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Optimized multiplex immunofluorescence single-cell analysis reveals tuft cell heterogeneity.

JCI insight

McKinley ET, Sui Y, Al-Kofahi Y, Millis BA, Tyska MJ, Roland JT, Santamaria-Pang A, Ohland CL, Jobin C, Franklin JL, Lau KS, Gerdes MJ, Coffey RJ.
PMID: 28570279
JCI Insight. 2017 Jun 02;2(11). doi: 10.1172/jci.insight.93487. eCollection 2017 Jun 02.

Intestinal tuft cells are a rare, poorly understood cell type recently shown to be a critical mediator of type 2 immune response to helminth infection. Here, we present advances in segmentation algorithms and analytical tools for multiplex immunofluorescence (MxIF),...

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McKinley ET, Sui Y, Al-Kofahi Y, et al. Optimized multiplex immunofluorescence single-cell analysis reveals tuft cell heterogeneity. JCI Insight. 2017;2(11)doi: 10.1172/jci.insight.93487.
McKinley, E. T., Sui, Y., Al-Kofahi, Y., Millis, B. A., Tyska, M. J., Roland, J. T., Santamaria-Pang, A., Ohland, C. L., Jobin, C., Franklin, J. L., Lau, K. S., Gerdes, M. J., & Coffey, R. J. (2017). Optimized multiplex immunofluorescence single-cell analysis reveals tuft cell heterogeneity. JCI insight, 2(11), . https://doi.org/10.1172/jci.insight.93487
McKinley, Eliot T, et al. "Optimized multiplex immunofluorescence single-cell analysis reveals tuft cell heterogeneity." JCI insight vol. 2,11 (2017). doi: https://doi.org/10.1172/jci.insight.93487
McKinley ET, Sui Y, Al-Kofahi Y, Millis BA, Tyska MJ, Roland JT, Santamaria-Pang A, Ohland CL, Jobin C, Franklin JL, Lau KS, Gerdes MJ, Coffey RJ. Optimized multiplex immunofluorescence single-cell analysis reveals tuft cell heterogeneity. JCI Insight. 2017 Jun 02;2(11). doi: 10.1172/jci.insight.93487. eCollection 2017 Jun 02. PMID: 28570279; PMCID: PMC5453701.
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Promotion of Tumor Invasion by Tumor-Associated Macrophages: The Role of CSF-1-Activated Phosphatidylinositol 3 Kinase and Src Family Kinase Motility Signaling.

Cancers

Dwyer AR, Greenland EL, Pixley FJ.
PMID: 28629162
Cancers (Basel). 2017 Jun 18;9(6). doi: 10.3390/cancers9060068.

Macrophages interact with cells in every organ to facilitate tissue development, function and repair. However, the close interaction between macrophages and parenchymal cells can be subverted in disease, particularly cancer. Motility is an essential capacity for macrophages to be...

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Dwyer AR, Greenland EL, Pixley FJ. Promotion of Tumor Invasion by Tumor-Associated Macrophages: The Role of CSF-1-Activated Phosphatidylinositol 3 Kinase and Src Family Kinase Motility Signaling. Cancers (Basel). 2017;9(6)doi: 10.3390/cancers9060068.
Dwyer, A. R., Greenland, E. L., & Pixley, F. J. (2017). Promotion of Tumor Invasion by Tumor-Associated Macrophages: The Role of CSF-1-Activated Phosphatidylinositol 3 Kinase and Src Family Kinase Motility Signaling. Cancers, 9(6), . https://doi.org/10.3390/cancers9060068
Dwyer, Amy R, et al. "Promotion of Tumor Invasion by Tumor-Associated Macrophages: The Role of CSF-1-Activated Phosphatidylinositol 3 Kinase and Src Family Kinase Motility Signaling." Cancers vol. 9,6 (2017). doi: https://doi.org/10.3390/cancers9060068
Dwyer AR, Greenland EL, Pixley FJ. Promotion of Tumor Invasion by Tumor-Associated Macrophages: The Role of CSF-1-Activated Phosphatidylinositol 3 Kinase and Src Family Kinase Motility Signaling. Cancers (Basel). 2017 Jun 18;9(6). doi: 10.3390/cancers9060068. PMID: 28629162; PMCID: PMC5483887.
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Canonical and Non-Canonical Aspects of JAK-STAT Signaling: Lessons from Interferons for Cytokine Responses.

Frontiers in immunology

Majoros A, Platanitis E, Kernbauer-Hölzl E, Rosebrock F, Müller M, Decker T.
PMID: 28184222
Front Immunol. 2017 Jan 26;8:29. doi: 10.3389/fimmu.2017.00029. eCollection 2017.

Janus kinase (JAK)-signal transducer and activator of transcription (STAT) signal transduction mediates cytokine responses. Canonical signaling is based on STAT tyrosine phosphorylation by activated JAKs. Downstream of interferon (IFN) receptors, activated JAKs cause the formation of the transcription factors...

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Majoros A, Platanitis E, Kernbauer-Hölzl E, et al. Canonical and Non-Canonical Aspects of JAK-STAT Signaling: Lessons from Interferons for Cytokine Responses. Front Immunol. 2017;8:29doi: 10.3389/fimmu.2017.00029.
Majoros, A., Platanitis, E., Kernbauer-Hölzl, E., Rosebrock, F., Müller, M., & Decker, T. (2017). Canonical and Non-Canonical Aspects of JAK-STAT Signaling: Lessons from Interferons for Cytokine Responses. Frontiers in immunology, 829. https://doi.org/10.3389/fimmu.2017.00029
Majoros, Andrea, et al. "Canonical and Non-Canonical Aspects of JAK-STAT Signaling: Lessons from Interferons for Cytokine Responses." Frontiers in immunology vol. 8 (2017): 29. doi: https://doi.org/10.3389/fimmu.2017.00029
Majoros A, Platanitis E, Kernbauer-Hölzl E, Rosebrock F, Müller M, Decker T. Canonical and Non-Canonical Aspects of JAK-STAT Signaling: Lessons from Interferons for Cytokine Responses. Front Immunol. 2017 Jan 26;8:29. doi: 10.3389/fimmu.2017.00029. eCollection 2017. PMID: 28184222; PMCID: PMC5266721.
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Exploring the Existing Drug Space for Novel pTyr Mimetic and SHP2 Inhibitors.

ACS medicinal chemistry letters

He R, Yu ZH, Zhang RY, Wu L, Gunawan AM, Lane BS, Shim JS, Zeng LF, He Y, Chen L, Wells CD, Liu JO, Zhang ZY.
PMID: 26191366
ACS Med Chem Lett. 2015 Jun 08;6(7):782-6. doi: 10.1021/acsmedchemlett.5b00118. eCollection 2015 Jul 09.

Protein tyrosine phosphatases (PTPs) are potential therapeutic targets for many diseases. Unfortunately, despite considerable drug discovery efforts devoted to PTPs, obtaining selective and cell permeable PTP inhibitors remains highly challenging. We describe a strategy to explore the existing drug...

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He R, Yu ZH, Zhang RY, et al. Exploring the Existing Drug Space for Novel pTyr Mimetic and SHP2 Inhibitors. ACS Med Chem Lett. 2015;6(7):782-6doi: 10.1021/acsmedchemlett.5b00118.
He, R., Yu, Z. H., Zhang, R. Y., Wu, L., Gunawan, A. M., Lane, B. S., Shim, J. S., Zeng, L. F., He, Y., Chen, L., Wells, C. D., Liu, J. O., & Zhang, Z. Y. (2015). Exploring the Existing Drug Space for Novel pTyr Mimetic and SHP2 Inhibitors. ACS medicinal chemistry letters, 6(7), 782-6. https://doi.org/10.1021/acsmedchemlett.5b00118
He, Rongjun, et al. "Exploring the Existing Drug Space for Novel pTyr Mimetic and SHP2 Inhibitors." ACS medicinal chemistry letters vol. 6,7 (2015): 782-6. doi: https://doi.org/10.1021/acsmedchemlett.5b00118
He R, Yu ZH, Zhang RY, Wu L, Gunawan AM, Lane BS, Shim JS, Zeng LF, He Y, Chen L, Wells CD, Liu JO, Zhang ZY. Exploring the Existing Drug Space for Novel pTyr Mimetic and SHP2 Inhibitors. ACS Med Chem Lett. 2015 Jun 08;6(7):782-6. doi: 10.1021/acsmedchemlett.5b00118. eCollection 2015 Jul 09. PMID: 26191366; PMCID: PMC4499873.
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Data on interleukin (IL)-2- and IL-15-dependent changes in IL-2R.

Data in brief

Osinalde N, Sánchez-Quiles V, Blagoev B, Kratchmarova I.
PMID: 28331895
Data Brief. 2017 Mar 02;11:499-506. doi: 10.1016/j.dib.2017.02.030. eCollection 2017 Apr.

We provide detailed datasets from our analysis of the proteins that associate with IL-2Rβ and IL-2Rγ in T-cells stimulated with IL-2 or IL-15 compared with resting T-cells, as identified by SILAC-based quantitative proteomics. We also include quantitative data regarding...

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Osinalde N, Sánchez-Quiles V, Blagoev B, et al. Data on interleukin (IL)-2- and IL-15-dependent changes in IL-2R. Data Brief. 2017;11:499-506doi: 10.1016/j.dib.2017.02.030.
Osinalde, N., Sánchez-Quiles, V., Blagoev, B., & Kratchmarova, I. (2017). Data on interleukin (IL)-2- and IL-15-dependent changes in IL-2R. Data in brief, 11499-506. https://doi.org/10.1016/j.dib.2017.02.030
Osinalde, Nerea, et al. "Data on interleukin (IL)-2- and IL-15-dependent changes in IL-2R." Data in brief vol. 11 (2017): 499-506. doi: https://doi.org/10.1016/j.dib.2017.02.030
Osinalde N, Sánchez-Quiles V, Blagoev B, Kratchmarova I. Data on interleukin (IL)-2- and IL-15-dependent changes in IL-2R. Data Brief. 2017 Mar 02;11:499-506. doi: 10.1016/j.dib.2017.02.030. eCollection 2017 Apr. PMID: 28331895; PMCID: PMC5345956.
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Tyrosine 601 of Bacillus subtilis DnaK Undergoes Phosphorylation and Is Crucial for Chaperone Activity and Heat Shock Survival.

Frontiers in microbiology

Shi L, Ravikumar V, Derouiche A, Macek B, Mijakovic I.
PMID: 27148221
Front Microbiol. 2016 Apr 19;7:533. doi: 10.3389/fmicb.2016.00533. eCollection 2016.

In order to screen for cellular substrates of the Bacillus subtilis BY-kinase PtkA, and its cognate phosphotyrosine-protein phosphatase PtpZ, we performed a triple Stable Isotope Labeling by Amino acids in Cell culture-based quantitative phosphoproteome analysis. Detected tyrosine phosphorylation sites...

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Shi L, Ravikumar V, Derouiche A, et al. Tyrosine 601 of Bacillus subtilis DnaK Undergoes Phosphorylation and Is Crucial for Chaperone Activity and Heat Shock Survival. Front Microbiol. 2016;7:533doi: 10.3389/fmicb.2016.00533.
Shi, L., Ravikumar, V., Derouiche, A., Macek, B., & Mijakovic, I. (2016). Tyrosine 601 of Bacillus subtilis DnaK Undergoes Phosphorylation and Is Crucial for Chaperone Activity and Heat Shock Survival. Frontiers in microbiology, 7533. https://doi.org/10.3389/fmicb.2016.00533
Shi, Lei, et al. "Tyrosine 601 of Bacillus subtilis DnaK Undergoes Phosphorylation and Is Crucial for Chaperone Activity and Heat Shock Survival." Frontiers in microbiology vol. 7 (2016): 533. doi: https://doi.org/10.3389/fmicb.2016.00533
Shi L, Ravikumar V, Derouiche A, Macek B, Mijakovic I. Tyrosine 601 of Bacillus subtilis DnaK Undergoes Phosphorylation and Is Crucial for Chaperone Activity and Heat Shock Survival. Front Microbiol. 2016 Apr 19;7:533. doi: 10.3389/fmicb.2016.00533. eCollection 2016. PMID: 27148221; PMCID: PMC4835898.
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The PTB Domain: The Name Doesn't Say It All.

Trends in endocrinology and metabolism: TEM

Margolis B.
PMID: 10461172
Trends Endocrinol Metab. 1999 Sep;10(7):262-267. doi: 10.1016/s1043-2760(99)00168-x.

The phosphotyrosine-binding domain is a recently described protein-protein interaction domain which, despite its name, is involved in both phosphotyrosine-dependent and -independent interactions. Proteins with this domain are involved in diverse cellular functions, ranging from receptor signaling to protein targeting.

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Margolis B. The PTB Domain: The Name Doesn't Say It All. Trends Endocrinol Metab. 1999;10(7):262-267doi: 10.1016/s1043-2760(99)00168-x.
Margolis, B. (1999). The PTB Domain: The Name Doesn't Say It All. Trends in endocrinology and metabolism: TEM, 10(7), 262-267. https://doi.org/10.1016/s1043-2760(99)00168-x
Margolis. "The PTB Domain: The Name Doesn't Say It All." Trends in endocrinology and metabolism: TEM vol. 10,7 (1999): 262-267. doi: https://doi.org/10.1016/s1043-2760(99)00168-x
Margolis B. The PTB Domain: The Name Doesn't Say It All. Trends Endocrinol Metab. 1999 Sep;10(7):262-267. doi: 10.1016/s1043-2760(99)00168-x. PMID: 10461172.
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Uncoupling of mitochondria activates protein phosphatases and inactivates MBP protein kinases.

Journal of Alzheimer's disease : JAD

Luo Y, Ingram VM.
PMID: 12214026
J Alzheimers Dis. 2001 Dec;3(6):593-598. doi: 10.3233/jad-2001-3610.

Dephosphorylation of PHF-tau was observed in carbonyl cyanide p-(trifluoromethoxy) phenylhydrazone (FCCP)-treated, but not in oligomycin-treated undifferentiated PC12 cells. FCCP depletes ATP levels by uncoupling oxidative phosphorylation and increases cytosolic calcium levels, while oligomycin inhibits the ATP synthase. We also...

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Luo Y, Ingram VM. Uncoupling of mitochondria activates protein phosphatases and inactivates MBP protein kinases. J Alzheimers Dis. 2001;3(6):593-598doi: 10.3233/jad-2001-3610.
Luo, Y., & Ingram, V. M. (2001). Uncoupling of mitochondria activates protein phosphatases and inactivates MBP protein kinases. Journal of Alzheimer's disease : JAD, 3(6), 593-598. https://doi.org/10.3233/jad-2001-3610
Luo, Yuan, and Ingram, Vernon M.. "Uncoupling of mitochondria activates protein phosphatases and inactivates MBP protein kinases." Journal of Alzheimer's disease : JAD vol. 3,6 (2001): 593-598. doi: https://doi.org/10.3233/jad-2001-3610
Luo Y, Ingram VM. Uncoupling of mitochondria activates protein phosphatases and inactivates MBP protein kinases. J Alzheimers Dis. 2001 Dec;3(6):593-598. doi: 10.3233/jad-2001-3610. PMID: 12214026.
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Oncogenes, Protein Tyrosine Kinases, and Signal Transduction.

Journal of biomedical science

Liu D, Wang LH.
PMID: 11725009
J Biomed Sci. 1994 Mar;1(2):65-82. doi: 10.1007/BF02257980.

Many oncogenes encode protein tyrosine kinases (PTKs). Oncogenic mutations of these genes invariably result in constitutive activation of these PTKs. Autophosphorylation of the PTKs and tyrosine phosphorylation of their cellular substrates are essential events for transmission of the mitogenic...

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Liu D, Wang LH. Oncogenes, Protein Tyrosine Kinases, and Signal Transduction. J Biomed Sci. 1994;1(2):65-82doi: 10.1007/BF02257980.
Liu, D., & Wang, L. H. (1994). Oncogenes, Protein Tyrosine Kinases, and Signal Transduction. Journal of biomedical science, 1(2), 65-82. https://doi.org/10.1007/BF02257980
Liu, D., and Wang, L.-H.. "Oncogenes, Protein Tyrosine Kinases, and Signal Transduction." Journal of biomedical science vol. 1,2 (1994): 65-82. doi: https://doi.org/10.1007/BF02257980
Liu D, Wang LH. Oncogenes, Protein Tyrosine Kinases, and Signal Transduction. J Biomed Sci. 1994 Mar;1(2):65-82. doi: 10.1007/BF02257980. PMID: 11725009.
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Cleavage of single-stranded DNA by the varphiX174 A protein: The A-single-stranded DNA covalent linkage.

Proceedings of the National Academy of Sciences of the United States of America

Sanhueza S, Eisenberg S.
PMID: 16593485
Proc Natl Acad Sci U S A. 1984 Jul;81(14):4285-9. doi: 10.1073/pnas.81.14.4285.

Phage varphiX174 A(*) protein cleaves single-stranded DNA and then binds to the 5'-phosphorylated terminus of the cleaved DNA fragment, forming a covalent protein-DNA complex. The bound A(*) protein can religate the termini to form covalently closed single-stranded circles. To...

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Sanhueza S, Eisenberg S. Cleavage of single-stranded DNA by the varphiX174 A protein: The A-single-stranded DNA covalent linkage. Proc Natl Acad Sci U S A. 1984;81(14):4285-9doi: 10.1073/pnas.81.14.4285.
Sanhueza, S., & Eisenberg, S. (1984). Cleavage of single-stranded DNA by the varphiX174 A protein: The A-single-stranded DNA covalent linkage. Proceedings of the National Academy of Sciences of the United States of America, 81(14), 4285-9. https://doi.org/10.1073/pnas.81.14.4285
Sanhueza, S, and Eisenberg, S. "Cleavage of single-stranded DNA by the varphiX174 A protein: The A-single-stranded DNA covalent linkage." Proceedings of the National Academy of Sciences of the United States of America vol. 81,14 (1984): 4285-9. doi: https://doi.org/10.1073/pnas.81.14.4285
Sanhueza S, Eisenberg S. Cleavage of single-stranded DNA by the varphiX174 A protein: The A-single-stranded DNA covalent linkage. Proc Natl Acad Sci U S A. 1984 Jul;81(14):4285-9. doi: 10.1073/pnas.81.14.4285. PMID: 16593485; PMCID: PMC345572.
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Human Lp(a): regions in sequences of apoproteins similar to domains in signal transduction proteins.

Endocrine practice : official journal of the American College of Endocrinology and the American Association of Clinical Endocrinologists

Guevara J, Valentinova NV, Davison D, Morrisett JD, Sparrow JT.
PMID: 15251573
Endocr Pract. 1995 Nov-Dec;1(6):440-8. doi: 10.4158/EP.1.6.440.

The major apoproteins of Lp(a)--apo(a) and apo B-100--are linked by only one intermolecular disulfide bond. This linkage has been suggested to be located between apo(a) Cys4057 and apo B-100 Cys3734. Several studies, however, have suggested other noncovalent interactions between...

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Guevara J, Valentinova NV, Davison D, et al. Human Lp(a): regions in sequences of apoproteins similar to domains in signal transduction proteins. Endocr Pract. 1995;1(6):440-8doi: 10.4158/EP.1.6.440.
Guevara, J., Valentinova, N. V., Davison, D., Morrisett, J. D., & Sparrow, J. T. (1995). Human Lp(a): regions in sequences of apoproteins similar to domains in signal transduction proteins. Endocrine practice : official journal of the American College of Endocrinology and the American Association of Clinical Endocrinologists, 1(6), 440-8. https://doi.org/10.4158/EP.1.6.440
Guevara, J, et al. "Human Lp(a): regions in sequences of apoproteins similar to domains in signal transduction proteins." Endocrine practice : official journal of the American College of Endocrinology and the American Association of Clinical Endocrinologists vol. 1,6 (1995): 440-8. doi: https://doi.org/10.4158/EP.1.6.440
Guevara J, Valentinova NV, Davison D, Morrisett JD, Sparrow JT. Human Lp(a): regions in sequences of apoproteins similar to domains in signal transduction proteins. Endocr Pract. 1995 Nov-Dec;1(6):440-8. doi: 10.4158/EP.1.6.440. PMID: 15251573.
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Signal transduction drug discovery: targets, mechanisms and structure-based design.

Current opinion in drug discovery & development

Dalgarno DC, Metcalf CA, Shakespeare WC, Sawyer TK.
PMID: 19649883
Curr Opin Drug Discov Devel. 2000 Sep;3(5):549-64.

Signal transduction targets include catalytic and/or non-catalytic domains, which are critical to various aspects of cell growth, differentiation, metabolism and function, mitogenesis, motility and gene transcription. Specific examples of molecular targets include the catalytic domains of protein tyrosine kinases...

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Dalgarno DC, Metcalf CA, Shakespeare WC, et al. Signal transduction drug discovery: targets, mechanisms and structure-based design. Curr Opin Drug Discov Devel. 2000;3(5):549-64
Dalgarno, D. C., Metcalf, C. A., Shakespeare, W. C., & Sawyer, T. K. (2000). Signal transduction drug discovery: targets, mechanisms and structure-based design. Current opinion in drug discovery & development, 3(5), 549-64.
Dalgarno, D C, et al. "Signal transduction drug discovery: targets, mechanisms and structure-based design." Current opinion in drug discovery & development vol. 3,5 (2000): 549-64.
Dalgarno DC, Metcalf CA, Shakespeare WC, Sawyer TK. Signal transduction drug discovery: targets, mechanisms and structure-based design. Curr Opin Drug Discov Devel. 2000 Sep;3(5):549-64. PMID: 19649883.
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Showing 1 to 12 of 200 entries