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The Role of CD4+ T Follicular Helper Cells in HIV Infection: From the Germinal Center to the Periphery.

Frontiers in immunology

Thornhill JP, Fidler S, Klenerman P, Frater J, Phetsouphanh C.
PMID: 28194154
Front Immunol. 2017 Jan 30;8:46. doi: 10.3389/fimmu.2017.00046. eCollection 2017.

T follicular helper cells (TFh) are key components of the adaptive immune system; they are primarily found in germinal centers (GCs) where their interaction with B cells supports humoral immune responses and efficient antibody production. They are defined by...

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Thornhill JP, Fidler S, Klenerman P, et al. The Role of CD4+ T Follicular Helper Cells in HIV Infection: From the Germinal Center to the Periphery. Front Immunol. 2017;8:46doi: 10.3389/fimmu.2017.00046.
Thornhill, J. P., Fidler, S., Klenerman, P., Frater, J., & Phetsouphanh, C. (2017). The Role of CD4+ T Follicular Helper Cells in HIV Infection: From the Germinal Center to the Periphery. Frontiers in immunology, 846. https://doi.org/10.3389/fimmu.2017.00046
Thornhill, John Patrick, et al. "The Role of CD4+ T Follicular Helper Cells in HIV Infection: From the Germinal Center to the Periphery." Frontiers in immunology vol. 8 (2017): 46. doi: https://doi.org/10.3389/fimmu.2017.00046
Thornhill JP, Fidler S, Klenerman P, Frater J, Phetsouphanh C. The Role of CD4+ T Follicular Helper Cells in HIV Infection: From the Germinal Center to the Periphery. Front Immunol. 2017 Jan 30;8:46. doi: 10.3389/fimmu.2017.00046. eCollection 2017. PMID: 28194154; PMCID: PMC5277018.
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Cryogenic-temperature electron microscopy direct imaging of carbon nanotubes and graphene solutions in superacids.

Journal of microscopy

Kleinerman O, Parra-Vasquez AN, Green MJ, Behabtu N, Schmidt J, Kesselman E, Young CC, Cohen Y, Pasquali M, Talmon Y.
PMID: 25818279
J Microsc. 2015 Jul;259(1):16-25. doi: 10.1111/jmi.12243. Epub 2015 Mar 25.

Cryogenic electron microscopy (cryo-EM) is a powerful tool for imaging liquid and semiliquid systems. While cryogenic transmission electron microscopy (cryo-TEM) is a standard technique in many fields, cryogenic scanning electron microscopy (cryo-SEM) is still not that widely used and...

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Kleinerman O, Parra-Vasquez AN, Green MJ, et al. Cryogenic-temperature electron microscopy direct imaging of carbon nanotubes and graphene solutions in superacids. J Microsc. 2015;259(1):16-25doi: 10.1111/jmi.12243.
Kleinerman, O., Parra-Vasquez, A. N., Green, M. J., Behabtu, N., Schmidt, J., Kesselman, E., Young, C. C., Cohen, Y., Pasquali, M., & Talmon, Y. (2015). Cryogenic-temperature electron microscopy direct imaging of carbon nanotubes and graphene solutions in superacids. Journal of microscopy, 259(1), 16-25. https://doi.org/10.1111/jmi.12243
Kleinerman, O, et al. "Cryogenic-temperature electron microscopy direct imaging of carbon nanotubes and graphene solutions in superacids." Journal of microscopy vol. 259,1 (2015): 16-25. doi: https://doi.org/10.1111/jmi.12243
Kleinerman O, Parra-Vasquez AN, Green MJ, Behabtu N, Schmidt J, Kesselman E, Young CC, Cohen Y, Pasquali M, Talmon Y. Cryogenic-temperature electron microscopy direct imaging of carbon nanotubes and graphene solutions in superacids. J Microsc. 2015 Jul;259(1):16-25. doi: 10.1111/jmi.12243. Epub 2015 Mar 25. PMID: 25818279.
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Sensitive light-sheet microscopy in multiwell plates using an AFM cantilever.

Biomedical optics express

Ponjavic A, Ye Y, Laue E, Lee SF, Klenerman D.
PMID: 31065399
Biomed Opt Express. 2018 Nov 02;9(12):5863-5880. doi: 10.1364/BOE.9.005863. eCollection 2018 Dec 01.

We present a sensitive inverted light sheet microscope, capable of single-molecule fluorescence imaging of cells in 96-well plates. Light sheet microscope designs are often complex and costly, requiring custom-made sample chambers that are incompatible with standard cell culture samples....

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Ponjavic A, Ye Y, Laue E, et al. Sensitive light-sheet microscopy in multiwell plates using an AFM cantilever. Biomed Opt Express. 2018;9(12):5863-5880doi: 10.1364/BOE.9.005863.
Ponjavic, A., Ye, Y., Laue, E., Lee, S. F., & Klenerman, D. (2018). Sensitive light-sheet microscopy in multiwell plates using an AFM cantilever. Biomedical optics express, 9(12), 5863-5880. https://doi.org/10.1364/BOE.9.005863
Ponjavic, Aleks, et al. "Sensitive light-sheet microscopy in multiwell plates using an AFM cantilever." Biomedical optics express vol. 9,12 (2018): 5863-5880. doi: https://doi.org/10.1364/BOE.9.005863
Ponjavic A, Ye Y, Laue E, Lee SF, Klenerman D. Sensitive light-sheet microscopy in multiwell plates using an AFM cantilever. Biomed Opt Express. 2018 Nov 02;9(12):5863-5880. doi: 10.1364/BOE.9.005863. eCollection 2018 Dec 01. PMID: 31065399; PMCID: PMC6490997.
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Extrinsic Amyloid-Binding Dyes for Detection of Individual Protein Aggregates in Solution.

Analytical chemistry

Taylor CG, Meisl G, Horrocks MH, Zetterberg H, Knowles TPJ, Klenerman D.
PMID: 30059210
Anal Chem. 2018 Sep 04;90(17):10385-10393. doi: 10.1021/acs.analchem.8b02226. Epub 2018 Aug 13.

Protein aggregation is a key molecular feature underlying a wide array of neurodegenerative disorders, including Alzheimer's and Parkinson's diseases. To understand protein aggregation in molecular detail, it is crucial to be able to characterize the array of heterogeneous aggregates...

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Taylor CG, Meisl G, Horrocks MH, et al. Extrinsic Amyloid-Binding Dyes for Detection of Individual Protein Aggregates in Solution. Anal Chem. 2018;90(17):10385-10393doi: 10.1021/acs.analchem.8b02226.
Taylor, C. G., Meisl, G., Horrocks, M. H., Zetterberg, H., Knowles, T. P. J., & Klenerman, D. (2018). Extrinsic Amyloid-Binding Dyes for Detection of Individual Protein Aggregates in Solution. Analytical chemistry, 90(17), 10385-10393. https://doi.org/10.1021/acs.analchem.8b02226
Taylor, Christopher G, et al. "Extrinsic Amyloid-Binding Dyes for Detection of Individual Protein Aggregates in Solution." Analytical chemistry vol. 90,17 (2018): 10385-10393. doi: https://doi.org/10.1021/acs.analchem.8b02226
Taylor CG, Meisl G, Horrocks MH, Zetterberg H, Knowles TPJ, Klenerman D. Extrinsic Amyloid-Binding Dyes for Detection of Individual Protein Aggregates in Solution. Anal Chem. 2018 Sep 04;90(17):10385-10393. doi: 10.1021/acs.analchem.8b02226. Epub 2018 Aug 13. PMID: 30059210; PMCID: PMC6127805.
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Soluble amyloid beta-containing aggregates are present throughout the brain at early stages of Alzheimer's disease.

Brain communications

Sideris DI, Danial JSH, Emin D, Ruggeri FS, Xia Z, Zhang YP, Lobanova E, Dakin H, De S, Miller A, Sang JC, Knowles TPJ, Vendruscolo M, Fraser G, Crowther D, Klenerman D.
PMID: 34396107
Brain Commun. 2021 Jul 02;3(3):fcab147. doi: 10.1093/braincomms/fcab147. eCollection 2021.

Protein aggregation likely plays a key role in the initiation and spreading of Alzheimer's disease pathology through the brain. Soluble aggregates of amyloid beta are believed to play a key role in this process. However, the aggregates present in...

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Sideris DI, Danial JSH, Emin D, et al. Soluble amyloid beta-containing aggregates are present throughout the brain at early stages of Alzheimer's disease. Brain Commun. 2021;3(3):fcab147doi: 10.1093/braincomms/fcab147.
Sideris, D. I., Danial, J. S. H., Emin, D., Ruggeri, F. S., Xia, Z., Zhang, Y. P., Lobanova, E., Dakin, H., De, S., Miller, A., Sang, J. C., Knowles, T. P. J., Vendruscolo, M., Fraser, G., Crowther, D., & Klenerman, D. (2021). Soluble amyloid beta-containing aggregates are present throughout the brain at early stages of Alzheimer's disease. Brain communications, 3(3), fcab147. https://doi.org/10.1093/braincomms/fcab147
Sideris, Dimitrios I, et al. "Soluble amyloid beta-containing aggregates are present throughout the brain at early stages of Alzheimer's disease." Brain communications vol. 3,3 (2021): fcab147. doi: https://doi.org/10.1093/braincomms/fcab147
Sideris DI, Danial JSH, Emin D, Ruggeri FS, Xia Z, Zhang YP, Lobanova E, Dakin H, De S, Miller A, Sang JC, Knowles TPJ, Vendruscolo M, Fraser G, Crowther D, Klenerman D. Soluble amyloid beta-containing aggregates are present throughout the brain at early stages of Alzheimer's disease. Brain Commun. 2021 Jul 02;3(3):fcab147. doi: 10.1093/braincomms/fcab147. eCollection 2021. PMID: 34396107; PMCID: PMC8361392.
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Distribution of the heavy metals Co, Cu, and Pb in sediments and Typha spp. And Phragmites mauritianus in three Zambian wetlands.

Journal of environmental management

Nabuyanda MM, Kelderman P, van Bruggen J, Irvine K.
PMID: 34864515
J Environ Manage. 2021 Dec 02;304:114133. doi: 10.1016/j.jenvman.2021.114133. Epub 2021 Dec 02.

Zambia has been mining cobalt (Co), copper (Cu), and lead (Pb) for over a century, with discharges entering wetlands without investigations on the level of sediment pollution and how to solve it. This present study investigated: 1) the extent...

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Nabuyanda MM, Kelderman P, van Bruggen J, et al. Distribution of the heavy metals Co, Cu, and Pb in sediments and Typha spp. And Phragmites mauritianus in three Zambian wetlands. J Environ Manage. 2021;304:114133doi: 10.1016/j.jenvman.2021.114133.
Nabuyanda, M. M., Kelderman, P., van Bruggen, J., & Irvine, K. (2021). Distribution of the heavy metals Co, Cu, and Pb in sediments and Typha spp. And Phragmites mauritianus in three Zambian wetlands. Journal of environmental management, 304114133. https://doi.org/10.1016/j.jenvman.2021.114133
Nabuyanda, Misery Mulele, et al. "Distribution of the heavy metals Co, Cu, and Pb in sediments and Typha spp. And Phragmites mauritianus in three Zambian wetlands." Journal of environmental management vol. 304 (2021): 114133. doi: https://doi.org/10.1016/j.jenvman.2021.114133
Nabuyanda MM, Kelderman P, van Bruggen J, Irvine K. Distribution of the heavy metals Co, Cu, and Pb in sediments and Typha spp. And Phragmites mauritianus in three Zambian wetlands. J Environ Manage. 2021 Dec 02;304:114133. doi: 10.1016/j.jenvman.2021.114133. Epub 2021 Dec 02. PMID: 34864515.
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An immunodominant NP.

Nature immunology

Peng Y, Felce SL, Dong D, Penkava F, Mentzer AJ, Yao X, Liu G, Yin Z, Chen JL, Lu Y, Wellington D, Wing PAC, Dominey-Foy DCC, Jin C, Wang W, Hamid MA, Fernandes RA, Wang B, Fries A, Zhuang X, Ashley N, Rostron T, Waugh C, Sopp P, Hublitz P, Beveridge R, Tan TK, Dold C, Kwok AJ, Rich-Griffin C, Dejnirattisa W, Liu C, Kurupati P, Nassiri I, Watson RA, Tong O, Taylor CA, Kumar Sharma P, Sun B, Curion F, Revale S, Garner LC, Jansen K, Ferreira RC, Attar M, Fry JW, Russell RA, Stauss HJ, James W, Townsend A, Ho LP, Klenerman P, Mongkolsapaya J, Screaton GR, Dendrou C, Sansom SN, Bashford-Rogers R, Chain B, Smith GL, McKeating JA, Fairfax BP, Bowness P, McMichael AJ, Ogg G, Knight JC, Dong T.
PMID: 34853448
Nat Immunol. 2022 Jan;23(1):50-61. doi: 10.1038/s41590-021-01084-z. Epub 2021 Dec 01.

NP

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Peng Y, Felce SL, Dong D, et al. An immunodominant NP. Nat Immunol. 2021;23(1):50-61doi: 10.1038/s41590-021-01084-z.
Peng, Y., Felce, S. L., Dong, D., Penkava, F., Mentzer, A. J., Yao, X., Liu, G., Yin, Z., Chen, J. L., Lu, Y., Wellington, D., Wing, P. A. C., Dominey-Foy, D. C. C., Jin, C., Wang, W., Hamid, M. A., Fernandes, R. A., Wang, B., Fries, A., Zhuang, X., Ashley, N., Rostron, T., Waugh, C., Sopp, P., Hublitz, P., Beveridge, R., Tan, T. K., Dold, C., Kwok, A. J., Rich-Griffin, C., Dejnirattisa, W., Liu, C., Kurupati, P., Nassiri, I., Watson, R. A., Tong, O., Taylor, C. A., Kumar Sharma, P., Sun, B., Curion, F., Revale, S., Garner, L. C., Jansen, K., Ferreira, R. C., Attar, M., Fry, J. W., Russell, R. A., Stauss, H. J., James, W., Townsend, A., Ho, L. P., Klenerman, P., Mongkolsapaya, J., Screaton, G. R., Dendrou, C., Sansom, S. N., Bashford-Rogers, R., Chain, B., Smith, G. L., McKeating, J. A., Fairfax, B. P., Bowness, P., McMichael, A. J., Ogg, G., Knight, J. C., & Dong, T. (2022). An immunodominant NP. Nature immunology, 23(1), 50-61. https://doi.org/10.1038/s41590-021-01084-z
Peng, Yanchun, et al. "An immunodominant NP." Nature immunology vol. 23,1 (2022): 50-61. doi: https://doi.org/10.1038/s41590-021-01084-z
Peng Y, Felce SL, Dong D, Penkava F, Mentzer AJ, Yao X, Liu G, Yin Z, Chen JL, Lu Y, Wellington D, Wing PAC, Dominey-Foy DCC, Jin C, Wang W, Hamid MA, Fernandes RA, Wang B, Fries A, Zhuang X, Ashley N, Rostron T, Waugh C, Sopp P, Hublitz P, Beveridge R, Tan TK, Dold C, Kwok AJ, Rich-Griffin C, Dejnirattisa W, Liu C, Kurupati P, Nassiri I, Watson RA, Tong O, Taylor CA, Kumar Sharma P, Sun B, Curion F, Revale S, Garner LC, Jansen K, Ferreira RC, Attar M, Fry JW, Russell RA, Stauss HJ, James W, Townsend A, Ho LP, Klenerman P, Mongkolsapaya J, Screaton GR, Dendrou C, Sansom SN, Bashford-Rogers R, Chain B, Smith GL, McKeating JA, Fairfax BP, Bowness P, McMichael AJ, Ogg G, Knight JC, Dong T. An immunodominant NP. Nat Immunol. 2022 Jan;23(1):50-61. doi: 10.1038/s41590-021-01084-z. Epub 2021 Dec 01. PMID: 34853448; PMCID: PMC8709787.
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Alpha Synuclein only Forms Fibrils In Vitro when Larger than its Critical Size of 70 Monomers.

Chembiochem : a European journal of chemical biology

Sanchez SE, Whiten DR, Meisl G, Ruggeri FS, Hidari E, Klenerman D.
PMID: 34383993
Chembiochem. 2021 Oct 01;22(19):2867-2871. doi: 10.1002/cbic.202100285. Epub 2021 Aug 24.

The aggregation of α-synuclein into small soluble aggregates and then fibrils is important in the development and spreading of aggregates through the brain in Parkinson's disease. Fibrillar aggregates can grow by monomer addition and then break into fragments that...

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Sanchez SE, Whiten DR, Meisl G, et al. Alpha Synuclein only Forms Fibrils In Vitro when Larger than its Critical Size of 70 Monomers. Chembiochem. 2021;22(19):2867-2871doi: 10.1002/cbic.202100285.
Sanchez, S. E., Whiten, D. R., Meisl, G., Ruggeri, F. S., Hidari, E., & Klenerman, D. (2021). Alpha Synuclein only Forms Fibrils In Vitro when Larger than its Critical Size of 70 Monomers. Chembiochem : a European journal of chemical biology, 22(19), 2867-2871. https://doi.org/10.1002/cbic.202100285
Sanchez, Santiago Enrique, et al. "Alpha Synuclein only Forms Fibrils In Vitro when Larger than its Critical Size of 70 Monomers." Chembiochem : a European journal of chemical biology vol. 22,19 (2021): 2867-2871. doi: https://doi.org/10.1002/cbic.202100285
Sanchez SE, Whiten DR, Meisl G, Ruggeri FS, Hidari E, Klenerman D. Alpha Synuclein only Forms Fibrils In Vitro when Larger than its Critical Size of 70 Monomers. Chembiochem. 2021 Oct 01;22(19):2867-2871. doi: 10.1002/cbic.202100285. Epub 2021 Aug 24. PMID: 34383993; PMCID: PMC8518629.
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Tumour necrosis factor induces increased production of extracellular amyloid-β- and α-synuclein-containing aggregates by human Alzheimer's disease neurons.

Brain communications

Whiten DR, Brownjohn PW, Moore S, De S, Strano A, Zuo Y, Haneklaus M, Klenerman D, Livesey FJ.
PMID: 33543132
Brain Commun. 2020 Sep 15;2(2):fcaa146. doi: 10.1093/braincomms/fcaa146. eCollection 2020.

In addition to increased aberrant protein aggregation, inflammation has been proposed as a key element in the pathogenesis and progression of Alzheimer's disease. How inflammation interacts with other disease pathways and how protein aggregation increases during disease are not...

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Whiten DR, Brownjohn PW, Moore S, et al. Tumour necrosis factor induces increased production of extracellular amyloid-β- and α-synuclein-containing aggregates by human Alzheimer's disease neurons. Brain Commun. 2020;2(2):fcaa146doi: 10.1093/braincomms/fcaa146.
Whiten, D. R., Brownjohn, P. W., Moore, S., De, S., Strano, A., Zuo, Y., Haneklaus, M., Klenerman, D., & Livesey, F. J. (2020). Tumour necrosis factor induces increased production of extracellular amyloid-β- and α-synuclein-containing aggregates by human Alzheimer's disease neurons. Brain communications, 2(2), fcaa146. https://doi.org/10.1093/braincomms/fcaa146
Whiten, Daniel R, et al. "Tumour necrosis factor induces increased production of extracellular amyloid-β- and α-synuclein-containing aggregates by human Alzheimer's disease neurons." Brain communications vol. 2,2 (2020): fcaa146. doi: https://doi.org/10.1093/braincomms/fcaa146
Whiten DR, Brownjohn PW, Moore S, De S, Strano A, Zuo Y, Haneklaus M, Klenerman D, Livesey FJ. Tumour necrosis factor induces increased production of extracellular amyloid-β- and α-synuclein-containing aggregates by human Alzheimer's disease neurons. Brain Commun. 2020 Sep 15;2(2):fcaa146. doi: 10.1093/braincomms/fcaa146. eCollection 2020. PMID: 33543132; PMCID: PMC7850285.
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Optimising T cell (re)boosting strategies for adenoviral and modified vaccinia Ankara vaccine regimens in humans.

NPJ vaccines

Capone S, Brown A, Hartnell F, Sorbo MD, Traboni C, Vassilev V, Colloca S, Nicosia A, Cortese R, Folgori A, Klenerman P, Barnes E, Swadling L.
PMID: 33083029
NPJ Vaccines. 2020 Oct 12;5:94. doi: 10.1038/s41541-020-00240-0. eCollection 2020.

Simian adenoviral and modified vaccinia Ankara (MVA) viral vectors used in heterologous prime-boost strategies are potent inducers of T cells against encoded antigens and are in advanced testing as vaccine carriers for a wide range of infectious agents and...

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Capone S, Brown A, Hartnell F, et al. Optimising T cell (re)boosting strategies for adenoviral and modified vaccinia Ankara vaccine regimens in humans. NPJ Vaccines. 2020;5:94doi: 10.1038/s41541-020-00240-0.
Capone, S., Brown, A., Hartnell, F., Sorbo, M. D., Traboni, C., Vassilev, V., Colloca, S., Nicosia, A., Cortese, R., Folgori, A., Klenerman, P., Barnes, E., & Swadling, L. (2020). Optimising T cell (re)boosting strategies for adenoviral and modified vaccinia Ankara vaccine regimens in humans. NPJ vaccines, 594. https://doi.org/10.1038/s41541-020-00240-0
Capone, Stefania, et al. "Optimising T cell (re)boosting strategies for adenoviral and modified vaccinia Ankara vaccine regimens in humans." NPJ vaccines vol. 5 (2020): 94. doi: https://doi.org/10.1038/s41541-020-00240-0
Capone S, Brown A, Hartnell F, Sorbo MD, Traboni C, Vassilev V, Colloca S, Nicosia A, Cortese R, Folgori A, Klenerman P, Barnes E, Swadling L. Optimising T cell (re)boosting strategies for adenoviral and modified vaccinia Ankara vaccine regimens in humans. NPJ Vaccines. 2020 Oct 12;5:94. doi: 10.1038/s41541-020-00240-0. eCollection 2020. PMID: 33083029; PMCID: PMC7550607.
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Prognostic Value of Cell-Surface Vimentin-Positive CTCs in Pediatric Sarcomas.

Frontiers in oncology

Dao L, Ragoonanan D, Batth I, Satelli A, Foglesong J, Wang J, Zaky W, Gill JB, Liu D, Albert A, Gordon N, Huh W, Harrison D, Herzog C, Kleinerman E, Gorlick R, Daw N, Li S.
PMID: 34956881
Front Oncol. 2021 Dec 09;11:760267. doi: 10.3389/fonc.2021.760267. eCollection 2021.

BACKGROUND: Despite advances in care, the 5 year overall survival for patients with relapsed and or metastatic sarcoma remains as low as < 35%. Currently, there are no biomarkers available to assess disease status in patients with sarcomas and...

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Dao L, Ragoonanan D, Batth I, et al. Prognostic Value of Cell-Surface Vimentin-Positive CTCs in Pediatric Sarcomas. Front Oncol. 2021;11:760267doi: 10.3389/fonc.2021.760267.
Dao, L., Ragoonanan, D., Batth, I., Satelli, A., Foglesong, J., Wang, J., Zaky, W., Gill, J. B., Liu, D., Albert, A., Gordon, N., Huh, W., Harrison, D., Herzog, C., Kleinerman, E., Gorlick, R., Daw, N., & Li, S. (2021). Prognostic Value of Cell-Surface Vimentin-Positive CTCs in Pediatric Sarcomas. Frontiers in oncology, 11760267. https://doi.org/10.3389/fonc.2021.760267
Dao, Long, et al. "Prognostic Value of Cell-Surface Vimentin-Positive CTCs in Pediatric Sarcomas." Frontiers in oncology vol. 11 (2021): 760267. doi: https://doi.org/10.3389/fonc.2021.760267
Dao L, Ragoonanan D, Batth I, Satelli A, Foglesong J, Wang J, Zaky W, Gill JB, Liu D, Albert A, Gordon N, Huh W, Harrison D, Herzog C, Kleinerman E, Gorlick R, Daw N, Li S. Prognostic Value of Cell-Surface Vimentin-Positive CTCs in Pediatric Sarcomas. Front Oncol. 2021 Dec 09;11:760267. doi: 10.3389/fonc.2021.760267. eCollection 2021. PMID: 34956881; PMCID: PMC8695931.
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Defining T Cell Subsets in Human Tonsils Using ChipCytometry.

Journal of immunology (Baltimore, Md. : 1950)

Hagel JP, Bennett K, Buffa F, Klenerman P, Willberg CB, Powell K.
PMID: 34099545
J Immunol. 2021 Jun 15;206(12):3073-3082. doi: 10.4049/jimmunol.2100063. Epub 2021 Jun 07.

ChipCytometry is a multiplex imaging method that can be used to analyze either cell suspensions or tissue sections. Images are acquired by iterative cycles of immunostaining with fluorescently labeled Abs, followed by photobleaching, which allows the accumulation of multiple...

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Hagel JP, Bennett K, Buffa F, et al. Defining T Cell Subsets in Human Tonsils Using ChipCytometry. J Immunol. 2021;206(12):3073-3082doi: 10.4049/jimmunol.2100063.
Hagel, J. P., Bennett, K., Buffa, F., Klenerman, P., Willberg, C. B., & Powell, K. (2021). Defining T Cell Subsets in Human Tonsils Using ChipCytometry. Journal of immunology (Baltimore, Md. : 1950), 206(12), 3073-3082. https://doi.org/10.4049/jimmunol.2100063
Hagel, Joachim P, et al. "Defining T Cell Subsets in Human Tonsils Using ChipCytometry." Journal of immunology (Baltimore, Md. : 1950) vol. 206,12 (2021): 3073-3082. doi: https://doi.org/10.4049/jimmunol.2100063
Hagel JP, Bennett K, Buffa F, Klenerman P, Willberg CB, Powell K. Defining T Cell Subsets in Human Tonsils Using ChipCytometry. J Immunol. 2021 Jun 15;206(12):3073-3082. doi: 10.4049/jimmunol.2100063. Epub 2021 Jun 07. PMID: 34099545; PMCID: PMC8278278.
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