Author

K.-T. Pan

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 2 Cell Biology· 1 Immunology· 1

Signature Assays, Organisms & Methods

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Organism:human· 4 Assay:proteomics· 4 Research Focus:cell type annotation· 2 Research Focus:differential expression· 2 Approach:experimental assay· 2 Research Focus:protein folding & dynamics· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:clustering· 1

Frequent Co-Authors

H. Urlaub· 4 shared Y. Ji· 3 shared I. Silbern· 2 shared P. Fang· 2 shared T. Oellerich· 2 shared A. Buskin· 1 shared C. Doebele· 1 shared C. Johnson· 1 shared

Activity by Year

2020-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 27 mutual co-author links

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4 shared papersBiochemistry

H. Urlaub

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Functional genomics identifies extension of complex N-glycans as a mechanism to evade lysis by natural killer cells

X. Zhuang, J. Woods, Y. Ji, S. Scheich, F. Mo, M. Voss, H. Urlaub, K.-T. Pan, E. O. Long

The paper identifies SPPL3 as a gene that enables tumor cells to evade NK cell lysis by altering N-glycan structures, and shows that inhibiting N-glycan maturation restores NK sensitivity.

bioRxiv · Apr 3, 2023 · PreprintImmunology

Progressive protein aggregation in PRPF31 patient retinal pigment epithelium cells: the mechanism and its reversal through activation of autophagy

M. Georgiou, C. Yang, R. Atkinson, K.-T. Pan, A. Buskin, M. Moya Molina, J. Collin, J. Al-Aama, F. Goertler, S. E. J. Ludwig, T. Davey, R. Luhrmann, S. Nagaraja-Grellscheid, C. Johnson, R. Ali, , M. Lako

This study shows that PRPF31 mutations cause progressive protein aggregation in RPE cells, which can be reversed by autophagy activation.

bioRxiv · Oct 11, 2021 · PreprintCell Biology

Evaluation and Optimization of High-Field Asymmetric Waveform Ion Mobility Spectrometry for Multiplexed Quantitative Site-specific N-glycoproteomics

P. Fang, Y. Ji, I. Silbern, R. Viner, T. Oellerich, K.-T. Pan, H. Urlaub

This study optimizes FAIMS settings for improved identification and quantification of site-specific N-glycopeptides using TMT labeling and Glyco-SPS-MS3 methods.

bioRxiv · Mar 23, 2021Biochemistry

SugarQuant: a streamlined pipeline for multiplexed quantitative site-specific N-glycoproteomics

P. Fang, Y. Ji, I. Silbern, C. Doebele, M. Ninov, C. Lenz, T. Oellerich, K.-T. Pan, H. Urlaub

SugarQuant provides a pipeline for site-specific N-glycoproteomics, enabling confident quantification of glycoforms in complex samples.

bioRxiv · May 20, 2020Biochemistry