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Mitochondrial CypD Acetylation Promotes Endothelial Dysfunction and Hypertension

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Ethanol Metabolism Modifies Hepatic Protein Acylation in Mice

Fritz, K. S., Green, M. F., Petersen, D. R., & Hirschey, M. D. (2013) · PLoS ONE · doi:10.1371/journal.pone.0075868 · Cited by 53

The ɛ‐Amino Group of Protein Lysine Residues Is Highly Susceptible to Nonenzymatic Acylation by Several Physiological Acyl‐CoA Thioesters

Simic, Z., Weiwad, M., Schierhorn, A., Steegborn, C., & Schutkowski, M. (2015) · ChemBioChem · doi:10.1002/cbic.201500364 · Cited by 55

Overexpression of Mitochondrial Sirtuins Alters Glycolysis and Mitochondrial Function in HEK293 Cells

de Moura, M. B., Uppala, R., Zhang, Y., Houten, B. V., & Goetzman, E. S. (2014) · PLoS ONE · doi:10.1371/journal.pone.0106028 · Cited by 51

Imbalance of Lysine Acetylation Contributes to the Pathogenesis of Parkinson’s Disease

Wang, R., Sun, H., Wang, G., & Ren, H. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21197182 · Cited by 51

Protein acetylation as a means to regulate protein function in tune with metabolic state

Shi, L., & Tu, B. P. (2014) · Biochemical Society Transactions · doi:10.1042/bst20140135 · Cited by 50

Development of the Swimbladder Surfactant System and Biogenesis of Lysosome-Related Organelles Is Regulated by BLOS1 in Zebrafish

Chen, T., Song, G., Yang, H., Mao, L., Cui, Z., & Huang, K. (2018) · Genetics · doi:10.1534/genetics.117.300621 · Cited by 49

Are sirtuin deacylase enzymes important modulators of mitochondrial energy metabolism?

Osborne, B., Cooney, G. J., & Turner, N. A. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.08.016 · Cited by 47

Loss of GCN5L1 in cardiac cells disrupts glucose metabolism and promotes cell death via reduced Akt/mTORC2 signaling

Manning, J. R., Thapa, D., Zhang, M., Stoner, M. W., Traba, J., Corey, C. G., Shiva, S., Sack, M. N., & Scott, I. (2019) · Biochemical Journal · doi:10.1042/bcj20190302 · Cited by 47

Understanding the acetylome: translating targeted proteomics into meaningful physiology

Philp, A., Rowland, T., Pérez‐Schindler, J., & Schenk, S. (2014) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00399.2013 · Cited by 48

Cardiac-specific deletion of GCN5L1 restricts recovery from ischemia-reperfusion injury

Manning, J. R., Thapa, D., Zhang, M., Stoner, M. W., Traba, J., McTiernan, C. F., Corey, C. G., Shiva, S., Sack, M. N., & Scott, I. (2019) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2019.02.009 · Cited by 45

The pea seedling mitochondrial Nε-lysine acetylome

Smith-Hammond, C. L., Hoyos, E., & Miernyk, J. A. (2014) · Mitochondrion · doi:10.1016/j.mito.2014.04.012 · Cited by 45

Mitochondrion as a Target for Heart Failure Therapy – Role of Protein Lysine Acetylation –

Lee, C. F., & Tian, R. (2015) · Circulation Journal · doi:10.1253/circj.cj-15-0742 · Cited by 46

Defining the Orphan Functions of Lysine Acetyltransferases

Montgomery, D. C., Sorum, A. W., & Meier, J. L. (2015) · ACS Chemical Biology · doi:10.1021/cb500853p · Cited by 44

Lysine acetylation of cytoskeletal proteins: Emergence of an actin code

Mu, A., Latario, C. J., Pickrell, L. E., & Higgs, H. N. (2020) · The Journal of Cell Biology · doi:10.1083/jcb.202006151 · Cited by 45

Dynamic regulation of lysine acetylation: the balance between acetyltransferase and deacetylase activities

Hyndman, K. A., & Knepper, M. A. (2017) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00313.2017 · Cited by 42

Chemical Biology Approaches for Investigating the Functions of Lysine Acetyltransferases

He, M., Han, Z. H., Liu, L., & Zheng, Y. G. (2017) · Angewandte Chemie International Edition · doi:10.1002/anie.201704745 · Cited by 43

Cardiomyocyte-specific deletion of GCN5L1 in mice restricts mitochondrial protein hyperacetylation in response to a high fat diet

Thapa, D., Manning, J. R., Stoner, M. W., Zhang, M., Xie, B., & Scott, I. (2020) · Scientific Reports · doi:10.1038/s41598-020-67812-x · Cited by 41

Plant mitochondrial retrograde signaling: post-translational modifications enter the stage

Hartl, M., & Finkemeier, I. (2012) · Frontiers in Plant Science · doi:10.3389/fpls.2012.00253 · Cited by 40

GCN5L1 Functions as a Mitochondrial Acetyltransferase that Regulates Mitophagy

Webster, B. R. (2015) · UNM’s Digital Repository (University of New Mexico) · Cited by 2

Sirtuin regulation of lysine acylation targets diverse metabolic networks in hepatic mitochondria (981.3)

Rardin, M. J., He, W., Sahu, A. K., Nishida, Y., Verdin, E. M., & Gibson, B. W. (2014) · The FASEB Journal · doi:10.1096/fasebj.28.1_supplement.981.3

Role of SIRT3 and GCN5L1 in regulation ob biogenesis and structural organization of the respiratory chain through reversible lysine acetylation

Hofer, A. (2016)

Deacetylation by SIRT3 Relieves Inhibition of Mitochondrial Protein Function

Chhoy, P., Anderson, K. A., Hershberger, K. A., Huynh, F. K., Martin, A. S., McDonnell, E., Peterson, B. S., Starzenski, L. A., Backos, D. S., Fritz, K. S., et al. (2016) · Springer eBooks · doi:10.1007/978-94-024-0962-8_5 · Cited by 3

A conserved prokaryotic region of GCN5L1 is required for mitochondrial acetyltransferase function

Scott, I., Webster, B. R., & Sack, M. N. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.08.500