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Current · Arkansas
Last published
2025
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OpenAlex · ORCID
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2026-10-07
T
Tetyana A. Kudlyk
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Also affiliated: United States Food and Drug Administration (2023–2025); University of Arkansas Medical Center (2009–2016)
12 h-index
20 pubs
708 cited
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
Vladimir Lupashin
University of Arkansas for Medical Sciences
18 shared publications
In database
- 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
Irina D. Pokrovskaya
University of Arkansas for Medical Sciences
9 shared publications
In database
- 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
Rose Willett
University of Arkansas at Little Rock
7 shared publications
In database
- 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
Amrita Khakurel
University of Arkansas for Medical Sciences
5 shared publications
In database
- 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
Jessica B. Blackburn
University of Arkansas for Medical Sciences (US)
3 shared publications
- 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
Zinia D’Souza
University of Arkansas for Medical Sciences
3 shared publications
In database
- 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
Richard D. Smith
University of Arkansas for Medical Sciences (US)
2 shared publications
- 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
Dániel Ungár
University of York (GB)
2 shared publications
- 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)
Rainer Duden
University of Lübeck (DE)
2 shared publications
- 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)
Leslie K. Climer
University of Arkansas at Little Rock (US)
2 shared publications
- 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
Juan S. Bonifacino
National Institutes of Health (US)
2 shared publications
- 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
I. V. Pokrovskaya
University of Arkansas for Medical Sciences
2 shared publications
In database
- 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
Camila Silva
National Center for Toxicological Research
2 shared publications
In database
- 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
Volodymyr Tryndyak
National Center for Toxicological Research
2 shared publications
In database
- 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
Adrienne W. Paton
The University of Adelaide (AU)
1 shared publication
- The COG Complex, Rab6 and COPI Define a Novel Golgi Retrograde Trafficking Pathway that is Exploited by SubAB Toxin
Similar Researchers
Based on overlapping research topics
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