R. (2019). Novel Propargyl-Linked Bisubstrate Analogues as Tight-Binding Inhibitors for Nicotinamide N-Methyltransferase. J Med Chem, 62(23), 10783-10797. DOI: 10.1021/acs.jmedchem.9b01255

Imai, Y, Meyer, K. J., Iinishi, A, Favre-Godal, Q, Green, R, Manuse, S, Caboni, M, Mori, M, Niles, S, Ghiglieri, M, Honrao, C, Ma, X, Gou, J, Makrijannis, A, Linares-Otoya, L, Bohringer, N, Wuisan, Z, Kaur, H, Wu, R, Mateus, A, Typas, A, Savitski, M, Espinoza, J, O'Rouke, A, Nelson, K, Hiller, S, Noinaj, N, Schaberle, T, D'Onofrio, A, and Lewis, K. (2019). A new antibiotic selectively kills Gram-negative pathogens. Nature, 576, 459–464. DOI: 10.1038/s41586-019-1791-1

Wu, R. Stephenson, R. Gichaba, A. & Noinaj, N. (2019). The big BAM theory: An open and closed case? Biochimica et Biophysica Acta (BBA) - Biomembranes, 183062. DOI: 10.1016/j.bbamem.2019.183062

Chen, D, Dong, G, Noinaj, N, Huang, R. (2019) Discovery of Bisubstrate Inhibitors for Protein N-Terminal Methyltransferase 1. J Med Chem, 62(7):3773-3779. DOI: 10.1021/acs.jmedchem.9b00206

2018

Ha L, Colquhoun J, Noinaj N, Das C, Dunman P, and Flaherty D. (2018) Crystal structure of the ribonuclease P protein subunit from Staphylococcus aureus. Acta Cryst F , 74(Pt 10):632-637. DOI: 10.1107/S2053230X18011512

Noinaj N and Buchanan SK (Eds.) (2018) Editorial Overview: Membranes and their embedded molecular machines. Current Opinion in Structural Biology - Membranes, 51:vii-viii. DOI: 10.1016/j.sbi.2018.10.005

Lundquist K, Bakelar J, Noinaj N, Gumbart JC. (2018) C-terminal kink formation is required for lateral gating in BamA. PNAS, 115(34):E7942-E7949 . DOI: 10.1073/pnas.1722530115

Sikora AE, Wierzbicki IH, Zielke RA, Ryner RF, Korotkov KV, Buchanan SK, and Noinaj N. (2018) Structural and functional insights into the role of BamD and BamE within the b-barrel assembly machinery in Neisseria gonorrhoeae. JBC, 293(4):1106-1119. DOI: 10.1074/jbc.RA117.000437

2017

O’ Neil P, Richardson LGL, Paila YD, Piszczek G, Chakravarthy S, Noinaj N, Schnell DJ. (2017). The POTRA domains of Toc75 exhibit chaperone-like function to facilitate import into chloroplasts. PNAS, 114(24):E4868-E4876. DOI: 10.1073/pnas.1621179114

Botos I, Noinaj N, and Buchanan SK. (2017). Insertion of proteins and lipopolysaccharide into the bacterial outer membrane. Royal Society Phil. Trans. B, 372(1726). DOI: 10.1098/rstb.2016.0224

Noinaj N, Gumbart JC, and Buchanan SK. (2017). The b-barrel assembly machinery in motion. Nature Reviews Microbiology 15(4):197-204. DOI: 10.1038/nrmicro.2016.191

2016

Bakelar J, Buchanan SK, and Noinaj N. (2016). Structural snapshots of the β-barrel assembly machinery. FEBS 2016 Nov 14. doi: 10.1111/febs.13960. DOI: 10.1111/febs.13960

Celia H, Noinaj N, Zakharov SD, Bordignon E, Botos I, Cramer WA, Lloubes R, and Buchanan SK. (2016). Structural insight into the role of the Ton complex in energy transduction. Nature 538(7623):60-65. DOI: 10.1038/nature19757

Abeykoon AH, Noinaj N, Choi BE, Wise L, He Y, Chao CC, Wang G, Gucek M, Ching WM, Chock PB, Buchanan SK, Yang DC. (2016). Structural Insights into Substrate Recognition and Catalysis in OmpB by Protein Lysine Methyltransferases from Rickettsia. JBC 291(38):19962-74. DOI: 10.1074/jbc.M116.723460

Tinoco AD, Saxena M, Sharma S, Noinaj N, Delgado Y, Quiñones González EP, Conklin SE, Zambrana N, Loza-Rosas SA, Parks TB. (2016). Unusual Synergism of Transferrin and Citrate in the Regulation of Ti(IV) Speciation, Transport, and Toxicity. J Am Chem Soc. 138(17):5659-65. DOI: 10.1021/jacs.6b01966

Bakelar J, Buchanan SK, Noinaj N. (2016). The structure of the β-barrel assembly machinery complex. Science. 351(6269):180-6. DOI: 10.1126/science.aad3460

Noinaj N, Mayclin S, Stanley AM, Jao C, Buchanan SK. (2016). From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins. J. Vis. Exp. (113), e53245, doi:10.3791/53245. DOI: 10.3791/53245

2015

Noinaj N, Rollauer SE, and Buchanan SK. (2015). The b-barrel membrane protein insertase machinery from Gram-negative bacteria. Curr Opin Struct Biol. 2015 Apr;31:35-42. DOI: 10.1016/j.sbi.2015.02.012

Buchanan SK and Noinaj N (Eds). (2015). Methods in Molecular Biology: The BAM complex.

Noinaj N, Kuszak AK, and Buchanan SK. (2015). Heat modifiability of outer membrane proteins from Gram-negative bacteria. Methods in Molecular Biology: The BAM complex 1329:51-6. DOI: 10.1007/978-1-4939-2871-2_4

Kuszak AK, Noinaj N, and Buchanan SK. (2015). Methods to characterize folding and function of BamA crosslink mutants. Methods in Molecular Biology: The BAM complex 1329:137-47.

Noinaj N, Buchanan SK. (2015). Summary and Future Directions. Methods Mol Biol. 1329:279-80.

Rollauer SE, Sooreshjani MA, Noinaj N, Buchanan SK. (2015). Outer membrane protein biogenesis in Gram-negative bacteria. Philos Trans R Soc Lond B Biol Sci. 370(1679). DOI: 10.1098/rstb.2015.0023

O'Neil PK, Rollauer SE, Noinaj N, Buchanan SK. (2015). Fitting the Pieces of the β-Barrel Assembly Machinery Complex. Biochemistry 54(41):6303-11. DOI: 10.1021/acs.biochem.5b00852

Cash DR, Noinaj N, Buchanan SK, Cornelissen CN. (2015). Beyond the Crystal Structure: Insight into the Function and Vaccine Potential of TbpA Expressed by Neisseria gonorrhoeae. Infect. Immun. 83(11):4438-49. DOI: 10.1128/IAI.00762-15

2014

Noinaj N, Kuszak A, Balusek C, Gumbart JC, and Buchanan SK. (2014). Lateral opening and exit pore formation are required for BamA function. Structure, 8:22(7):1055-62. DOI: 10.1016/j.str.2014.05.008

Noinaj N, Buchanan SK. (2014). FhaC takes a bow to FHA in the two-partner do-si-do. Mol Micro, 92(6):1155-8. DOI: 10.1111/mmi.12627

Noinaj N, Buchanan SK. (2014). Structural insights into the transport of small molecules across membranes. Curr Opin Struct Biol., 26;27C:8-15. DOI: 10.1016/j.sbi.2014.02.007

Yu X, Strub MP, Barnard TJ, Noinaj N, Piszczek G, Buchanan SK, Taraska JW. (2014). An engineered palette of metal ion quenchable fluorescent proteins. PLoS One. 21;9(4):e95808. DOI: 10.1371/journal.pone.0095808

Shen HH, Leyton DL, Belousoff MJ, Noinaj N, Lu J, Holt S, Tan K, Selkrig J, Shiota T, Webb CT, Buchanan SK, Martin L and Lithgow T. (2014). Reconstitution of a nanomachine driving protein assembly into bacterial outer membranes. Nature Communications 5:5078. DOI: 10.1038/ncomms6078

2013

Noinaj N, Kuszak AJ, Gumbart JC, Lukacik P, Chang H, Easley NC, Lithgow T, and Buchanan SK. (2013). Structural insight into the biogenesis of b-barrel membrane proteins. Nature, 501(7467):385-90. DOI: 10.1038/nature12521

Bosserman MA, Downey T, Noinaj N, Buchanan SK, and Rohr J. (2013). Molecular Insight into Substrate Recognition and Catalysis of Baeyer-Villiger Monooxygenase MtmOIV. ACS Chem Biol. 15;8(11):2466-77.

DOI: 10.1021/cb400399b

Noinaj N, Cornelissen CN, Buchanan SK. (2013). Structural insight into the lactoferrin receptors from pathogenic Neisseria. J Struct Biol. 2013 184(1):83-92. DOI: 10.1016/j.jsb.2013.02.009

Roecker L, Aiyegbo M, Al-Haddad A, Fletcher E, Kc R, Hurst J, Lane T, Larsen R, Noinaj N, Teh SL, Wade SK, Parkin S. (2013). Synthesis and characterisation of [(en)2Co] 3+ complexes coordinated by substituted thiourea ligands. Aust J. Chem, 66(8) 944-951.

2012

Noinaj N, Easley N, Oke M, Mizuno N, Gumbart JC, Boura E, Steere A, Zak O, Aisen P, Tajkhorshid E, Evans RW, Gorringe AR, Mason AB, Steven AC, and Buchanan SK. (2012). Structural basis for iron piracy in pathogenic Neisseria, Nature, 483 (7387):53-8.

White JF, Noinaj N, Shibata Y, Love J, Kloss B, Xu F, Gvozdenovic-Jeremic J, Shah P, Shiloach J, Tate CG, Grisshammer R. (2012). Structure of the agonist-bound neurotensin receptor NTS1. Nature, 490 (7421):508-513.

Noinaj N, Buchanan SK, and Cornelissen CN, (2012). The transferrin–iron import system from pathogenic Neisseria species. Mol Micro, 86 (2):246-257.

Noinaj N, Buchanan SK. (2012). Selenophosphate Synthetase. (Encyclopedia of Metalloproteins).

Noinaj N, Wattanasak R, Lee DY, Wally J, Piszczek G, Chock PB, Stadtman TC, and Buchanan SK. (2012). Structural insights into the catalytic mechanism of E. coli selenophosphate synthetase, J. Bacteriology, 194(2):499-508.

Noinaj N, Song ES, Bhasin S, Alper BJ, Schmidt WK, Hersh LB, and Rodgers DW. (2012). Anion activation site of insulin degrading enzyme, JBC, 287(1):48-57.

Webb C, Selkrig J, Perry A, Noinaj N, Buchanan SK, and Lithgow T. (2012) Dynamic association of BAM complex modules includes surface exposure of the lipoprotein BamC. JMB. 422(4):545-55.

Fairman JW, Dautin N, Wojtowicz, Liu W, Noinaj N, Barnard TJ, Przytycka T, Cherezov V, and Buchanan SK. (2012). Beta-domain structures of Escherichia coli 0157:H7 intimin and Yersinia pseudotuberculosis invasin. Structure, 3;20(7):1233-43.

Barnard T, Gumbart JC, Peterson JH, Noinaj N, Easley NC, Dautin N, Kuszak AJ, Tajkhorshid E, Bernstein HD, and Buchanan SK. (2012). Molecular basis for the activation of a catalytic asparagine residue in a self-cleaving bacterial autotransporter. JMB, 415(1):128-42.

Lukacik P, Barnard TJ, Keller PW, Chaturvedi KS, Seddiki N, Fairman JW, Noinaj N, Kirby TL, Henderson JP, Steven AC, Hinnebusch BJ, and Buchanan SK. (2012) Structural engineering of a phase lysin that targets Gram-negative pathogens. PNAS. 109(25):9857-62.

2011

Noinaj N, Bhasin SK, Song ES, Scoggin KE, Juliano MA, Juliano L, Hersh LB, Rodgers DW. (2011). Identification of the Allosteric Regulatory Site of Insulysin. PLoS One, 6(6): e20864.

Noinaj N, Bosserman MA, Schickli MA, Piszczek G, Kharel MK, Pahari P, Buchanan SK, Rohr J. (2011). The crystal structure and mechanism of an unusual oxidoreductase, GilR, involved in gilvocarcin V biosynthesis. JBC, 286(26):23533-43.

Noinaj N, Fairman JW, Buchanan SK. (2011). The Crystal Structure of BamB Suggests Interactions with BamA and Its Role within the BAM Complex. JMB, 407(2):248-60.

Fairman JW, Noinaj N, Buchanan SK. (2011). The structural biology of b-barrel membrane proteins: a summary of recent reports. Current Opinion in Structural Biology, 21:1–9.

Yamashita, S., Lukacik, P., Barnard, T.J., Noinaj, N. Felek, S., Tsang, T.M., Krukonis, E.S., Hinnebusch, B.J. & Buchanan, S.K. (2011). Structural insights into Ail-mediated virulence in Yersinia pestis, Structure, 19(11):1672-82.

2010

Noinaj N, Guillier M, Barnard T, and Buchanan SK. (2010). TonB-dependent transporters: regulation, structure, and function. Annu Rev Microbiol, 64:43-60.

Tong J, Dolezal P, Selkrig J, Crawford S, Simpson AG, Noinaj N, Buchanan SK, Gabriel K, Lithgow T. (2010). Ancestral and derived protein import pathways in the mitochondrion of Reclinomonas americana. Mol Biol Evol, 28(5):1581-91.

Anwari K, Poggio S, Perry A, Gatsos X, Ramarathinam SH, Williamson NA, Noinaj N, Buchanan S, Gabriel K, Purcell AW, Jacobs-Wagner C, Lithgow T. (2010). A modular BAM complex in the outer membrane of the alpha-proteobacterium Caulobacter crescentus. PLoS One, 5(1):e8619.

2009

Beam MP, Bosserman MA, Noinaj N, Wehenkel M, Rohr J. (2009). Crystal structure of Baeyer-Villiger monooxygenase MtmOIV, the key enzyme of the mithramycin biosynthetic pathway. Biochemistry, 48(21):4476-87.

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