The DOI matches its Crossref record; 25 of the 25 references it cites were found in a registry or an index.
O -Linked GlcNAc Modification of Cardiac Myofilament Proteins: A Novel Regulator of Myocardial Contractile Function
Open accessAbstract
In addition to O -phosphorylation, O -linked modifications of serine and threonine by β- N -acetyl- d -glucosamine (GlcNAc) may regulate muscle contractile function. This study assessed the potential role of O -GlcNAcylation in cardiac muscle contractile activation. To identify specific sites of O -GlcNAcylation in cardiac myofilament proteins, a recently developed methodology based on GalNAz-biotin labeling followed by dithiothreitol replacement and light chromatography/tandem mass spectrometry site mapping was adopted. Thirty-two O -GlcNAcylated peptides from cardiac myofilaments were identified on cardiac myosin heavy chain, actin, myosin light chains, and troponin I. To assess the potential physiological role of the GlcNAc, force–[Ca 2+ ] relationships were studied in skinned rat trabeculae. Exposure to GlcNAc significantly decreased calcium sensitivity (pCa50), whereas maximal force ( F max ) and Hill coefficient ( n ) were not modified. Using a pan-specific O -GlcNAc antibody, it was determined that acute exposure of myofilaments to GlcNAc induced a significant increase in actin O -GlcNAcylation. This study provides the first identification of O -GlcNAcylation sites in cardiac myofilament proteins and demonstrates their potential role in regulating myocardial contractile function.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“The PTMs of sarcomeric proteins are known to be important mediators of cardiac signaling and exert various effects on contractile function (13–17).”
From Distinct hypertrophic cardiomyopathy genotypes result in convergent sarcomeric proteoform profiles revealed by top-down proteomics (2020) · cites this paper as [17]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
New type of cardiomyopathy associated with diabetic glomerulosclerosis
Rubler, S., Dlugash, J., Yuceoglu, Y. Z., Kumral, T., Branwood, A. W., & Grishman, A. (1972) · The American Journal of Cardiology · doi:10.1016/0002-9149(72)90595-4 · Cited by 1,835
Diabetic Cardiomyopathy Revisited
Boudina, S., & Abel, E. D. (2007) · Circulation · doi:10.1161/circulationaha.106.679597 · Cited by 1,543
Cycling of O-linked β-N-acetylglucosamine on nucleocytoplasmic proteins
Hart, G. W., Housley, M. P., & Slawson, C. (2007) · Nature · doi:10.1038/nature05815 · Cited by 1,418
Self-citationWang, Z., Guček, M., & Hart, G. W. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0806216105 · Cited by 341
Self-citationCharacterization of a Mouse Monoclonal Antibody Specific for O-Linked N-Acetylglucosamine
Comer, F. I., Vosseller, K., Wells, L., Accavitti, M. A., & Hart, G. W. (2001) · Analytical Biochemistry · doi:10.1006/abio.2001.5132 · Cited by 295
Self-citationMechanisms of [Ca2+]i Transient Decrease in Cardiomyopathy of db/db Type 2 Diabetic Mice
Pereira, L., Matthes, J., Schuster, I., Valdivia, H. H., Herzig, S., Richard, S., & Gomez, A. M. (2006) · Diabetes · doi:10.2337/diabetes.55.03.06.db05-1284 · Cited by 261
Cardioprotection by N -Acetylglucosamine Linkage to Cellular Proteins
Jones, S. P., Zachara, N. E., Ngoh, G. A., Hill, B. G., Teshima, Y., Bhatnagar, A., Hart, G. W., & Marbán, E. (2008) · Circulation · doi:10.1161/circulationaha.107.730515 · Cited by 258
Self-citationHu, Y., Belke, D. D., Suárez, J., Swanson, E., Clark, R., Hoshijima, M., & DILLMANN, W. H. (2005) · Circulation Research · doi:10.1161/01.res.0000165478.06813.58 · Cited by 228
Wang, Z., Pandey, A., & Hart, G. W. (2007) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m600453-mcp200 · Cited by 217
Self-citationCovalent and Noncovalent Modification of Thin Filament Action
Metzger, J. M., & Westfall, M. V. (2004) · Circulation Research · doi:10.1161/01.res.0000110083.17024.60 · Cited by 179
Research works printed but not linked: 1
- 10.1161/res.89.6.480 · DOI
Cited by
Sorted by citations
Hart, G. W., Slawson, C., Ramirez-Correa, G., & Lagerlof, O. (2011) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060608-102511 · Cited by 1,317
Self-citationGiri, B., Dey, S., Das, T., Sarkar, M., Banerjee, J., & Dash, S. K. (2018) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2018.07.157 · Cited by 706
Huynh, K., Bernardo, B. C., McMullen, J. R., & Ritchie, R. H. (2014) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2014.01.003 · Cited by 555
Role of O -linked N -acetylglucosamine protein modification in cellular (patho)physiology
Chatham, J. C., Zhang, J., & Wende, A. R. (2020) · Physiological Reviews · doi:10.1152/physrev.00043.2019 · Cited by 365
Glucose Metabolism in Cardiac Hypertrophy and Heart Failure
Tran, D. H., & Wang, Z. V. (2019) · Journal of the American Heart Association · doi:10.1161/jaha.119.012673 · Cited by 336
Self-citationO-GlcNAc profiling: from proteins to proteomes
Ma, J., & Hart, G. W. (2014) · Clinical Proteomics · doi:10.1186/1559-0275-11-8 · Cited by 291
Self-citationFinding the weakest link – exploring integrin-mediated mechanical molecular pathways
Roca‐Cusachs, P., Iskratsch, T., & Sheetz, M. P. (2012) · Journal of Cell Science · doi:10.1242/jcs.095794 · Cited by 269
AMPK activation counteracts cardiac hypertrophy by reducing O-GlcNAcylation
Gélinas, R., Mailleux, F., Dontaine, J., Bultot, L., Demeulder, B., Ginion, A., Daskalopoulos, E. P., Esfahani, H., Dubois‐Deruy, E., Lauzier, B., et al. (2018) · Nature Communications · doi:10.1038/s41467-017-02795-4 · Cited by 261
Protein O -GlcNAcylation in diabetes and diabetic complications
Ma, J., & Hart, G. W. (2013) · Expert Review of Proteomics · doi:10.1586/14789450.2013.820536 · Cited by 265
Self-citationCracking the O-GlcNAc code in metabolism
Ruan, H., Singh, J. P., Li, M., Wu, J., & Yang, X. (2013) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2013.02.002 · Cited by 224
Post-translational modification and regulation of actin
Terman, J. R., & Kashina, A. S. (2012) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2012.10.009 · Cited by 232
Cross-talk between Two Essential Nutrient-sensitive Enzymes
Bullen, J. W., Balsbaugh, J. L., Chanda, D., Shabanowitz, J., Hunt, D. F., Neumann, D., & Hart, G. W. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.523068 · Cited by 228
Self-citationStølen, T., Høydal, M. A., Kemi, O. J., Catalucci, D., Ceci, M., Aasum, E., Larsen, T. S., Rolim, N. P. L., Condorelli, G., Smith, G. L., et al. (2009) · Circulation Research · doi:10.1161/circresaha.109.199810 · Cited by 203
Sequeira, V., Wijnker, P. J. M., Nijenkamp, L. L. A. M., Kuster, D. W. D., Najafi, A., Witjas‐Paalberends, E. R., Regan, J. A., Boontje, N. M., ten Cate, F. J., Germans, T., et al. (2013) · Circulation Research · doi:10.1161/circresaha.111.300436 · Cited by 196
Self-citationDiabetes-associated dysregulation of O -GlcNAcylation in rat cardiac mitochondria
Banerjee, P. S., Ma, J., & Hart, G. W. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1424017112 · Cited by 193
Self-citationCardiac O-GlcNAc signaling is increased in hypertrophy and heart failure
Lunde, I. G., Aronsen, J. M., Kvaløy, H., Qvigstad, E., Sjaastad, I., Tønnessen, T., Christensen, G., Grønning-Wang, L. M., & Carlson, C. R. (2011) · Physiological Genomics · doi:10.1152/physiolgenomics.00016.2011 · Cited by 196
Glycopeptide-specific monoclonal antibodies suggest new roles for O-GlcNAc
Teo, C. F., Ingale, S., Wolfert, M. A., Elsayed, G. A., Nöt, L. G., Chatham, J. C., Wells, L., & Boons, G. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.338 · Cited by 187
O-linked β- N -acetylglucosamine transferase is indispensable in the failing heart
Watson, L. J., Facundo, H. T., Ngoh, G. A., Ameen, M., Brainard, R. E., Lemma, K. M., Long, B. W., Prabhu, S. D., Xuan, Y., & Jones, S. P. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1001907107 · Cited by 186
Functions of myosin light chain-2 (MYL2) in cardiac muscle and disease
Sheikh, F., Lyon, R. C., & Chen, J. (2015) · Gene · doi:10.1016/j.gene.2015.06.027 · Cited by 177
Analytical and Biochemical Perspectives of Protein O-GlcNAcylation
Ma, J., Wu, C., & Hart, G. W. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.0c00884 · Cited by 172
Self-citationRoles of O-GlcNAc in chronic diseases of aging
Banerjee, P. S., Lagerlöf, O., & Hart, G. W. (2016) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2016.05.005 · Cited by 157
Self-citationRegulation of Calcium/Calmodulin-dependent Kinase IV by O-GlcNAc Modification
Dias, W. B., Cheung, W. D., Wang, Z., & Hart, G. W. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.007310 · Cited by 165
Self-citationProteinO-GlcNAcylation: a new signaling paradigm for the cardiovascular system
Laczy, B., Hill, B. G., Wang, K., Paterson, A. J., White, C. R., Xing, D., Chen, Y.-F., Darley-Usmar, V. M., Oparil, S., & Chatham, J. C. (2008) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01056.2008 · Cited by 150
TNNI1, TNNI2 and TNNI3: Evolution, regulation, and protein structure–function relationships
Sheng, J., & Jin, J. (2015) · Gene · doi:10.1016/j.gene.2015.10.052 · Cited by 146
New insights: A role forO-GlcNAcylation in diabetic complications
Peterson, S. B., & Hart, G. W. (2016) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2015.1135102 · Cited by 124
Self-citationLucena, M. C., Carvalho‐cruz, P., Donadio, J. L., Oliveira, I. D. A., de Queiroz, R. M., Marinho-Carvalho, M. M., Sola‐Penna, M., Paula, I. F. D., Gondim, K. C., McComb, M. E., et al. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.729236 · Cited by 130
Self-citationO-GlcNAcylation and cardiovascular disease
Wright, J. N., Collins, H. E., Wende, A. R., & Chatham, J. C. (2017) · Biochemical Society Transactions · doi:10.1042/bst20160164 · Cited by 109
Tucholski, T., Cai, W., Gregorich, Z. R., Bayne, E. F., Mitchell, S. D., McIlwain, S. J., de Lange, W. J., Wrobbel, M., Karp, H., Hite, Z., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2006764117 · Cited by 107
Removal of Abnormal Myofilament O-GlcNAcylation Restores Ca2+ Sensitivity in Diabetic Cardiac Muscle
Ramirez‐Correa, G. A., Ma, J., Slawson, C. M., Zeidan, Q., Lugo‐Fagundo, N. S., Xu, M., Shen, X., Gao, W. D., Caceres, V., Chakir, K., et al. (2015) · Diabetes · doi:10.2337/db14-1107 · Cited by 104
Self-citationOliveira, S. M., Zhang, Y.-H., Solis, R. S., Isackson, H., Bellahcene, M., Yavari, A., Pinter, K., Davies, J. K., Ge, Y., Ashrafian, H., et al. (2012) · Circulation Research · doi:10.1161/circresaha.111.259952 · Cited by 86
Tampering with springs: phosphorylation of titin affecting the mechanical function of cardiomyocytes
Hamdani, N., Herwig, M., & Linke, W. A. (2017) · Biophysical Reviews · doi:10.1007/s12551-017-0263-9 · Cited by 85
Biesiadecki, B. J., Davis, J. P., Ziolo, M. T., & Janssen, P. M. L. (2014) · Biophysical Reviews · doi:10.1007/s12551-014-0143-5 · Cited by 83
Myofilament Calcium Sensitivity: Role in Regulation of In vivo Cardiac Contraction and Relaxation
Chung, J.-H., Biesiadecki, B. J., Ziolo, M. T., Davis, J. P., & Janssen, P. M. L. (2016) · Frontiers in Physiology · doi:10.3389/fphys.2016.00562 · Cited by 83
Chronic O-GlcNAcylation and Diabetic Cardiomyopathy: The Bitterness of Glucose
Ducheix, S., Magré, J., Cariou, B., & Prieur, X. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00642 · Cited by 84
Thick Filament Protein Network, Functions, and Disease Association
Wang, L., Geist, J., Grogan, A., Hu, L. R., & Kontrogianni‐Konstantopoulos, A. (2018) · Comprehensive physiology · doi:10.1002/cphy.c170023 · Cited by 82
Scheen, M., Giraud, R., & Bendjelid, K. (2021) · Physiological Reports · doi:10.14814/phy2.14713 · Cited by 88
Mesubi, O. O., Rokita, A. G., Abrol, N., Wu, Y., Chen, B., Wang, Q., Granger, J. M., Tucker-Bartley, A., Luczak, E. D., Murphy, K. R., et al. (2020) · Journal of Clinical Investigation · doi:10.1172/jci95747 · Cited by 82
Self-citationO-GlcNAcylation, enemy or ally during cardiac hypertrophy development?
Mailleux, F., Gélinas, R., Beauloye, C., Horman, S., & Bertrand, L. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.08.012 · Cited by 74
The roles ofO-linked β-N-acetylglucosamine in cardiovascular physiology and disease
Zachara, N. E. (2012) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00445.2011 · Cited by 73
Qin, C. X., Sleaby, R., Davidoff, A. J., Bell, J. R., Blasio, M. J. D., Delbridge, L. M. D., Chatham, J. C., & Ritchie, R. H. (2016) · Pharmacological Research · doi:10.1016/j.phrs.2016.12.016 · Cited by 73
Eyk, J. E. V. (2011) · Circulation Research · doi:10.1161/circresaha.110.226894 · Cited by 71
Nixon, B. R., Thawornkaiwong, A., Jin, J., Brundage, E. A., Little, S. C., Davis, J. P., Solaro, R. J., & Biesiadecki, B. J. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.323048 · Cited by 69
Opportunities for Therapeutic Modulation of O-GlcNAc
Cheng, S. S., Mody, A. C., & Woo, C. M. (2024) · Chemical Reviews · doi:10.1021/acs.chemrev.4c00417 · Cited by 64
Agnetti, G., Husberg, C., & Eyk, J. E. V. (2011) · Circulation Research · doi:10.1161/circresaha.110.226910 · Cited by 60
Lee, A., Miller, D., Henry, R. K., Paruchuri, V. D. P., O’Meally, R. N., Boronina, T. N., Cole, R. N., & Zachara, N. E. (2016) · Journal of Proteome Research · doi:10.1021/acs.jproteome.6b00369 · Cited by 60
Protein O-GlcNAcylation in cardiovascular diseases
Wang, H., Wang, Y., Zhou, Y., Wei, Y., Yan, Y., Zhang, Z., & Jing, Z. (2022) · Acta Pharmacologica Sinica · doi:10.1038/s41401-022-00934-2 · Cited by 57
The role of hyperglycaemia in the development of diabetic cardiomyopathy
Hayek, M. S. E., Ernande, L., Bénitah, J., Gomez, A. M., & Pereira, L. (2021) · Archives of cardiovascular diseases · doi:10.1016/j.acvd.2021.08.004 · Cited by 58
Perlman, D. H., Bauer, S. M., Ashrafian, H., Bryan, N. S., Garcia-Saura, M. F., Lim, C. C., Fernandez, B. O., Infusini, G., McComb, M. E., Costello, C. E., et al. (2009) · Circulation Research · doi:10.1161/circresaha.108.187005 · Cited by 57
Dubois‐Deruy, E., Belliard, A., Mulder, P. G. H., Bouvet, M., Smet‐Nocca, C., Janel, S., Lafont, F., Beseme, O., Amouyel, P., Richard, V. J., et al. (2015) · Cardiovascular Research · doi:10.1093/cvr/cvv136 · Cited by 55
O-GlcNAc Transferase Inhibitor Synergistically Enhances Doxorubicin-Induced Apoptosis in HepG2 Cells
Lee, S. J., & Kwon, O. (2020) · Cancers · doi:10.3390/cancers12113154 · Cited by 52
Medford, H. M., Chatham, J. C., & Marsh, S. A. (2012) · Life Sciences · doi:10.1016/j.lfs.2012.04.030 · Cited by 50
Lambert, M. R., Bastide, B., & Cieniewski‐Bernard, C. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00578 · Cited by 45
Akimoto, Y., Miura, Y., Toda, T., Wolfert, M. A., Wells, L., Boons, G., Hart, G. W., Endo, T., & Kawakami, H. (2011) · Clinical Proteomics · doi:10.1186/1559-0275-8-15 · Cited by 43
Self-citationProteome-wide profiling and mapping of post translational modifications in human hearts
Bagwan, N., Ali, H. H. E., & Lundby, A. (2021) · Scientific Reports · doi:10.1038/s41598-021-81986-y · Cited by 41
Rookyard, A. W., Paulech, J., Thyssen, S., Liddy, K. A., Puckeridge, M., Li, D. K., White, M. Y., & Cordwell, S. J. (2020) · Antioxidants and Redox Signaling · doi:10.1089/ars.2019.7765 · Cited by 39
Myocardial glucotoxicity: Mechanisms and potential therapeutic targets
Battault, S., Renguet, E., Steenbergen, A. V., Horman, S., Beauloye, C., & Bertrand, L. (2020) · Archives of cardiovascular diseases · doi:10.1016/j.acvd.2020.06.006 · Cited by 43
The continuing evolution of cardiac troponin I biomarker analysis: from protein to proteoform
Soetkamp, D., Raedschelders, K., Mastali, M., Sobhani, K., Bairey Merz, C. N., & Van Eyk, J. (2017) · Expert Review of Proteomics · doi:10.1080/14789450.2017.1387054 · Cited by 36
Protein O‐GlcNAcylation in the heart
Ng, Y. H., Okolo, C. A., Erickson, J. R., Baldi, J. C., & Jones, P. P. (2021) · Acta Physiologica · doi:10.1111/apha.13696 · Cited by 36
The role of post‐translational modifications in acute and chronic cardiovascular disease
Smith, L. E., & White, M. Y. (2014) · PROTEOMICS - CLINICAL APPLICATIONS · doi:10.1002/prca.201400052 · Cited by 36
Regulation of cardiac O-GlcNAcylation: More than just nutrient availability
Collins, H. E., & Chatham, J. C. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2020.165712 · Cited by 36
Dozio, E., Massaccesi, L., & Romanelli, M. M. C. (2021) · Journal of Clinical Medicine · doi:10.3390/jcm10204792 · Cited by 32
Janssens, J. V., Ma, B., Brimble, M. A., Eyk, J. E. V., Delbridge, L. M. D., & Mellor, K. M. (2018) · Scientific Reports · doi:10.1038/s41598-018-33886-x · Cited by 31
Defining the Sarcomeric Proteoform Landscape in Ischemic Cardiomyopathy by Top-Down Proteomics
Chapman, E. A., Aballo, T. J., Melby, J. A., Zhou, T., Price, S. J., Rossler, K. J., Lei, I., Tang, P. C. Y., & Ge, Y. (2023) · Journal of Proteome Research · doi:10.1021/acs.jproteome.2c00729 · Cited by 31
Deracinois, B., Camoin, L., Lambert, M. R., Boyer, J.-B., Dupont, E., Bastide, B., & Cieniewski‐Bernard, C. (2018) · Journal of Proteomics · doi:10.1016/j.jprot.2018.07.005 · Cited by 33
Top‐down mass spectrometry of cardiac myofilament proteins in health and disease
Peng, Y., Ayaz‐Güner, Ş., Yu, D., & Ge, Y. (2014) · PROTEOMICS - CLINICAL APPLICATIONS · doi:10.1002/prca.201400043 · Cited by 29
Acute stress induces long-term metabolic, functional, and structural remodeling of the heart
Yoganathan, T., Pérez-Liva, M., Balvay, D., Gall, M. L., Lallemand, A., Certain, A., Autret, G., Mokrani, Y., Guillonneau, F., Bruce, J., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-39590-3 · Cited by 29
Altered calcium signaling in colonic smooth muscle of type 1 diabetic mice
Touw, K., Chakraborty, S., Zhang, W., Obukhov, A. G., Tune, J. D., Gunst, S. J., & Herring, B. P. (2011) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00183.2011 · Cited by 29
Altered Actin Dynamics in Cell Migration of GNE Mutant Cells
Devi, S. S., Yadav, R., & Arya, R. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.603742 · Cited by 27
Myslicki, J. P., Belke, D. D., & Shearer, J. (2014) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/apnm-2014-0122 · Cited by 28
Cieniewski‐Bernard, C., Montel, V., Berthoin, S., & Bastide, B. (2012) · PLoS ONE · doi:10.1371/journal.pone.0048218 · Cited by 29
OGT (O-GlcNAc Transferase) Selectively Modifies Multiple Residues Unique to Lamin A
Simon, D. N., Wriston, A., Fan, Q., Shabanowitz, J., Florwick, A., Dharmaraj, T., Peterson, S. B., Gruenbaum, Y., Carlson, C. R., Grønning-Wang, L. M., et al. (2018) · Cells · doi:10.3390/cells7050044 · Cited by 25
Guo, L., Du, Y., Li, H., He, T., Yao, L., Yang, G., & Yang, X. (2025) · Metabolism · doi:10.1016/j.metabol.2025.156144 · Cited by 25
Burnham‐Marusich, A. R., Snodgrass, C. J., Johnson, A. M., Kiyoshi, C. M., Buzby, S. E., Gruner, M., & Berninsone, P. M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0049020 · Cited by 24
Lambert, M. R., Richard, É., Duban‐Deweer, S., Krzewinski, F., Deracinois, B., Dupont, E., Bastide, B., & Cieniewski‐Bernard, C. (2016) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2016.06.011 · Cited by 28
Ednie, A. R., & Bennett, E. S. (2020) · Basic Research in Cardiology · doi:10.1007/s00395-020-00820-0 · Cited by 24
The dual role of the hexosamine biosynthetic pathway in cardiac physiology and pathophysiology
Cairns, M., Joseph, D. E., & Essop, M. F. (2022) · Frontiers in Endocrinology · doi:10.3389/fendo.2022.984342 · Cited by 23
O-GlcNAcylation and phosphorylation of β-actin Ser199in diabetic nephropathy
Akimoto, Y., Yan, K., Miura, Y., Tsumoto, H., Toda, T., Fukutomi, T., Sugahara, D., Kudo, A., Arai, T., Chiba, Y., et al. (2019) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00566.2018 · Cited by 24
Self-citationO-GlcNAcylation, an original modulator of contractile activity in striated muscle
Cieniewski‐Bernard, C., Montel, V., Stevens, L., & Bastide, B. (2009) · Journal of Muscle Research and Cell Motility · doi:10.1007/s10974-010-9201-1 · Cited by 23
Cardiac Transcription Factor Nkx2.5 Is Downregulated under Excessive O-GlcNAcylation Condition
Kim, H. S., Woo, J. S., Joo, H. J., & Moon, W. K. (2012) · PLoS ONE · doi:10.1371/journal.pone.0038053 · Cited by 23
The multifaceted role of intracellular glycosylation in cytoprotection and heart disease
Umapathi, P., Aggarwal, A., Zahra, F., Narayanan, B., & Zachara, N. E. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107296 · Cited by 19
Cardiac energy metabolism in diabetes: emerging therapeutic targets and clinical implications
Panwar, A., Malik, S. O., Adib, M., & Lopaschuk, G. D. (2025) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00615.2024 · Cited by 19
Vang, S., Helton, E. S., Guo, Y., Burpee, B., Rose, E., Easter, M., Bollenbecker, S., Hirsch, M. J., Matthews, E. L., Jones, L., et al. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1387197 · Cited by 18
O-GlcNAcylation, contractile protein modifications and calcium affinity in skeletal muscle
Cieniewski‐Bernard, C., Lambert, M. R., Dupont, E., Montel, V., Stevens, L., & Bastide, B. (2014) · Frontiers in Physiology · doi:10.3389/fphys.2014.00421 · Cited by 19
Exercise training increases protein O-GlcNAcylation in rat skeletal muscle
Hortemo, K. H., Lunde, P., Anonsen, J. H., Kvaløy, H., Munkvik, M., Rehn, T. A., Sjaastad, I., Lunde, I. G., Aronsen, J. M., & Sejersted, O. M. (2016) · Physiological Reports · doi:10.14814/phy2.12896 · Cited by 19
Post‐translational modifications in diabetic cardiomyopathy
Li, Z., Chen, J., Huang, H., Zhan, Q., Wang, F., Chen, Z., Lu, X., & Sun, G. (2024) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.18158 · Cited by 17
Proteomic analysis in cardiovascular research
Oda, T., & Matsumoto, K. (2015) · Surgery Today · doi:10.1007/s00595-015-1169-4 · Cited by 16
Stevens, L., Bastide, B., Hédou, J., Cieniewski‐Bernard, C., Montel, V., Cochon, L., Dupont, E., & Mounier, Y. (2013) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2013.10.016 · Cited by 16
Cieniewski‐Bernard, C., Dupont, E., Richard, É., & Bastide, B. (2014) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-014-1453-y · Cited by 19
O-GlcNAcylation: The Underestimated Emerging Regulators of Skeletal Muscle Physiology
Liu, Y., Hu, Y., Fan, W.-X., Quan, X., Xu, B., & Li, S. (2022) · Cells · doi:10.3390/cells11111789 · Cited by 15
Leung, M.-C., Hitchen, P. G., Ward, D. G., Messer, A. E., & Marston, S. B. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.410316 · Cited by 15
Focus on cardiac troponin complex: From gene expression to cardiomyopathy
Ragusa, R., & Caselli, C. (2024) · Genes & Diseases · doi:10.1016/j.gendis.2024.101263 · Cited by 14
Post‐translational modifications of vertebrate striated muscle myosin heavy chains
Morales, P. F. N., Coons, A. N., Koopman, A. J., Patel, S., Chase, P. B., Parvatiyar, M. S., & Pinto, J. R. (2024) · Cytoskeleton · doi:10.1002/cm.21857 · Cited by 14
Cao, H. W., Hu, Y., Zhu, X., Yao, N., Gu, J., Wang, Y., & Zhu, W. (2020) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2020.05.010 · Cited by 14
Lambert, M. R., Claeyssen, C., Bastide, B., & Cieniewski‐Bernard, C. (2019) · Acta Physiologica · doi:10.1111/apha.13301 · Cited by 13
Oncometabolism: A Paradigm for the Metabolic Remodeling of the Failing Heart
Kuhn, A.-R., & van Bilsen, M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232213902 · Cited by 13
Targeted proteomics of myofilament phosphorylation and other protein posttranslational modifications
Ramirez‐Correa, G. A., Martinez‐Ferrando, M. I., Zhang, P., & Murphy, A. M. (2014) · PROTEOMICS - CLINICAL APPLICATIONS · doi:10.1002/prca.201400034 · Cited by 13
Self-citationMercier, T., Bouvet, M., Dubois‐Deruy, E., Dechaumes, A., Beseme, O., Richard, V. J., Mulder, P. G. H., & Pinet, F. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00598 · Cited by 12
Christopher, B. A., Pizarro, G. O., Nicholson, B., Yuen, S. L., Hoit, B. D., & Ogut, O. (2009) · Journal of Muscle Research and Cell Motility · doi:10.1007/s10974-009-9180-2 · Cited by 12
Overview on chronic complications of diabetes mellitus
Vlacho, B., Rossell-Rusiñol, J., Granado-Casas, M., Mauricio, D., & Julve, J. (2024) · Elsevier eBooks · doi:10.1016/b978-0-323-88426-6.00009-9 · Cited by 11
Impaired calcium handling mechanisms in atrial trabeculae of diabetic patients
Jones, T. L. M., Kaur, S., Kang, N., Ruygrok, P., & Ward, M. (2023) · Physiological Reports · doi:10.14814/phy2.15599 · Cited by 11
Metadata
- Authors
- Ramirez-Correa, G. A., Jin, W., Wang, Z., Zhong, X., Gao, W. D., Dias, W. B., Vecoli, C., Hart, G. W., & Murphy, A. M.
- Affiliations
- From the Departments of Pediatrics (G.A.R.-C., W.J., A.M.M.) and Medicine (C.V.), Division of Cardiology; Departments of Biological Chemistry (Z.W., W.B.D., G.W.H.) and Anesthesia and Critical Care Medicine (X.Z., W.D.G.), Johns Hopkins University School of Medicine, Baltimore, Md; and Department of Pathophysiology (X.Z.), Harbin Medical University, People’s Republic of China.
- Johns Hopkins University (US)
- Venue
- Circulation Research
- Published
- 2008-12-05
- Volume
- 103
- Issue
- 12
- Pages
- 1354-1358
- ISSN
- 0009-7330 (ISSN-L)
- 1524-4571
- PMC
- PMC2615199
- OpenAlex
- W2120416709
- Cited by
- 145
- References
- 25
- Citations by year
- 2026: 5 · 2025: 6 · 2024: 12 · 2023: 7 · 2022: 7 · 2021: 8 · 2020: 15 · 2019: 4 · 2018: 12 · 2017: 3 · 2016: 12 · 2015: 7 · 2014: 13 · 2013: 5 · 2012: 14
- FWCI
- 2.06
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Circulation Research (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health (n01hv28180-13-0-0)
- National Heart, Lung, and Blood Institute (N01 HV-28180, R01HL063038, N01 HV028180, R01-HL-63038)
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK061671, R01-DK61671)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiomyopathy and Myosin Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- O-GlcNAcylation, cardiac contractility, calcium sensitivity, myosin heavy chain, myosin light chain, troponin I, Hill coefficient
- MeSH terms
- Acetylglucosamine, Acylation, Animals, Carbohydrate Conformation, Mice, Inbred C57BL, Actin Cytoskeleton, Myocardial Contraction, Myocardium, Mice, Rats
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review