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Cited by in CrossRef
For: Phadke M, Krynetskaia N, Mishra A, Barrero C, Merali S, Gothe SA, Krynetskiy E. Disruption of NAD+ binding site in glyceraldehyde 3-phosphate dehydrogenase affects its intranuclear interactions. World J Biol Chem 2015; 6(4): 366-378 [PMID: 26629320 DOI: 10.4331/wjbc.v6.i4.366]
URL: https://www.wjgnet.com/1949-8454/full/v6/i4/366.htm
Number Citing Articles
1
Elsa D. Garcin. GAPDH as a model non-canonical AU-rich RNA binding proteinSeminars in Cell & Developmental Biology 2019; 86: 162 doi: 10.1016/j.semcdb.2018.03.013
2
Maria Letizia Taddei, Elisa Pardella, Erica Pranzini, Giovanni Raugei, Paolo Paoli. Role of tyrosine phosphorylation in modulating cancer cell metabolismBiochimica et Biophysica Acta (BBA) - Reviews on Cancer 2020; 1874(2): 188442 doi: 10.1016/j.bbcan.2020.188442
3
Melanie R. McReynolds, Karthikeyani Chellappa, Joseph A. Baur. Age-related NAD+ declineExperimental Gerontology 2020; 134: 110888 doi: 10.1016/j.exger.2020.110888
4
He Meng, Michael C. Fitzgerald. Proteome-Wide Characterization of Phosphorylation-Induced Conformational Changes in Breast CancerJournal of Proteome Research 2018; 17(3): 1129 doi: 10.1021/acs.jproteome.7b00795
5
Michael A. Sirover. Glyceraldehyde-3-phosphate Dehydrogenase (GAPDH)2017; : 3 doi: 10.1016/B978-0-12-809852-3.00001-7
6
Helen S. Tang, Chelsea R. Gates, Michael C. Schultz, Prasanth Puthanveetil. Biochemical evidence that the whole compartment activity behavior of GAPDH differs between the cytoplasm and nucleusPLOS ONE 2023; 18(8): e0290892 doi: 10.1371/journal.pone.0290892