Tetyana A. Kudlyk
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Also affiliated: United States Food and Drug Administration (2023–2025); University of Arkansas Medical Center (2009–2016)
Research Areas
Biomedical Subjects
Links
Biography and Research Information
OverviewAI-generated summary
Tetyana Kudlyk's research investigates cellular transport mechanisms, with a focus on the Golgi apparatus and its role in protein glycosylation. Her work has explored the function of the Golgi-associated retrograde protein (GARP) complex, demonstrating its importance in maintaining Golgi glycosylation machinery and its interaction with COPI machinery and Golgi v-SNAREs. Studies have also examined the consequences of GARP dysfunction, including COPI displacement and depletion of specific proteins. Kudlyk has also contributed to research on the molecular mechanisms of inorganic arsenic-induced apoptosis in zebrafish and has been involved in generating and analyzing specific cell lines for research purposes. Her recent work has also included the analysis of SARS-CoV-2 sublineages in wastewater datasets. Kudlyk has published 20 papers, with a total of 663 citations and an h-index of 12. She has collaborated with researchers from the University of Arkansas for Medical Sciences, including Vladimir Lupashin and Amrita Khakurel.
Metrics
- h-index: 12
- Publications: 20
- Citations: 708
Selected Publications
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Wastewater dataset on the SARS-CoV-2 sublineages circulating in Central Arkansas, USA, post-COVID-19 pandemic (2025)
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Gene expression analyses reveal potential mechanism of inorganic arsenic‐induced apoptosis in zebrafish (2023)
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GARP dysfunction results in COPI displacement, depletion of Golgi v-SNAREs and calcium homeostasis proteins (2022)
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Generation and Analysis of hTERT-RPE1 VPS54 Knock-Out and Rescued Cell Lines (2022)
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GARP complex controls Golgi physiology by stabilizing COPI machinery and Golgi v-SNAREs (2022)
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The Golgi-associated retrograde protein (GARP) complex plays an essential role in the maintenance of the Golgi glycosylation machinery (2021)
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The Golgi-associated retrograde protein (GARP) complex plays an essential role in the maintenance of the Golgi glycosylation machinery (2020)
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Defects in COG-Mediated Golgi Trafficking Alter Endo-Lysosomal System in Human Cells (2019)
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More than just sugars: Conserved oligomeric Golgi complex deficiency causes glycosylation‐independent cellular defects (2018)
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COG lobe B sub-complex engages v-SNARE GS15 and functions via regulated interaction with lobe A sub-complex (2016)
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Identification of Rab41/6d Effectors Provides an Explanation for the Differential Effects of Rab41/6d and Rab6a/a' on Golgi Organization (2016)
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Expression of Functional Myc-Tagged Conserved Oligomeric Golgi (COG) Subcomplexes in Mammalian Cells (2014)
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Cog5–Cog7 crystal structure reveals interactions essential for the function of a multisubunit tethering complex (2014)
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Multipronged interaction of the COG complex with intracellular membranes (2014)
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Oxysterol-binding protein (OSBP) is required for the perinuclear localization of intra-Golgi v-SNAREs (2013)
Collaboration Network
Top Collaborators
- Conserved oligomeric Golgi complex specifically regulates the maintenance of Golgi glycosylation machinery
- COG complexes form spatial landmarks for distinct SNARE complexes
- Molecular Insights into Vesicle Tethering at the Golgi by the Conserved Oligomeric Golgi (COG) Complex and the Golgin TATA Element Modulatory Factor (TMF)
- The COG Complex, Rab6 and COPI Define a Novel Golgi Retrograde Trafficking Pathway that is Exploited by SubAB Toxin
- COG6 Interacts with a Subset of the Golgi SNAREs and Is Important for the Golgi Complex Integrity
Showing 5 of 18 shared publications
- Conserved oligomeric Golgi complex specifically regulates the maintenance of Golgi glycosylation machinery
- COG complexes form spatial landmarks for distinct SNARE complexes
- The COG Complex, Rab6 and COPI Define a Novel Golgi Retrograde Trafficking Pathway that is Exploited by SubAB Toxin
- COG6 Interacts with a Subset of the Golgi SNAREs and Is Important for the Golgi Complex Integrity
- More than just sugars: Conserved oligomeric Golgi complex deficiency causes glycosylation‐independent cellular defects
Showing 5 of 9 shared publications
- Conserved oligomeric Golgi complex specifically regulates the maintenance of Golgi glycosylation machinery
- COG complexes form spatial landmarks for distinct SNARE complexes
- The COG Complex, Rab6 and COPI Define a Novel Golgi Retrograde Trafficking Pathway that is Exploited by SubAB Toxin
- COG6 Interacts with a Subset of the Golgi SNAREs and Is Important for the Golgi Complex Integrity
- COG lobe B sub-complex engages v-SNARE GS15 and functions via regulated interaction with lobe A sub-complex
Showing 5 of 7 shared publications
- The Golgi-associated retrograde protein (GARP) complex plays an essential role in the maintenance of the Golgi glycosylation machinery
- GARP dysfunction results in COPI displacement, depletion of Golgi v-SNAREs and calcium homeostasis proteins
- Generation and Analysis of hTERT-RPE1 VPS54 Knock-Out and Rescued Cell Lines
- The Golgi-associated retrograde protein (GARP) complex plays an essential role in the maintenance of the Golgi glycosylation machinery
- GARP complex controls Golgi physiology by stabilizing COPI machinery and Golgi v-SNAREs
- More than just sugars: Conserved oligomeric Golgi complex deficiency causes glycosylation‐independent cellular defects
- COG lobe B sub-complex engages v-SNARE GS15 and functions via regulated interaction with lobe A sub-complex
- Defects in COG-Mediated Golgi Trafficking Alter Endo-Lysosomal System in Human Cells
- Defects in COG-Mediated Golgi Trafficking Alter Endo-Lysosomal System in Human Cells
- GARP dysfunction results in COPI displacement, depletion of Golgi v-SNAREs and calcium homeostasis proteins
- GARP complex controls Golgi physiology by stabilizing COPI machinery and Golgi v-SNAREs
- Conserved oligomeric Golgi complex specifically regulates the maintenance of Golgi glycosylation machinery
- The COG Complex, Rab6 and COPI Define a Novel Golgi Retrograde Trafficking Pathway that is Exploited by SubAB Toxin
- COG complexes form spatial landmarks for distinct SNARE complexes
- Molecular Insights into Vesicle Tethering at the Golgi by the Conserved Oligomeric Golgi (COG) Complex and the Golgin TATA Element Modulatory Factor (TMF)
- COG complexes form spatial landmarks for distinct SNARE complexes
- Molecular Insights into Vesicle Tethering at the Golgi by the Conserved Oligomeric Golgi (COG) Complex and the Golgin TATA Element Modulatory Factor (TMF)
- COG lobe B sub-complex engages v-SNARE GS15 and functions via regulated interaction with lobe A sub-complex
- Cog5–Cog7 crystal structure reveals interactions essential for the function of a multisubunit tethering complex
- The Golgi-associated retrograde protein (GARP) complex plays an essential role in the maintenance of the Golgi glycosylation machinery
- The Golgi-associated retrograde protein (GARP) complex plays an essential role in the maintenance of the Golgi glycosylation machinery
- GARP dysfunction results in COPI displacement, depletion of Golgi v-SNAREs and calcium homeostasis proteins
- GARP complex controls Golgi physiology by stabilizing COPI machinery and Golgi v-SNAREs
- Gene expression analyses reveal potential mechanism of inorganic arsenic‐induced apoptosis in zebrafish
- Wastewater dataset on the SARS-CoV-2 sublineages circulating in Central Arkansas, USA, post-COVID-19 pandemic
- Gene expression analyses reveal potential mechanism of inorganic arsenic‐induced apoptosis in zebrafish
- Wastewater dataset on the SARS-CoV-2 sublineages circulating in Central Arkansas, USA, post-COVID-19 pandemic
- The COG Complex, Rab6 and COPI Define a Novel Golgi Retrograde Trafficking Pathway that is Exploited by SubAB Toxin
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