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A Membrane-Permeable and Immobilized Metal Affinity Chromatography (IMAC)-Enrichable Cross-Linking Reagent to Advance In Vivo Cross-Linking Mass Spectrometry.

Angewandte Chemie (International ed. in English)

Jiang PL, Wang C, Diehl A, Viner R, Etienne C, Nandhikonda P, Foster L, Bomgarden RD, Liu F.
PMID: 34927332
Angew Chem Int Ed Engl. 2021 Dec 19; doi: 10.1002/anie.202113937. Epub 2021 Dec 19.

Cross-linking mass spectrometry (XL-MS) is an attractive method for the proteome-wide characterization of protein structures and interactions. Currently, the depth of in vivo XL-MS studies is lagging behind the established applications to cell lysates, because cross-linking reagents that can...

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Jiang PL, Wang C, Diehl A, et al. A Membrane-Permeable and Immobilized Metal Affinity Chromatography (IMAC)-Enrichable Cross-Linking Reagent to Advance In Vivo Cross-Linking Mass Spectrometry. Angew Chem Int Ed Engl. 2021;doi: 10.1002/anie.202113937.
Jiang, P. L., Wang, C., Diehl, A., Viner, R., Etienne, C., Nandhikonda, P., Foster, L., Bomgarden, R. D., & Liu, F. (2021). A Membrane-Permeable and Immobilized Metal Affinity Chromatography (IMAC)-Enrichable Cross-Linking Reagent to Advance In Vivo Cross-Linking Mass Spectrometry. Angewandte Chemie (International ed. in English), . https://doi.org/10.1002/anie.202113937
Jiang, Pin-Lian, et al. "A Membrane-Permeable and Immobilized Metal Affinity Chromatography (IMAC)-Enrichable Cross-Linking Reagent to Advance In Vivo Cross-Linking Mass Spectrometry." Angewandte Chemie (International ed. in English) vol. (2021). doi: https://doi.org/10.1002/anie.202113937
Jiang PL, Wang C, Diehl A, Viner R, Etienne C, Nandhikonda P, Foster L, Bomgarden RD, Liu F. A Membrane-Permeable and Immobilized Metal Affinity Chromatography (IMAC)-Enrichable Cross-Linking Reagent to Advance In Vivo Cross-Linking Mass Spectrometry. Angew Chem Int Ed Engl. 2021 Dec 19; doi: 10.1002/anie.202113937. Epub 2021 Dec 19. PMID: 34927332.
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Cross-Linking Strategies for Fluorine-Containing Polymer Coatings for Durable Resistant Water- and Oil-Repellency.

Polymers

Kredel J, Schmitt D, Schäfer JL, Biesalski M, Gallei M.
PMID: 33673433
Polymers (Basel). 2021 Feb 27;13(5). doi: 10.3390/polym13050723.

Functional coatings for application on surfaces are of growing interest. Especially in the textile industry, durable water and oil repellent finishes are of special demand for implementation in the outdoor sector, but also as safety-protection clothes against oil or...

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Kredel J, Schmitt D, Schäfer JL, et al. Cross-Linking Strategies for Fluorine-Containing Polymer Coatings for Durable Resistant Water- and Oil-Repellency. Polymers (Basel). 2021;13(5)doi: 10.3390/polym13050723.
Kredel, J., Schmitt, D., Schäfer, J. L., Biesalski, M., & Gallei, M. (2021). Cross-Linking Strategies for Fluorine-Containing Polymer Coatings for Durable Resistant Water- and Oil-Repellency. Polymers, 13(5), . https://doi.org/10.3390/polym13050723
Kredel, Julia, et al. "Cross-Linking Strategies for Fluorine-Containing Polymer Coatings for Durable Resistant Water- and Oil-Repellency." Polymers vol. 13,5 (2021). doi: https://doi.org/10.3390/polym13050723
Kredel J, Schmitt D, Schäfer JL, Biesalski M, Gallei M. Cross-Linking Strategies for Fluorine-Containing Polymer Coatings for Durable Resistant Water- and Oil-Repellency. Polymers (Basel). 2021 Feb 27;13(5). doi: 10.3390/polym13050723. PMID: 33673433; PMCID: PMC7956606.
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Synthesis of cross-linked core-shell polymer particles by free-radical dispersion copolymerization of 4-vinylpyridine with polystyrene macromonomers in nonaqueous media.

Journal of colloid and interface science

Ishizu K, Yasuda M, Tamura T.
PMID: 14583207
J Colloid Interface Sci. 2003 Nov 15;267(2):320-5. doi: 10.1016/s0021-9797(03)00704-5.

Cross-linked core-shell polymer particles were synthesized by free-radical dispersion copolymerization of 4-vinylpyridine (4VP) and various kinds of cross-linking reagents with methacryloyl-terminated polystyrene (PS) macromonomers in nonaqueous media such as 1,4-dioxane and cyclohexane. Well-defined particles were obtained by copolymerization of...

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Ishizu K, Yasuda M, Tamura T. Synthesis of cross-linked core-shell polymer particles by free-radical dispersion copolymerization of 4-vinylpyridine with polystyrene macromonomers in nonaqueous media. J Colloid Interface Sci. 2003;267(2):320-5doi: 10.1016/s0021-9797(03)00704-5.
Ishizu, K., Yasuda, M., & Tamura, T. (2003). Synthesis of cross-linked core-shell polymer particles by free-radical dispersion copolymerization of 4-vinylpyridine with polystyrene macromonomers in nonaqueous media. Journal of colloid and interface science, 267(2), 320-5. https://doi.org/10.1016/s0021-9797(03)00704-5
Ishizu, Koji, et al. "Synthesis of cross-linked core-shell polymer particles by free-radical dispersion copolymerization of 4-vinylpyridine with polystyrene macromonomers in nonaqueous media." Journal of colloid and interface science vol. 267,2 (2003): 320-5. doi: https://doi.org/10.1016/s0021-9797(03)00704-5
Ishizu K, Yasuda M, Tamura T. Synthesis of cross-linked core-shell polymer particles by free-radical dispersion copolymerization of 4-vinylpyridine with polystyrene macromonomers in nonaqueous media. J Colloid Interface Sci. 2003 Nov 15;267(2):320-5. doi: 10.1016/s0021-9797(03)00704-5. PMID: 14583207.
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The use of natural biopolymer of chitosan as biodegradable beads for local antibiotic delivery: release studies.

Jundishapur journal of natural pharmaceutical products

Movaffagh J, Ghodsi A, Fazly Bazzaz BS, Sajadi Tabassi SA, Ghodrati Azadi H.
PMID: 24624183
Jundishapur J Nat Pharm Prod. 2013;8(1):27-33. Epub 2013 Feb 13.

BACKGROUND: Chitosan is a naturally occurring biopolymer which has been widely used in a variety of biomedical applications including local antibiotic delivery due to its excellent mechanical properties, biodegradability and biocompatibility. Beads are spherical, porous carriers which are prepared...

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Movaffagh J, Ghodsi A, Fazly Bazzaz BS, et al. The use of natural biopolymer of chitosan as biodegradable beads for local antibiotic delivery: release studies. Jundishapur J Nat Pharm Prod. 2013;8(1):27-33
Movaffagh, J., Ghodsi, A., Fazly Bazzaz, B. S., Sajadi Tabassi, S. A., & Ghodrati Azadi, H. (2013). The use of natural biopolymer of chitosan as biodegradable beads for local antibiotic delivery: release studies. Jundishapur journal of natural pharmaceutical products, 8(1), 27-33.
Movaffagh, Jebraeel, et al. "The use of natural biopolymer of chitosan as biodegradable beads for local antibiotic delivery: release studies." Jundishapur journal of natural pharmaceutical products vol. 8,1 (2013): 27-33.
Movaffagh J, Ghodsi A, Fazly Bazzaz BS, Sajadi Tabassi SA, Ghodrati Azadi H. The use of natural biopolymer of chitosan as biodegradable beads for local antibiotic delivery: release studies. Jundishapur J Nat Pharm Prod. 2013;8(1):27-33. Epub 2013 Feb 13. PMID: 24624183; PMCID: PMC3941884.
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Programmable and Bidirectional Bending of Soft Actuators Based on Janus Structure with Sticky Tough PAA-Clay Hydrogel.

ACS applied materials & interfaces

Zhao L, Huang J, Zhang Y, Wang T, Sun W, Tong Z.
PMID: 28290198
ACS Appl Mater Interfaces. 2017 Apr 05;9(13):11866-11873. doi: 10.1021/acsami.7b00138. Epub 2017 Mar 24.

Facile preparation, rapid actuating, and versatile actions are great challenges in exploring new kinds of hydrogel actuators. In this paper, we presented a facile sticking method to prepare Janus bilayer and multilayer hydrogel actuators that benefited from a special...

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Zhao L, Huang J, Zhang Y, et al. Programmable and Bidirectional Bending of Soft Actuators Based on Janus Structure with Sticky Tough PAA-Clay Hydrogel. ACS Appl Mater Interfaces. 2017;9(13):11866-11873doi: 10.1021/acsami.7b00138.
Zhao, L., Huang, J., Zhang, Y., Wang, T., Sun, W., & Tong, Z. (2017). Programmable and Bidirectional Bending of Soft Actuators Based on Janus Structure with Sticky Tough PAA-Clay Hydrogel. ACS applied materials & interfaces, 9(13), 11866-11873. https://doi.org/10.1021/acsami.7b00138
Zhao, Lei, et al. "Programmable and Bidirectional Bending of Soft Actuators Based on Janus Structure with Sticky Tough PAA-Clay Hydrogel." ACS applied materials & interfaces vol. 9,13 (2017): 11866-11873. doi: https://doi.org/10.1021/acsami.7b00138
Zhao L, Huang J, Zhang Y, Wang T, Sun W, Tong Z. Programmable and Bidirectional Bending of Soft Actuators Based on Janus Structure with Sticky Tough PAA-Clay Hydrogel. ACS Appl Mater Interfaces. 2017 Apr 05;9(13):11866-11873. doi: 10.1021/acsami.7b00138. Epub 2017 Mar 24. PMID: 28290198.
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The effect of detergent on the structure and composition of chlorosomes isolated from Chloroflexus aurantiacus.

Photosynthesis research

Miller M, Simpson D, Redlinger TE.
PMID: 24318757
Photosynth Res. 1993 Mar;35(3):275-83. doi: 10.1007/BF00016558.

Isolated chlorosomes, treated with the detergent lithium dodecyl sulfate (LDS), can be separated into two green fractions by agarose gel electrophoresis. One fraction contains chlorosomes with a full complement of proteins and antenna BChl c absorbing at 740 nm,...

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Miller M, Simpson D, Redlinger TE. The effect of detergent on the structure and composition of chlorosomes isolated from Chloroflexus aurantiacus. Photosynth Res. 1993;35(3):275-83doi: 10.1007/BF00016558.
Miller, M., Simpson, D., & Redlinger, T. E. (1993). The effect of detergent on the structure and composition of chlorosomes isolated from Chloroflexus aurantiacus. Photosynthesis research, 35(3), 275-83. https://doi.org/10.1007/BF00016558
Miller, M, et al. "The effect of detergent on the structure and composition of chlorosomes isolated from Chloroflexus aurantiacus." Photosynthesis research vol. 35,3 (1993): 275-83. doi: https://doi.org/10.1007/BF00016558
Miller M, Simpson D, Redlinger TE. The effect of detergent on the structure and composition of chlorosomes isolated from Chloroflexus aurantiacus. Photosynth Res. 1993 Mar;35(3):275-83. doi: 10.1007/BF00016558. PMID: 24318757.
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β-endorphin binding in cultured adrenal cortical cells.

Endocrine

Gelfand RA, Bobrow A, Pham L, Young C, Parker L.
PMID: 21153195
Endocrine. 1995 Mar;3(3):201-7. doi: 10.1007/BF02994444.

The polypeptide β-endorphin binds to cultured bovine adrenal cortical cells in a naloxone insensitive manner, β-endorphin and N-Acetyl-β-endorphin are equipotent in inhibiting binding. The amino terminal 27 amino acid fragment referred to as β-endorphin[1-27] shows no ability to inhibit...

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Gelfand RA, Bobrow A, Pham L, et al. β-endorphin binding in cultured adrenal cortical cells. Endocrine. 1995;3(3):201-7doi: 10.1007/BF02994444.
Gelfand, R. A., Bobrow, A., Pham, L., Young, C., & Parker, L. (1995). β-endorphin binding in cultured adrenal cortical cells. Endocrine, 3(3), 201-7. https://doi.org/10.1007/BF02994444
Gelfand, R A, et al. "β-endorphin binding in cultured adrenal cortical cells." Endocrine vol. 3,3 (1995): 201-7. doi: https://doi.org/10.1007/BF02994444
Gelfand RA, Bobrow A, Pham L, Young C, Parker L. β-endorphin binding in cultured adrenal cortical cells. Endocrine. 1995 Mar;3(3):201-7. doi: 10.1007/BF02994444. PMID: 21153195.
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Development of a fluoroimmunosensor for theophylline using immobilised antibody.

Talanta

Garcinuño RM, Fernández P, Pérez-Conde C, Gutiérrez AM, Cámara C.
PMID: 18968042
Talanta. 2000 Aug 16;52(5):825-32.

A flowthrough theophylline fluoroimmunosensor with an antibody covalently immobilised on a solid support has been developed. The immobilisation technique proposed in this paper used Protein-A on control pore glass (Protein A-CPG) in an immunoreactor and dimethylsuberimidate as a cross-linking...

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Garcinuño RM, Fernández P, Pérez-Conde C, et al. Development of a fluoroimmunosensor for theophylline using immobilised antibody. Talanta. 2000;52(5):825-32
Garcinuño, R. M., Fernández, P., Pérez-Conde, C., Gutiérrez, A. M., & Cámara, C. (2000). Development of a fluoroimmunosensor for theophylline using immobilised antibody. Talanta, 52(5), 825-32.
Garcinuño, R M, et al. "Development of a fluoroimmunosensor for theophylline using immobilised antibody." Talanta vol. 52,5 (2000): 825-32.
Garcinuño RM, Fernández P, Pérez-Conde C, Gutiérrez AM, Cámara C. Development of a fluoroimmunosensor for theophylline using immobilised antibody. Talanta. 2000 Aug 16;52(5):825-32. PMID: 18968042.
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Delayed-Onset Transient Light Sensitivity Syndrome after Corneal Collagen Cross-Linking: A Case Series.

Medical hypothesis, discovery & innovation ophthalmology journal

Moshirfar M, Vaidyanathan U, Hopping GC, Ronquillo YC, Hoopes PC.
PMID: 31598524
Med Hypothesis Discov Innov Ophthalmol. 2019;8(3):250-256.

In this case series, we report a potentially novel association of corneal collagen crosslinking (CCL) with the development of photophobia symptoms in a series of patients at a tertiary ophthalmology clinic and describe their clinical course. Photosensitivity is a...

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Moshirfar M, Vaidyanathan U, Hopping GC, et al. Delayed-Onset Transient Light Sensitivity Syndrome after Corneal Collagen Cross-Linking: A Case Series. Med Hypothesis Discov Innov Ophthalmol. 2019;8(3):250-256
Moshirfar, M., Vaidyanathan, U., Hopping, G. C., Ronquillo, Y. C., & Hoopes, P. C. (2019). Delayed-Onset Transient Light Sensitivity Syndrome after Corneal Collagen Cross-Linking: A Case Series. Medical hypothesis, discovery & innovation ophthalmology journal, 8(3), 250-256.
Moshirfar, Majid, et al. "Delayed-Onset Transient Light Sensitivity Syndrome after Corneal Collagen Cross-Linking: A Case Series." Medical hypothesis, discovery & innovation ophthalmology journal vol. 8,3 (2019): 250-256.
Moshirfar M, Vaidyanathan U, Hopping GC, Ronquillo YC, Hoopes PC. Delayed-Onset Transient Light Sensitivity Syndrome after Corneal Collagen Cross-Linking: A Case Series. Med Hypothesis Discov Innov Ophthalmol. 2019;8(3):250-256. PMID: 31598524; PMCID: PMC6778466.
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Identification of Full-Length Wild-Type and Mutant Huntingtin Interacting Proteins by Crosslinking Immunoprecipitation in Mice Brain Cortex.

Journal of Huntington's disease

Sap KA, Guler AT, Bury A, Dekkers D, Demmers JAA, Reits EA.
PMID: 34151850
J Huntingtons Dis. 2021;10(3):335-347. doi: 10.3233/JHD-210476.

BACKGROUND: Huntington's disease is a neurodegenerative disorder caused by a CAG expansion in the huntingtin gene, resulting in a polyglutamine expansion in the ubiquitously expressed mutant huntingtin protein.OBJECTIVE: Here we set out to identify proteins interacting with the full-length...

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Sap KA, Guler AT, Bury A, et al. Identification of Full-Length Wild-Type and Mutant Huntingtin Interacting Proteins by Crosslinking Immunoprecipitation in Mice Brain Cortex. J Huntingtons Dis. 2021;10(3):335-347doi: 10.3233/JHD-210476.
Sap, K. A., Guler, A. T., Bury, A., Dekkers, D., Demmers, J. A. A., & Reits, E. A. (2021). Identification of Full-Length Wild-Type and Mutant Huntingtin Interacting Proteins by Crosslinking Immunoprecipitation in Mice Brain Cortex. Journal of Huntington's disease, 10(3), 335-347. https://doi.org/10.3233/JHD-210476
Sap, Karen A, et al. "Identification of Full-Length Wild-Type and Mutant Huntingtin Interacting Proteins by Crosslinking Immunoprecipitation in Mice Brain Cortex." Journal of Huntington's disease vol. 10,3 (2021): 335-347. doi: https://doi.org/10.3233/JHD-210476
Sap KA, Guler AT, Bury A, Dekkers D, Demmers JAA, Reits EA. Identification of Full-Length Wild-Type and Mutant Huntingtin Interacting Proteins by Crosslinking Immunoprecipitation in Mice Brain Cortex. J Huntingtons Dis. 2021;10(3):335-347. doi: 10.3233/JHD-210476. PMID: 34151850; PMCID: PMC8609692.
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Gas-Phase Ion/Ion Chemistry for Structurally Sensitive Probes of Gaseous Protein Ion Structure: Electrostatic and Electrostatic to Covalent Cross-Linking.

International journal of mass spectrometry

Kit MCS, Carvalho VV, Vilseck JZ, Webb IK.
PMID: 33716558
Int J Mass Spectrom. 2021 May;463. doi: 10.1016/j.ijms.2021.116549. Epub 2021 Feb 17.

Intramolecular interactions within a protein are key in maintaining protein tertiary structure and understanding how proteins function. Ion mobility-mass spectrometry (IM-MS) has become a widely used approach in structural biology since it provides rapid measurements of collision cross sections...

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Kit MCS, Carvalho VV, Vilseck JZ, et al. Gas-Phase Ion/Ion Chemistry for Structurally Sensitive Probes of Gaseous Protein Ion Structure: Electrostatic and Electrostatic to Covalent Cross-Linking. Int J Mass Spectrom. 2021;463doi: 10.1016/j.ijms.2021.116549.
Kit, M. C. S., Carvalho, V. V., Vilseck, J. Z., & Webb, I. K. (2021). Gas-Phase Ion/Ion Chemistry for Structurally Sensitive Probes of Gaseous Protein Ion Structure: Electrostatic and Electrostatic to Covalent Cross-Linking. International journal of mass spectrometry, 463. https://doi.org/10.1016/j.ijms.2021.116549
Kit, Melanie Cheung See, et al. "Gas-Phase Ion/Ion Chemistry for Structurally Sensitive Probes of Gaseous Protein Ion Structure: Electrostatic and Electrostatic to Covalent Cross-Linking." International journal of mass spectrometry vol. 463 (2021). doi: https://doi.org/10.1016/j.ijms.2021.116549
Kit MCS, Carvalho VV, Vilseck JZ, Webb IK. Gas-Phase Ion/Ion Chemistry for Structurally Sensitive Probes of Gaseous Protein Ion Structure: Electrostatic and Electrostatic to Covalent Cross-Linking. Int J Mass Spectrom. 2021 May;463. doi: 10.1016/j.ijms.2021.116549. Epub 2021 Feb 17. PMID: 33716558; PMCID: PMC7946065.
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Cross-Linking Mass Spectrometry for Investigating Protein Conformations and Protein-Protein Interactions─A Method for All Seasons.

Chemical reviews

Piersimoni L, Kastritis PL, Arlt C, Sinz A.
PMID: 34797068
Chem Rev. 2021 Nov 19; doi: 10.1021/acs.chemrev.1c00786. Epub 2021 Nov 19.

Mass spectrometry (MS) has become one of the key technologies of structural biology. In this review, the contributions of chemical cross-linking combined with mass spectrometry (XL-MS) for studying three-dimensional structures of proteins and for investigating protein-protein interactions are outlined....

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Piersimoni L, Kastritis PL, Arlt C, et al. Cross-Linking Mass Spectrometry for Investigating Protein Conformations and Protein-Protein Interactions─A Method for All Seasons. Chem Rev. 2021;doi: 10.1021/acs.chemrev.1c00786.
Piersimoni, L., Kastritis, P. L., Arlt, C., & Sinz, A. (2021). Cross-Linking Mass Spectrometry for Investigating Protein Conformations and Protein-Protein Interactions─A Method for All Seasons. Chemical reviews, . https://doi.org/10.1021/acs.chemrev.1c00786
Piersimoni, Lolita, et al. "Cross-Linking Mass Spectrometry for Investigating Protein Conformations and Protein-Protein Interactions─A Method for All Seasons." Chemical reviews vol. (2021). doi: https://doi.org/10.1021/acs.chemrev.1c00786
Piersimoni L, Kastritis PL, Arlt C, Sinz A. Cross-Linking Mass Spectrometry for Investigating Protein Conformations and Protein-Protein Interactions─A Method for All Seasons. Chem Rev. 2021 Nov 19; doi: 10.1021/acs.chemrev.1c00786. Epub 2021 Nov 19. PMID: 34797068.
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Showing 13 to 24 of 25 entries