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 # Citing and Resources  
 
 When using PyHDX in your research, please cite our publication:  
 
 - Smit, J. H.; Krishnamurthy, S.; Srinivasu, B. Y.; Parakra, R.; Karamanou, S.; Economou, A. Probing Universal Protein Dynamics Using Hydrogen–Deuterium Exchange Mass Spectrometry-Derived Residue-Level Gibbs Free Energy. _Anal. Chem._ **2021**, _93_ (38), 12840–12847. [https://doi.org/10.1021/acs.analchem.1c02155](https://doi.org/10.1021/acs.analchem.1c02155).  
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 ## Citing dependencies  
 
 When using the different modules offered by PyHDX, please consider citing the following papers:
@@ -23,8 +25,9 @@ See [HDXrate](https://github.com/Jhsmit/HDXrate) for a python implementation of
 
 ## Publications using PyHDX  
 
-- Lin, X.; Haller, P.; Bavi, N.; Faruk, N.; Perozo, E.; Sosnick, T. R. Folding of Prestin’s Anion-Binding Site and the Mechanism of Outer Hair Cell Electromotility. bioRxiv February 28, 2023, p 2023.02.27.530320. [https://doi.org/10.1101/2023.02.27.530320](https://doi.org/10.1101/2023.02.27.530320).
+- Lin, X.; Haller, P.; Bavi, N.; Faruk, N.; Perozo, E.; Sosnick, T. R. Folding of Prestin’s Anion-Binding Site and the Mechanism of Outer Hair Cell Electromotility. _eLife_ **2023**, _12_. [https://doi.org/10.7554/eLife.89635](https://doi.org/10.7554/eLife.89635).
 - Bademosi, A. T.; Decet, M.; Kuenen, S.; Calatayud, C.; Swerts, J.; Gallego, S. F.; Schoovaerts, N.; Karamanou, S.; Louros, N.; Martin, E.; Sibarita, J.-B.; Vints, K.; Gounko, N. V.; Meunier, F. A.; Economou, A.; Versées, W.; Rousseau, F.; Schymkowitz, J.; Soukup, S.-F.; Verstreken, P. EndophilinA-Dependent Coupling between Activity-Induced Calcium Influx and Synaptic Autophagy Is Disrupted by a Parkinson-Risk Mutation. _Neuron_ **2023**. [https://doi.org/10.1016/j.neuron.2023.02.001](https://doi.org/10.1016/j.neuron.2023.02.001).
+- Huang, J.; Chu, X.; Luo, Y.; Wang, Y.; Zhang, Y.; Zhang, Y.; Li, H. Insights into Phosphorylation-Induced Protein Allostery and Conformational Dynamics of Glycogen Phosphorylase via Integrative Structural Mass Spectrometry and In Silico Modeling. _ACS Chem. Biol._ **2022**. [https://doi.org/10.1021/acschembio.2c00393](https://doi.org/10.1021/acschembio.2c00393).
 - Krishnamurthy, S.; Eleftheriadis, N.; Karathanou, K.; Smit, J. H.; Portaliou, A. G.; Chatzi, K. E.; Karamanou, S.; Bondar, A.-N.; Gouridis, G.; Economou, A. A Nexus of Intrinsic Dynamics Underlies Translocase Priming. _Structure_ **2021**, _29_ (8), 846-858.e7. [https://doi.org/10.1016/j.str.2021.03.015](https://doi.org/10.1016/j.str.2021.03.015).
 - Yuan, B.; Portaliou, A. G.; Parakra, R.; Smit, J. H.; Wald, J.; Li, Y.; Srinivasu, B.; Loos, M. S.; Dhupar, H. S.; Fahrenkamp, D.; Kalodimos, C. G.; Duong van Hoa, F.; Cordes, T.; Karamanou, S.; Marlovits, T. C.; Economou, A. Structural Dynamics of the Functional Nonameric Type III Translocase Export Gate. *Journal of Molecular Biology* **2021**, 433 (21), 167188. https://doi.org/10.1016/j.jmb.2021.167188.
 - Krishnamurthy, S.; Sardis, M.-F.; Eleftheriadis, N.; Chatzi, K. E.; Smit, J. H.; Karathanou, K.; Gouridis, G.; Portaliou, A. G.; Bondar, A.-N.; Karamanou, S.; Economou, A. Preproteins Couple the Intrinsic Dynamics of SecA to Its ATPase Cycle to Translocate via a Catch and Release Mechanism. _Cell Reports_ **2022**, _38_ (6). [https://doi.org/10.1016/j.celrep.2022.110346](https://doi.org/10.1016/j.celrep.2022.110346).
@@ -34,6 +37,9 @@ See [HDXrate](https://github.com/Jhsmit/HDXrate) for a python implementation of
 
 ## Publications citing PyHDX
 
+-  Yu, J.; Uzuner, U.; Long, B.; Wang, Z.; Yuan, J. S.; Dai, S. Y. Artificial Intelligence-Based HDX (AI-HDX) Prediction Reveals Fundamental Characteristics to Protein Dynamics: Mechanisms on SARS-CoV-2 Immune Escape. _iScience_ **2023**, _26_ (4), 106282. [https://doi.org/10.1016/j.isci.2023.106282](https://doi.org/10.1016/j.isci.2023.106282).
+- Anderson, K. W.; Hudgens, J. W. Hydrophilic Interaction Liquid Chromatography at Subzero Temperature for Hydrogen–Deuterium Exchange Mass Spectrometry. _J. Am. Soc. Mass Spectrom._ **2023**, _34_ (12), 2672–2679. [https://doi.org/10.1021/jasms.3c00243](https://doi.org/10.1021/jasms.3c00243).
+- Largy, E.; Ranz, M. OligoR: A Native HDX/MS Data Processing Application Dedicated to Oligonucleotides. _Anal. Chem._ **2023**, _95_ (25), 9615–9622. [https://doi.org/10.1021/acs.analchem.3c01321](https://doi.org/10.1021/acs.analchem.3c01321).
 - Vinciauskaite, V.; Masson, G. R. Fundamentals of HDX-MS. *Essays in Biochemistry* **2022**, EBC20220111. https://doi.org/10.1042/EBC20220111.
 - Stofella, M.; Skinner, S. P.; Sobott, F.; Houwing-Duistermaat, J.; Paci, E. High-Resolution Hydrogen–Deuterium Protection Factors from Sparse Mass Spectrometry Data Validated by Nuclear Magnetic Resonance Measurements. _J. Am. Soc. Mass Spectrom._ **2022**, _33_ (5), 813–822. [https://doi.org/10.1021/jasms.2c00005](https://doi.org/10.1021/jasms.2c00005).
 - Zhang, W.; Xiang, Y.; Xu, W. Probing Protein Higher-Order Structures by Native Capillary Electrophoresis-Mass Spectrometry. _TrAC Trends in Analytical Chemistry_ **2022**, _157_, 116739. [https://doi.org/10.1016/j.trac.2022.116739](https://doi.org/10.1016/j.trac.2022.116739).
@@ -52,6 +58,6 @@ See [HDXrate](https://github.com/Jhsmit/HDXrate) for a python implementation of
 - [Hadexversum HDX-MS-resources](https://github.com/hadexversum/HDX-MS-resources)  
 - [HDXMS.net resources](http://hdxms.net/resources/)
 
-**HDX-MS datasets (alpha):**
+**HDX-MS datasets:**
 
 - [hdxms-datasets on GitHub](https://github.com/Jhsmit/hdxms-datasets)