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Expanding the Disorder-Function Paradigm in the C-Terminal Tails of Erbbs.

Biomolecules

Pinet L, Assrir N, van Heijenoort C.
PMID: 34827688
Biomolecules. 2021 Nov 14;11(11). doi: 10.3390/biom11111690.

ErbBs are receptor tyrosine kinases involved not only in development, but also in a wide variety of diseases, particularly cancer. Their extracellular, transmembrane, juxtamembrane, and kinase folded domains were described extensively over the past 20 years, structurally and functionally....

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Pinet L, Assrir N, van Heijenoort C. Expanding the Disorder-Function Paradigm in the C-Terminal Tails of Erbbs. Biomolecules. 2021;11(11)doi: 10.3390/biom11111690.
Pinet, L., Assrir, N., & van Heijenoort, C. (2021). Expanding the Disorder-Function Paradigm in the C-Terminal Tails of Erbbs. Biomolecules, 11(11), . https://doi.org/10.3390/biom11111690
Pinet, Louise, et al. "Expanding the Disorder-Function Paradigm in the C-Terminal Tails of Erbbs." Biomolecules vol. 11,11 (2021). doi: https://doi.org/10.3390/biom11111690
Pinet L, Assrir N, van Heijenoort C. Expanding the Disorder-Function Paradigm in the C-Terminal Tails of Erbbs. Biomolecules. 2021 Nov 14;11(11). doi: 10.3390/biom11111690. PMID: 34827688; PMCID: PMC8615588.
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Quantitative proteomics identifies PTP1B as modulator of B cell antigen receptor signaling.

Life science alliance

Schwarz JJ, Grundmann L, Kokot T, Kläsener K, Fotteler S, Medgyesi D, Köhn M, Reth M, Warscheid B.
PMID: 34526379
Life Sci Alliance. 2021 Sep 15;4(11). doi: 10.26508/lsa.202101084. Print 2021 Nov.

B cell antigen receptor (BCR) signaling is initiated by protein kinases and limited by counteracting phosphatases that currently are less well studied in their regulation of BCR signaling. Here, we used the B cell line Ramos to identify and...

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Schwarz JJ, Grundmann L, Kokot T, et al. Quantitative proteomics identifies PTP1B as modulator of B cell antigen receptor signaling. Life Sci Alliance. 2021;4(11)doi: 10.26508/lsa.202101084.
Schwarz, J. J., Grundmann, L., Kokot, T., Kläsener, K., Fotteler, S., Medgyesi, D., Köhn, M., Reth, M., & Warscheid, B. (2021). Quantitative proteomics identifies PTP1B as modulator of B cell antigen receptor signaling. Life science alliance, 4(11), . https://doi.org/10.26508/lsa.202101084
Schwarz, Jennifer J, et al. "Quantitative proteomics identifies PTP1B as modulator of B cell antigen receptor signaling." Life science alliance vol. 4,11 (2021). doi: https://doi.org/10.26508/lsa.202101084
Schwarz JJ, Grundmann L, Kokot T, Kläsener K, Fotteler S, Medgyesi D, Köhn M, Reth M, Warscheid B. Quantitative proteomics identifies PTP1B as modulator of B cell antigen receptor signaling. Life Sci Alliance. 2021 Sep 15;4(11). doi: 10.26508/lsa.202101084. Print 2021 Nov. PMID: 34526379; PMCID: PMC8473724.
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[No title available]

HGG advances

Chmielewska JJ, Burkardt D, Granadillo JL, Slaugh R, Morgan S, Rotenberg J, Keren B, Mignot C, Escobar L, Turnpenny P, Zuteck M, Seaver LH, Ploski R, Dziembowska M, Wynshaw-Boris A, Adegbola A.
PMID: 34527963
HGG Adv. 2021 Jul 08;2(3). doi: 10.1016/j.xhgg.2021.100033. Epub 2021 Apr 05.

Protein-tyrosine phosphatases (PTPs) are pleomorphic regulators of eukaryotic cellular responses to extracellular signals that function by modulating the phosphotyrosine of specific proteins. A handful of PTPs have been implicated in germline and somatic human disease. Using exome sequencing, we...

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Chmielewska JJ, Burkardt D, Granadillo JL, et al. . HGG Adv. 2021;2(3)doi: 10.1016/j.xhgg.2021.100033.
Chmielewska, J. J., Burkardt, D., Granadillo, J. L., Slaugh, R., Morgan, S., Rotenberg, J., Keren, B., Mignot, C., Escobar, L., Turnpenny, P., Zuteck, M., Seaver, L. H., Ploski, R., Dziembowska, M., Wynshaw-Boris, A., & Adegbola, A. (2021). . HGG advances, 2(3), . https://doi.org/10.1016/j.xhgg.2021.100033
Chmielewska, Joanna J, et al. "." HGG advances vol. 2,3 (2021). doi: https://doi.org/10.1016/j.xhgg.2021.100033
Chmielewska JJ, Burkardt D, Granadillo JL, Slaugh R, Morgan S, Rotenberg J, Keren B, Mignot C, Escobar L, Turnpenny P, Zuteck M, Seaver LH, Ploski R, Dziembowska M, Wynshaw-Boris A, Adegbola A. . HGG Adv. 2021 Jul 08;2(3). doi: 10.1016/j.xhgg.2021.100033. Epub 2021 Apr 05. PMID: 34527963; PMCID: PMC8439436.
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Multifunctional lanthanide metal-organic framework based ratiometric fluorescence visual detection platform for alkaline phosphatase activity.

Mikrochimica acta

Xiong L, Yu L, Li S, Feng L, Xiao Y.
PMID: 34165637
Mikrochim Acta. 2021 Jun 24;188(7):236. doi: 10.1007/s00604-021-04880-4.

A turn-on/off ratiometric fluorescence detection platform based on multifunctional lanthanide metal-organic framework (Ln-MOF) and an enzymatic cascade reaction is proposed for alkaline phosphatase (ALP) activity assay. L-phosphotyrosine is hydrolyzed to levodopa (L-dopa) by two steps of enzymatic reaction. L-dopa...

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Xiong L, Yu L, Li S, et al. Multifunctional lanthanide metal-organic framework based ratiometric fluorescence visual detection platform for alkaline phosphatase activity. Mikrochim Acta. 2021;188(7):236doi: 10.1007/s00604-021-04880-4.
Xiong, L., Yu, L., Li, S., Feng, L., & Xiao, Y. (2021). Multifunctional lanthanide metal-organic framework based ratiometric fluorescence visual detection platform for alkaline phosphatase activity. Mikrochimica acta, 188(7), 236. https://doi.org/10.1007/s00604-021-04880-4
Xiong, Li, et al. "Multifunctional lanthanide metal-organic framework based ratiometric fluorescence visual detection platform for alkaline phosphatase activity." Mikrochimica acta vol. 188,7 (2021): 236. doi: https://doi.org/10.1007/s00604-021-04880-4
Xiong L, Yu L, Li S, Feng L, Xiao Y. Multifunctional lanthanide metal-organic framework based ratiometric fluorescence visual detection platform for alkaline phosphatase activity. Mikrochim Acta. 2021 Jun 24;188(7):236. doi: 10.1007/s00604-021-04880-4. PMID: 34165637.
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DUSP5 promotes osteogenic differentiation through SCP1/2-dependent phosphorylation of SMAD1.

Stem cells (Dayton, Ohio)

Liu X, Liu X, Du Y, Hu M, Tian Y, Li Z, Lv L, Zhang X, Liu Y, Zhou Y, Zhang P.
PMID: 34169608
Stem Cells. 2021 Oct;39(10):1395-1409. doi: 10.1002/stem.3428. Epub 2021 Jul 10.

Dual-specificity phosphatases (DUSPs) are defined by their capability to dephosphorylate both phosphoserine/phosphothreonine (pSer/pThr) and phosphotyrosine (pTyr). DUSP5, a member of DUSPs superfamily, is located in the nucleus and plays crucially regulatory roles in the signaling pathway transduction. In our...

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Liu X, Liu X, Du Y, et al. DUSP5 promotes osteogenic differentiation through SCP1/2-dependent phosphorylation of SMAD1. Stem Cells. 2021;39(10):1395-1409doi: 10.1002/stem.3428.
Liu, X., Liu, X., Du, Y., Hu, M., Tian, Y., Li, Z., Lv, L., Zhang, X., Liu, Y., Zhou, Y., & Zhang, P. (2021). DUSP5 promotes osteogenic differentiation through SCP1/2-dependent phosphorylation of SMAD1. Stem cells (Dayton, Ohio), 39(10), 1395-1409. https://doi.org/10.1002/stem.3428
Liu, Xuejiao, et al. "DUSP5 promotes osteogenic differentiation through SCP1/2-dependent phosphorylation of SMAD1." Stem cells (Dayton, Ohio) vol. 39,10 (2021): 1395-1409. doi: https://doi.org/10.1002/stem.3428
Liu X, Liu X, Du Y, Hu M, Tian Y, Li Z, Lv L, Zhang X, Liu Y, Zhou Y, Zhang P. DUSP5 promotes osteogenic differentiation through SCP1/2-dependent phosphorylation of SMAD1. Stem Cells. 2021 Oct;39(10):1395-1409. doi: 10.1002/stem.3428. Epub 2021 Jul 10. PMID: 34169608; PMCID: PMC8518947.
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Synthesis and structural characterization of a monocarboxylic inhibitor for GRB2 SH2 domain.

Bioorganic & medicinal chemistry letters

Xiao T, Sun L, Zhang M, Li Z, Haura EB, Schonbrunn E, Ji H.
PMID: 34506932
Bioorg Med Chem Lett. 2021 Nov 01;51:128354. doi: 10.1016/j.bmcl.2021.128354. Epub 2021 Sep 07.

A monocarboxylic inhibitor was designed and synthesized to disrupt the protein-protein interaction (PPI) between GRB2 and phosphotyrosine-containing proteins. Biochemical characterizations show compound 7 binds with the Src homology 2 (SH2) domain of GRB2 and is more potent than EGFR

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Xiao T, Sun L, Zhang M, et al. Synthesis and structural characterization of a monocarboxylic inhibitor for GRB2 SH2 domain. Bioorg Med Chem Lett. 2021;51:128354doi: 10.1016/j.bmcl.2021.128354.
Xiao, T., Sun, L., Zhang, M., Li, Z., Haura, E. B., Schonbrunn, E., & Ji, H. (2021). Synthesis and structural characterization of a monocarboxylic inhibitor for GRB2 SH2 domain. Bioorganic & medicinal chemistry letters, 51128354. https://doi.org/10.1016/j.bmcl.2021.128354
Xiao, Tao, et al. "Synthesis and structural characterization of a monocarboxylic inhibitor for GRB2 SH2 domain." Bioorganic & medicinal chemistry letters vol. 51 (2021): 128354. doi: https://doi.org/10.1016/j.bmcl.2021.128354
Xiao T, Sun L, Zhang M, Li Z, Haura EB, Schonbrunn E, Ji H. Synthesis and structural characterization of a monocarboxylic inhibitor for GRB2 SH2 domain. Bioorg Med Chem Lett. 2021 Nov 01;51:128354. doi: 10.1016/j.bmcl.2021.128354. Epub 2021 Sep 07. PMID: 34506932; PMCID: PMC8526398.
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Pharmacological Programming of Endosomal Signaling Activated by Small Molecule Ligands of the Follicle Stimulating Hormone Receptor.

Frontiers in pharmacology

Sposini S, De Pascali F, Richardson R, Sayers NS, Perrais D, Yu HN, Palmer S, Nataraja S, Reiter E, Hanyaloglu AC.
PMID: 33329002
Front Pharmacol. 2020 Nov 30;11:593492. doi: 10.3389/fphar.2020.593492. eCollection 2020.

Follicle-stimulating hormone receptor (FSHR) is a G protein-coupled receptor (GPCR) with pivotal roles in reproduction. One key mechanism dictating the signal activity of GPCRs is membrane trafficking. After binding its hormone FSH, FSHR undergoes internalization to very early endosomes...

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Sposini S, De Pascali F, Richardson R, et al. Pharmacological Programming of Endosomal Signaling Activated by Small Molecule Ligands of the Follicle Stimulating Hormone Receptor. Front Pharmacol. 2020;11:593492doi: 10.3389/fphar.2020.593492.
Sposini, S., De Pascali, F., Richardson, R., Sayers, N. S., Perrais, D., Yu, H. N., Palmer, S., Nataraja, S., Reiter, E., & Hanyaloglu, A. C. (2020). Pharmacological Programming of Endosomal Signaling Activated by Small Molecule Ligands of the Follicle Stimulating Hormone Receptor. Frontiers in pharmacology, 11593492. https://doi.org/10.3389/fphar.2020.593492
Sposini, Silvia, et al. "Pharmacological Programming of Endosomal Signaling Activated by Small Molecule Ligands of the Follicle Stimulating Hormone Receptor." Frontiers in pharmacology vol. 11 (2020): 593492. doi: https://doi.org/10.3389/fphar.2020.593492
Sposini S, De Pascali F, Richardson R, Sayers NS, Perrais D, Yu HN, Palmer S, Nataraja S, Reiter E, Hanyaloglu AC. Pharmacological Programming of Endosomal Signaling Activated by Small Molecule Ligands of the Follicle Stimulating Hormone Receptor. Front Pharmacol. 2020 Nov 30;11:593492. doi: 10.3389/fphar.2020.593492. eCollection 2020. PMID: 33329002; PMCID: PMC7734412.
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Characterization of Human Spermatic Subpopulations by ConA-Binding Sites and Tyrosine Phosphorylation during in vitro Capacitation and Acrosome Reaction.

Cells, tissues, organs

Sáez-Espinosa P, López-Huedo A, Robles-Gómez L, Huerta-Retamal N, Aizpurua J, Gómez-Torres MJ.
PMID: 33873194
Cells Tissues Organs. 2021;210(1):1-9. doi: 10.1159/000513275. Epub 2021 Apr 19.

Spermatozoa capacitation is a time-dependent physiological process essential for acquiring the fertilizing capacity. In this context, reorganization of spermatozoa surface sugars and tyrosine phosphorylation are some of the most important biochemical changes involved in capacitation. However, the relationship between...

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Sáez-Espinosa P, López-Huedo A, Robles-Gómez L, et al. Characterization of Human Spermatic Subpopulations by ConA-Binding Sites and Tyrosine Phosphorylation during in vitro Capacitation and Acrosome Reaction. Cells Tissues Organs. 2021;210(1):1-9doi: 10.1159/000513275.
Sáez-Espinosa, P., López-Huedo, A., Robles-Gómez, L., Huerta-Retamal, N., Aizpurua, J., & Gómez-Torres, M. J. (2021). Characterization of Human Spermatic Subpopulations by ConA-Binding Sites and Tyrosine Phosphorylation during in vitro Capacitation and Acrosome Reaction. Cells, tissues, organs, 210(1), 1-9. https://doi.org/10.1159/000513275
Sáez-Espinosa, Paula, et al. "Characterization of Human Spermatic Subpopulations by ConA-Binding Sites and Tyrosine Phosphorylation during in vitro Capacitation and Acrosome Reaction." Cells, tissues, organs vol. 210,1 (2021): 1-9. doi: https://doi.org/10.1159/000513275
Sáez-Espinosa P, López-Huedo A, Robles-Gómez L, Huerta-Retamal N, Aizpurua J, Gómez-Torres MJ. Characterization of Human Spermatic Subpopulations by ConA-Binding Sites and Tyrosine Phosphorylation during in vitro Capacitation and Acrosome Reaction. Cells Tissues Organs. 2021;210(1):1-9. doi: 10.1159/000513275. Epub 2021 Apr 19. PMID: 33873194.
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Showing 193 to 200 of 200 entries