BPG is committed to discovery and dissemination of knowledge
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 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) doi: 10.1016/j.bbcan.2020.188442
3
Melanie R. McReynolds, Karthikeyani Chellappa, Joseph A. Baur. Age-related NAD+ declineExperimental Gerontology 2020; 134 doi: 10.1016/j.exger.2020.110888
4
Nadezhda Frolova, Daria Gorbach, Christian Ihling, Tatiana Bilova, Anastasia Orlova, Elena Lukasheva, Ksenia Fedoseeva, Irina Dodueva, Lyudmila A. Lutova, Andrej Frolov. Proteome and Metabolome Alterations in Radish (Raphanus sativus L.) Seedlings Induced by Inoculation with Agrobacterium tumefaciensBiomolecules 2025; 15(2) doi: 10.3390/biom15020290
5
He Meng, Michael C. Fitzgerald. Proteome-Wide Characterization of Phosphorylation-Induced Conformational Changes in Breast CancerJournal of Proteome Research 2018; 17(3) doi: 10.1021/acs.jproteome.7b00795
6
Michael A. Sirover. Glyceraldehyde-3-phosphate Dehydrogenase (GAPDH)2017;  doi: 10.1016/B978-0-12-809852-3.00001-7
7
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) doi: 10.1371/journal.pone.0290892