Bibliografías temáticas / Heterobifunctional / Artículos de revistas

Artículos de revistas sobre el tema "Heterobifunctional"

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Autor: Grafiati
Publicado: 4 de junio de 2021
Última modificación: 20 de febrero de 2023

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1

Kim, Yong Joo, Yukio Nagasaki, Kazunori Kataoka, Masao Kato, Masayuki Yokoyama, Teruo Okano y Yasuhisa Sakurai. "Heterobifunctional poly(ethylene oxide)". Polymer Bulletin 33, n.º 1 (junio de 1994): 1–6. http://dx.doi.org/10.1007/bf00313466.

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2

Ji, Tae H. y Inhae Ji. "Heterobifunctional photoaffinity labeling reagents". Pharmacology & Therapeutics 43, n.º 3 (enero de 1989): 321–32. http://dx.doi.org/10.1016/0163-7258(89)90013-2.

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3

Shriver-Lake, Lisa C., Brian Donner, Rebecca Edelstein, Kristen Breslin, Suresh K. Bhatia y Frances S. Ligler. "Antibody immobilization using heterobifunctional crosslinkers". Biosensors and Bioelectronics 12, n.º 11 (diciembre de 1997): 1101–6. http://dx.doi.org/10.1016/s0956-5663(97)00070-5.

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4

Pairault, Noël, Hui Zhu, Dennis Jansen, Alexander Huber, Constantin G. Daniliuc, Stefan Grimme y Jochen Niemeyer. "Heterobifunctional Rotaxanes for Asymmetric Catalysis". Angewandte Chemie 132, n.º 13 (16 de enero de 2020): 5140–45. http://dx.doi.org/10.1002/ange.201913781.

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5

Pairault, Noël, Hui Zhu, Dennis Jansen, Alexander Huber, Constantin G. Daniliuc, Stefan Grimme y Jochen Niemeyer. "Heterobifunctional Rotaxanes for Asymmetric Catalysis". Angewandte Chemie International Edition 59, n.º 13 (23 de marzo de 2020): 5102–7. http://dx.doi.org/10.1002/anie.201913781.

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6

Galdeano, Carles. "Expanding the Toolbox of E3 Ligases for Protein Degradation: Targeting the “Undruggable” Fbw7 E3 Ligase". Proceedings 22, n.º 1 (12 de noviembre de 2019): 101. http://dx.doi.org/10.3390/proceedings2019022101.

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7

Steinebach, Christian, Hannes Kehm, Stefanie Lindner, Lan Phuong Vu, Simon Köpff, Álvaro López Mármol, Corinna Weiler et al. "PROTAC-mediated crosstalk between E3 ligases". Chemical Communications 55, n.º 12 (2019): 1821–24. http://dx.doi.org/10.1039/c8cc09541h.

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8

Bloemen, M., L. Vanpraet, M. Ceulemans, T. N. Parac-Vogt, K. Clays, N. Geukens, A. Gils y T. Verbiest. "Selective protein purification by PEG–IDA-functionalized iron oxide nanoparticles". RSC Advances 5, n.º 82 (2015): 66549–53. http://dx.doi.org/10.1039/c5ra11614g.

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9

Salerno, Gianluca, Simona Scarano, Marianna Mamusa, Marco Consumi, Stefano Giuntini, Antonella Macagnano, Stefano Nativi et al. "A small heterobifunctional ligand provides stable and water dispersible core–shell CdSe/ZnS quantum dots (QDs)". Nanoscale 10, n.º 42 (2018): 19720–32. http://dx.doi.org/10.1039/c8nr05566a.

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10

Dupuis, Gilles. "An asymmetrical disulfide-containing photoreactive heterobifunctional reagent designed to introduce radioactive labeling into biological receptors". Canadian Journal of Chemistry 65, n.º 10 (1 de octubre de 1987): 2450–53. http://dx.doi.org/10.1139/v87-409.

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The synthesis of succinimido 1-amino-(4-azidosalicyloyl)-3,4-dithio-5-carboxylate, a heterobifunctional photoaffinity labeling reagent, is described. The cross-linker possesses an asymmetrical disulfide bond, and a general method for generating a spacer arm bearing an asymmetrical or symmetrical disulfide bond is detailed. The heterobifunctional reagent has been obtained in a minimum of steps and intermediates have been characterized. It is further shown that the reagent can be trace-labeled with [125I]-iodine and it has been used to modify phytohemagglutinin, a model protein. Upon irradiation, polymeric phytohemagglutinin derivatives are produced, as evidenced by electrophoretic analysis.
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11

Sibley, Christopher D. y John S. Schneekloth. "Heterobifunctional molecules tackle targeted protein dephosphorylation". Trends in Pharmacological Sciences 43, n.º 4 (abril de 2022): 263–65. http://dx.doi.org/10.1016/j.tips.2022.01.005.

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12

Ji, Inhae, Jaekyoon Shin y Tae H. Ji. "Radioiodination of a photoactivatable heterobifunctional reagent". Analytical Biochemistry 151, n.º 2 (diciembre de 1985): 348–49. http://dx.doi.org/10.1016/0003-2697(85)90186-1.

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13

Dai, Jingwen, Zili Li, Taisheng Wang y Ruke Bai. "A highly stable and versatile heterobifunctional fluoroalkylation reagent for preparation of fluorinated organic compounds". Organic & Biomolecular Chemistry 14, n.º 19 (2016): 4382–86. http://dx.doi.org/10.1039/c6ob00637j.

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14

António, João P. M., Hélio Faustino y Pedro M. P. Gois. "A 2-formylphenylboronic acid (2FPBA)-maleimide crosslinker: a versatile platform for Cys-peptide–hydrazine conjugation and interplay". Organic & Biomolecular Chemistry 19, n.º 28 (2021): 6221–26. http://dx.doi.org/10.1039/d1ob00917f.

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15

Ho, Hien The, Alexandre Bénard, Gwenaël Forcher, Maël Le Bohec, Véronique Montembault, Sagrario Pascual y Laurent Fontaine. "Azlactone-based heterobifunctional linkers with orthogonal clickable groups: efficient tools for bioconjugation with complete atom economy". Organic & Biomolecular Chemistry 16, n.º 39 (2018): 7124–28. http://dx.doi.org/10.1039/c8ob01807c.

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16

Yang, Yifei, Zhenwei Wu, Pan Chen, Peiyuan Zheng, Huibin Zhang y Jinpei Zhou. "Proteolysis-targeting chimeras mediate the degradation of bromodomain and extra-terminal domain proteins". Future Medicinal Chemistry 12, n.º 18 (septiembre de 2020): 1669–83. http://dx.doi.org/10.4155/fmc-2017-0264.

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Bromodomain and extra-terminal domain (BET) protein family plays an important role in regulating gene transcription preferentially at super-enhancer regions and has been involved with several types of cancers as a candidate. Up to now, there are 16 pan-BET inhibitors in clinical trials, however, most of them have undesirable off-target and side-effects. The proteolysis-targeting chimeras technology through a heterobifunctional molecule to link the target protein and E3 ubiquitin ligase, causes the target’s ubiquitination and subsequent degradation. By using this technology, the heterobifunctional small-molecule BET degraders can induce BET protein degradation. In this review, we discuss the advances in the drug discovery and development of BET-targeting proteolysis-targeting chimeras.
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17

Maurizi, Lionel, Vanessa Bellat, Mathieu Moreau, Emmanuel De Maistre, Julien Boudon, Laure Dumont, Franck Denat, David Vandroux y Nadine Millot. "Titanate nanoribbon-based nanobiohybrid for potential applications in regenerative medicine". RSC Advances 12, n.º 41 (2022): 26875–81. http://dx.doi.org/10.1039/d2ra04753e.

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Titanate nanoribbons functionalized by heterobifunctional polymer and type I collagen for cellular adhesion and proliferation. This new nanobiohybrid affected neither cytotoxicity nor platelet aggregation ability.
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18

Pahattuge, Thilanga N., J. Matt Jackson, Rane Digamber, Harshani Wijerathne, Virginia Brown, Malgorzata A. Witek, Chamani Perera, Richard S. Givens, Blake R. Peterson y Steven A. Soper. "Visible photorelease of liquid biopsy markers following microfluidic affinity-enrichment". Chemical Communications 56, n.º 29 (2020): 4098–101. http://dx.doi.org/10.1039/c9cc09598e.

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19

Goodwin, Andrew P., Stephanie S. Lam y Jean M. J. Fréchet. "Rapid, Efficient Synthesis of Heterobifunctional Biodegradable Dendrimers". Journal of the American Chemical Society 129, n.º 22 (junio de 2007): 6994–95. http://dx.doi.org/10.1021/ja071530z.

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20

Lala, Anil K., H. F. Batliwala y R. M. Mogre. "A new radioactive diazofluorene based heterobifunctional reagent". Journal of Biosciences 14, n.º 2 (junio de 1989): 127–32. http://dx.doi.org/10.1007/bf02703164.

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21

Agarwal, Deepali, Kushal Sen y M. L. Gulrajani. "Application of heterobifunctional reactive dyes on silk". Journal of the Society of Dyers and Colourists 112, n.º 1 (22 de octubre de 2008): 10–16. http://dx.doi.org/10.1111/j.1478-4408.1996.tb01748.x.

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22

Tomczyk, T., J. M. Arencibia, M. Milewicz, D. Trębicka, J. Skalska, K. Poniatowska, J. Adamczyk et al. "Development of selective MCL-1 heterobifunctional degraders". European Journal of Cancer 174 (octubre de 2022): S104. http://dx.doi.org/10.1016/s0959-8049(22)01076-0.

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23

Li, Jane, Curtis F. Crasto, James S. Weinberg, Mansoor Amiji, Dinesh Shenoy, Srinivas Sridhar, Glenn J. Bubley y Graham B. Jones. "An approach to heterobifunctional poly(ethyleneglycol) bioconjugates". Bioorganic & Medicinal Chemistry Letters 15, n.º 24 (diciembre de 2005): 5558–61. http://dx.doi.org/10.1016/j.bmcl.2005.08.108.

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24

Antonovič, Leposava, Petr Hodek, Stanislav Smrček, Petr Novák, Mirek Šulc y Henry W. Strobel. "Heterobifunctional Photoaffinity Probes for Cytochrome P450 2B". Archives of Biochemistry and Biophysics 370, n.º 2 (octubre de 1999): 208–15. http://dx.doi.org/10.1006/abbi.1999.1408.

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25

Brownsey, Duncan K., Ben C. Rowley, Evgueni Gorobets, Benjamin S. Gelfand y Darren J. Derksen. "Rapid synthesis of pomalidomide-conjugates for the development of protein degrader libraries". Chemical Science 12, n.º 12 (2021): 4519–25. http://dx.doi.org/10.1039/d0sc05442a.

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Current methods for the preparation of heterobifunctional pomalidomide-conjugates rely on methods that are often low yielding and produce intractable byproducts. Herein we describe our strategy for the succinct preparation of pomalidomide-linkers.
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26

Ma, He-Ming, Yun Liu, Ying-Xuan Liu, Jin-Jun Qiu y Cheng-Mei Liu. "Vinyl benzoxazine: a novel heterobifunctional monomer that can undergo both free radical polymerization and cationic ring-opening polymerization". RSC Advances 5, n.º 124 (2015): 102441–47. http://dx.doi.org/10.1039/c5ra18058a.

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A novel heterobifunctional monomer (6-ethenyl-3-phenyl-3,4-dihydro-2H-1,3-benzoxazine (VBOZO)) containing both a vinyl group and benzoxazine group was successfully prepared and the homo- and copolymerization reactions of this monomer were studied.
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27

Schembri, Mark A. y Per Klemm. "Heterobinary Adhesins Based on theEscherichia coli FimH Fimbrial Protein". Applied and Environmental Microbiology 64, n.º 5 (1 de mayo de 1998): 1628–33. http://dx.doi.org/10.1128/aem.64.5.1628-1633.1998.

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ABSTRACT The FimH adhesin of Escherichia coli type 1 fimbriae confers the ability to bind to d-mannosides by virtue of a receptor-binding domain located in its N-terminal region. This protein was engineered into a heterobifunctional adhesin by introducing a secondary binding site in the C-terminal region. The insertion of histidine clusters into this site resulted in coordination of various metal ions by recombinant cells expressing chimeric FimH proteins. In addition, libraries consisting of random peptide sequences inserted into the FimH display system and screened by a “panning” technique were used to identify specific sequences conferring the ability to adhere to Ni2+ and Cu2+. Recombinant cells expressing heterobifunctional FimH adhesins could adhere simultaneously to both metals and saccharides. Finally, combining the metal-binding modifications with alterations in the natural receptor-binding region demonstrated the ability to independently modulate the binding of FimH to two ligands simultaneously.
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28

Heitel, Pascal. "Emerging TACnology: Heterobifunctional Small Molecule Inducers of Targeted Posttranslational Protein Modifications". Molecules 28, n.º 2 (10 de enero de 2023): 690. http://dx.doi.org/10.3390/molecules28020690.

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Posttranslational modifications (PTMs) play an important role in cell signaling and they are often deregulated in disease. This review addresses recent advances in the development of heterobifunctional small molecules that enable targeting or hijacking PTMs. This emerging field is spearheaded by proteolysis-targeting chimeras (PROTACs), that induce ubiquitination of their targets and, thus, tag them for degradation by the proteasome. Within the last decade, several improvements have been made to enhance spatiotemporal control of PROTAC-induced degradation as well as cell permeability. Inspired by the success story of PROTACs, additional concepts based on chimeric small molecules have emerged such as phosphatase-recruiting chimeras (PhoRCs). Herein, an overview of strategies causing (de-)phosphorylation, deubiquitination as well as acetylation is provided, and the opportunities and challenges of heterobifunctional molecules for drug discovery are highlighted. Although significant progress has been achieved, a plethora of PTMs have not yet been covered and PTM-inducing chimeras will be helpful tools for chemical biology and could even find application in pharmacotherapy.
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29

Lu, Changhai y Wen Zhong. "Synthesis of Propargyl-Terminated Heterobifunctional Poly(ethylene glycol)". Polymers 2, n.º 4 (13 de octubre de 2010): 407–17. http://dx.doi.org/10.3390/polym2040407.

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30

Sabnis, Ram W. "Heterobifunctional Compounds as BRAF Degraders for Treating Cancer". ACS Medicinal Chemistry Letters 13, n.º 3 (7 de febrero de 2022): 332–33. http://dx.doi.org/10.1021/acsmedchemlett.2c00039.

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31

Wang, Wesley W., Li-Yun Chen, Jacob M. Wozniak, Appaso M. Jadhav, Hayden Anderson, Taylor E. Malone y Christopher G. Parker. "Targeted Protein Acetylation in Cells Using Heterobifunctional Molecules". Journal of the American Chemical Society 143, n.º 40 (30 de septiembre de 2021): 16700–16708. http://dx.doi.org/10.1021/jacs.1c07850.

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32

Cavell, Ronald G., Robert W. Reed, Kattesh V. Katti, Maravanji S. Balakrishna, Paul W. Collins, Vivian Mozol y Ingrid Bartz. "Heterobifunctional Phosphorus-Nitrogen Compounds: Iminophosphoranophosphines and Their Complexes". Phosphorus, Sulfur, and Silicon and the Related Elements 76, n.º 1-4 (marzo de 1993): 9–12. http://dx.doi.org/10.1080/10426509308032345.

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33

Vadala, M. L., M. S. Thompson, M. A. Ashworth, Y. Lin, T. P. Vadala, R. Ragheb y J. S. Riffle. "Heterobifunctional Poly(ethylene oxide) Oligomers Containing Carboxylic Acids". Biomacromolecules 9, n.º 3 (marzo de 2008): 1035–43. http://dx.doi.org/10.1021/bm701067d.

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34

Crocker, Peter J., Nobuyuki Imai, Krishnan Rajagopalan, Michael A. Boggess, Stefan Kwiatkowski, Lori D. Dwyer, Thomas C. Vanaman y David S. Watt. "Heterobifunctional cross-linking agents incorporating perfluorinated aryl azides". Bioconjugate Chemistry 1, n.º 6 (noviembre de 1990): 419–24. http://dx.doi.org/10.1021/bc00006a008.

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35

Reddy, Rajarathnam E., Yon-Yih Chen, Donald D. Johnson, Gangamani S. Beligere, Sushil D. Rege, You Pan y John K. Thottathil. "An Efficient Synthesis of a Heterobifunctional Coupling Agent". Bioconjugate Chemistry 16, n.º 5 (septiembre de 2005): 1323–28. http://dx.doi.org/10.1021/bc040259x.

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36

Bieniarz, Christopher, Mazhar Husain, Grady Barnes, Carol A. King y Christopher J. Welch. "Extended Length Heterobifunctional Coupling Agents for Protein Conjugations". Bioconjugate Chemistry 7, n.º 1 (enero de 1996): 88–95. http://dx.doi.org/10.1021/bc950080+.

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37

Burkinshaw, S. M. y M. Paraskevas. "The dyeing of silk: Part 4 heterobifunctional dyes". Dyes and Pigments 88, n.º 3 (marzo de 2011): 396–402. http://dx.doi.org/10.1016/j.dyepig.2010.08.018.

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38

Fischer, Lutz y Juri Rappsilber. "False discovery rate estimation and heterobifunctional cross-linkers". PLOS ONE 13, n.º 5 (10 de mayo de 2018): e0196672. http://dx.doi.org/10.1371/journal.pone.0196672.

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39

Sharma, Chiranjeev, Myeong A. Choi, Yoojin Song y Young Ho Seo. "Rational Design and Synthesis of HSF1-PROTACs for Anticancer Drug Development". Molecules 27, n.º 5 (2 de marzo de 2022): 1655. http://dx.doi.org/10.3390/molecules27051655.

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PROTACs employ the proteosome-mediated proteolysis via E3 ligase and recruit the natural protein degradation machinery to selectively degrade the cancerous proteins. Herein, we have designed and synthesized heterobifunctional small molecules that consist of different linkers tethering KRIBB11, a HSF1 inhibitor, with pomalidomide, a commonly used E3 ligase ligand for anticancer drug development.
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40

Wigle, Tim J., Yue Ren, Jennifer R. Molina, Danielle J. Blackwell, Laurie B. Schenkel, Kerren K. Swinger, Kristy Kuplast‐Barr et al. "Targeted Degradation of PARP14 Using a Heterobifunctional Small Molecule". ChemBioChem 22, n.º 12 (4 de mayo de 2021): 2107–10. http://dx.doi.org/10.1002/cbic.202100047.

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41

Guillaumet, G屍ald, Thierry Besson, Benoit Joseph, Pascale Moreau, Marie-Claude Viaud y G屍ard Coudert. "Synthesis and Fluorescent Properties of New Heterobifunctional Fluorescent Probes". HETEROCYCLES 34, n.º 2 (1992): 273. http://dx.doi.org/10.3987/com-91-5899.

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42

Singh, Yashveer, Nicolas Spinelli, Eric Defrancq y Pascal Dumy. "A novel heterobifunctional linker for facile access to bioconjugates". Organic & Biomolecular Chemistry 4, n.º 7 (2006): 1413. http://dx.doi.org/10.1039/b518151h.

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43

OHNISHI, MIKIO, HIROYUKI SUGIMOTO, HIDENORI YAMADA, TAIJI IMOTO, KIYOSHI ZAITSU y YOSUKE OHKURA. "Heterobifunctional reagents for cross-linking of sugar with protein." CHEMICAL & PHARMACEUTICAL BULLETIN 33, n.º 2 (1985): 674–78. http://dx.doi.org/10.1248/cpb.33.674.

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44

Imai, Nobuyuki, Tadashi Kometani, Peter J. Crocker, Jean B. Bowdan, Ayhan Demir, Lori D. Dwyer, Dennis M. Mann, Thomas C. Vanaman y David S. Watt. "Photoaffinity heterobifunctional crosslinking reagents based on N-(azidobenzoyl)tyrosines". Bioconjugate Chemistry 1, n.º 2 (marzo de 1990): 138–43. http://dx.doi.org/10.1021/bc00002a008.

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45

Imai, Nobuyuki, Lori D. Dwyer, Tadashi Kometani, Tae Ji, Thomas C. Vanaman y David S. Watt. "Photoaffinity heterobifunctional crosslinking reagents based on azide-substituted salicylates". Bioconjugate Chemistry 1, n.º 2 (marzo de 1990): 144–48. http://dx.doi.org/10.1021/bc00002a009.

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46

Heindel, Ned D., Huiru Zhao, Roger A. Egolf, Chien Hsing Chang, Keith J. Schray, Jacqueline G. Emrich, Joanne P. McLaughlin y David V. Woo. "A novel heterobifunctional linker for formyl to thiol coupling". Bioconjugate Chemistry 2, n.º 6 (noviembre de 1991): 427–30. http://dx.doi.org/10.1021/bc00012a008.

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47

Johnson, Gary M., James P. Albarella y Christoph Petry. "Heterobifunctional Cross-Linkers Containing 4,9-Dioxa-1,12-dodecanediamine Spacers". Bioconjugate Chemistry 8, n.º 3 (mayo de 1997): 447–52. http://dx.doi.org/10.1021/bc970026o.

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48

Hypolite, Claire L., Terri L. McLernon, Derek N. Adams, Kenneth E. Chapman, Curtis B. Herbert, C. C. Huang, Mark D. Distefano y Wei-Shou Hu. "Formation of Microscale Gradients of Protein Using Heterobifunctional Photolinkers". Bioconjugate Chemistry 8, n.º 5 (septiembre de 1997): 658–63. http://dx.doi.org/10.1021/bc9701252.

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49

Johnson, Gary M., James P. Albarella y Christoph Petry. "Heterobifunctional Cross-Linkers Containing 4,9-Dioxa-1,12-dodecanediamine Spacers". Bioconjugate Chemistry 9, n.º 2 (marzo de 1998): 304. http://dx.doi.org/10.1021/bc9800062.

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50

Bettinger, Thierry, Jean-Serge Remy, Patrick Erbacher y Jean-Paul Behr. "Convenient Polymer-Supported Synthetic Route to Heterobifunctional Polyethylene Glycols". Bioconjugate Chemistry 9, n.º 6 (noviembre de 1998): 842–46. http://dx.doi.org/10.1021/bc980039h.

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