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

Year Number of Results
1994 1
1995 1
1998 2
2000 3
2001 3
2003 3
2004 7
2005 2
2006 2
2009 1
2010 2
2011 3
2012 1
2013 1
2014 2
2015 2
2016 1
2017 3
2018 5
2019 1
2020 6
2021 3
2022 3
2023 3
2024 2

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Page 1
Epidemiology and outcomes of hospital-acquired bloodstream infections in intensive care unit patients: the EUROBACT-2 international cohort study.
Tabah A, Buetti N, Staiquly Q, Ruckly S, Akova M, Aslan AT, Leone M, Conway Morris A, Bassetti M, Arvaniti K, Lipman J, Ferrer R, Qiu H, Paiva JA, Povoa P, De Bus L, De Waele J, Zand F, Gurjar M, Alsisi A, Abidi K, Bracht H, Hayashi Y, Jeon K, Elhadi M, Barbier F, Timsit JF; EUROBACT-2 Study Group, ESICM, ESCMID ESGCIP and the OUTCOMEREA Network. Tabah A, et al. Intensive Care Med. 2023 Feb;49(2):178-190. doi: 10.1007/s00134-022-06944-2. Epub 2023 Feb 10. Intensive Care Med. 2023. PMID: 36764959 Free PMC article.
Tissue remodeling by an opportunistic pathogen triggers allergic inflammation.
Agaronyan K, Sharma L, Vaidyanathan B, Glenn K, Yu S, Annicelli C, Wiggen TD, Penningroth MR, Hunter RC, Dela Cruz CS, Medzhitov R. Agaronyan K, et al. Immunity. 2022 May 10;55(5):895-911.e10. doi: 10.1016/j.immuni.2022.04.001. Epub 2022 Apr 27. Immunity. 2022. PMID: 35483356 Free PMC article.
Mechanism of p-hydroxyphenylacetate-3-hydroxylase. A two-protein enzyme.
Arunachalam U, Massey V, Miller SM. Arunachalam U, et al. J Biol Chem. 1994 Jan 7;269(1):150-5. J Biol Chem. 1994. PMID: 8276789 Free article.
p-Hydroxyphenylacetate-3-hydroxylase purified from Pseudomonas putida is a two-protein enzyme requiring a flavoprotein and a coupling protein for productive hydroxylation (Arunachalam, U., Massey, V., and Vaidyanathan, C. S. (1992) J. Biol. Chem. 267, 25848-2 …
p-Hydroxyphenylacetate-3-hydroxylase purified from Pseudomonas putida is a two-protein enzyme requiring a flavoprotein and a coupling protei …
Deep learning for the fully automated segmentation of the inner ear on MRI.
Vaidyanathan A, van der Lubbe MFJA, Leijenaar RTH, van Hoof M, Zerka F, Miraglio B, Primakov S, Postma AA, Bruintjes TD, Bilderbeek MAL, Sebastiaan H, Dammeijer PFM, van Rompaey V, Woodruff HC, Vos W, Walsh S, van de Berg R, Lambin P. Vaidyanathan A, et al. Sci Rep. 2021 Feb 3;11(1):2885. doi: 10.1038/s41598-021-82289-y. Sci Rep. 2021. PMID: 33536451 Free PMC article.
2,3-Dihydroxybenzoic acid decarboxylase from Aspergillus niger. A novel decarboxylase.
Santha R, Savithri HS, Rao NA, Vaidyanathan CS. Santha R, et al. Eur J Biochem. 1995 May 15;230(1):104-10. Eur J Biochem. 1995. PMID: 7601088 Free article.
Unlike most other decarboxylases, this enzyme does not require a cofactor, underlining the importance of active-site residues in the reaction mechanism. Earlier studies from this laboratory [Kamath, A. V., Appaji Rao, N. & Vaidyanathan, C. S. (1989) Bioch …
Unlike most other decarboxylases, this enzyme does not require a cofactor, underlining the importance of active-site residues in the reactio …
Targeted replacement of full-length CFTR in human airway stem cells by CRISPR-Cas9 for pan-mutation correction in the endogenous locus.
Vaidyanathan S, Baik R, Chen L, Bravo DT, Suarez CJ, Abazari SM, Salahudeen AA, Dudek AM, Teran CA, Davis TH, Lee CM, Bao G, Randell SH, Artandi SE, Wine JJ, Kuo CJ, Desai TJ, Nayak JV, Sellers ZM, Porteus MH. Vaidyanathan S, et al. Mol Ther. 2022 Jan 5;30(1):223-237. doi: 10.1016/j.ymthe.2021.03.023. Epub 2021 Mar 29. Mol Ther. 2022. PMID: 33794364 Free PMC article.
57 results