RosettaCommons/UTexasAptamer huggingface dataset:
Aptamer: anti-mDEC205 aptamer, min.2
Target: Murine receptor DEC205 (mDEC205)
Type of nucleic acid: 2'-fluoro-RNA
Sequence: 5'GGGAGGUGUGUUAGCACACGAUUCAUAAUCAGCUACCCUCCC3'
Sequence length: 42
GC content: 0.5238095238095238
Affinity: Kd app = 23 ± 6 nmol/l.
Pool type: 5′-GGGAGGTGAATGGTTCTACGAT-N50-TTACATGCGAGATGACCACGTAATTGAATTAAATGCCCGCCATGACCAG-3′
Pool random region: 50
Binding buffer/conditions: Not Reported 
Buffer type: Not Reported
Molecular weight of target: Not reported
Post-SELEX modifications: Truncation: "using these clones as a starting point, we tested a series of successive truncations aimed at preserving this sequence but minimizing the overall size of the aptamer. This resulted in the identification of a minimized sequence composed of a 42-nucleotide aptamer core, “min.2” which performed better than the bulk Round 5 pool"
Application as quoted in the referenced paper: Therapeutic: "Compared with a nonspecific ribonucleic acid (RNA) of similar length, DEC205 aptamer-OVA-mediated antigen delivery stimulated strong proliferation and production of interferon (IFN)-γ and interleukin (IL)-2. The immune responses elicited by aptamer-OVA conjugates were sufficient to inhibit the growth of established OVA-expressing B16 tumor cells. Our results demonstrate a new application of aptamer technology for the development of effective T cell-mediated vaccines."
Additional information: The 2′F modification can be readily incorporated during transcription by substituting 2′F CTP and 2′F UTP instead of the natural CTP and UTP and using the mutant T7 RNA polymerase protein Y639F
DNA library/pool was used as a template to generate the RNA pool used in the selection. A T7 promoter sequence might be necessary to use this DNA library/pool as a template to generate the RNA pool in the selection..
"additional 3′ constant region used for hybridization of a fluorescent probe for flow cytometry"
"The sequences of the minimized aptamer, min.2, and a nonbinding control aptamer, c36, an aptamer-like, nonfunctional sequence which we have previously utilized as a nonbinding control6 were: 5S GGGAGGUGUGUUAGCACACGAUUCAUAAUCAGCUACCCUCCCt and 5SGGCGUAGUGAUUAUGAAUCGUGUGCUAAUACACGCCt, respectively, where “t” is a 3′ inverted dT and “5S” is the 5′ thiol. All aptamers were synthesized with the final 4,4′-dimethoxytrityl protecting group left on. "
Reference (2014,Mol Ther
): Wengerter, B. C., Katakowski, J. A., Rosenberg, J. M., Park, C. G., Almo, S. C., Palliser, D., & Levy, M. (2014). Aptamer-targeted antigen delivery. Molecular therapy : the journal of the American Society of Gene Therapy, 22(7), 1375–1387. https://doi.org/10.1038/mt.2014.51
Aptamer: cntrl.36 (C36)
Target: N/A (negative control, binds to nothing)
Type of nucleic acid: 2'-fluoro-RNA
Sequence: 5'GGCGUAGUGAUUAUGAAUCGUGUGCUAAUACACGCC3'
Sequence length: 36
GC content: 0.4722222222222222
Affinity: Not Applicable
Pool type: 5′-GGGAGGTGAATGGTTCTACGAT-N50-TTACATGCGAGATGACCACGTAATTGAATTAAATGCCCGCCATGACCAG-3′
Pool random region: 50
Binding buffer/conditions: Not Reported 
Buffer type: Not Reported
Molecular weight of target: Not reported
Post-SELEX modifications: Truncation: "using these clones as a starting point, we tested a series of successive truncations aimed at preserving this sequence but minimizing the overall size of the aptamer. This resulted in the identification of a minimized sequence composed of a 42-nucleotide aptamer core, “min.2” which performed better than the bulk Round 5 pool"
Application as quoted in the referenced paper: Therapeutic: "Compared with a nonspecific ribonucleic acid (RNA) of similar length, DEC205 aptamer-OVA-mediated antigen delivery stimulated strong proliferation and production of interferon (IFN)-γ and interleukin (IL)-2. The immune responses elicited by aptamer-OVA conjugates were sufficient to inhibit the growth of established OVA-expressing B16 tumor cells. Our results demonstrate a new application of aptamer technology for the development of effective T cell-mediated vaccines."
Additional information: The 2′F modification can be readily incorporated during transcription by substituting 2′F CTP and 2′F UTP instead of the natural CTP and UTP and using the mutant T7 RNA polymerase protein Y639F
DNA library/pool was used as a template to generate the RNA pool used in the selection. A T7 promoter sequence might be necessary to use this DNA library/pool as a template to generate the RNA pool in the selection..
"additional 3′ constant region used for hybridization of a fluorescent probe for flow cytometry"
"The sequences of the minimized aptamer, min.2, and a nonbinding control aptamer, c36, an aptamer-like, nonfunctional sequence which we have previously utilized as a nonbinding control6 were: 5S GGGAGGUGUGUUAGCACACGAUUCAUAAUCAGCUACCCUCCCt and 5SGGCGUAGUGAUUAUGAAUCGUGUGCUAAUACACGCCt, respectively, where “t” is a 3′ inverted dT and “5S” is the 5′ thiol. All aptamers were synthesized with the final 4,4′-dimethoxytrityl protecting group left on. "
Reference (2014,Mol Ther
): Wengerter, B. C., Katakowski, J. A., Rosenberg, J. M., Park, C. G., Almo, S. C., Palliser, D., & Levy, M. (2014). Aptamer-targeted antigen delivery. Molecular therapy : the journal of the American Society of Gene Therapy, 22(7), 1375–1387. https://doi.org/10.1038/mt.2014.51
Aptamer: XEO2mini
Target: Prostate cancer (PCa) cells
Type of nucleic acid: 2'-O-Me-RNA
Sequence: 5'CACGACGCUGAUGGAUCGUUACGACUAGCAUCGC3'
Sequence length: 34
GC content: 0.5588235294117647
Affinity: Not reported
Pool type: 5'-CATCGATGCTAGTCGTAACGATCC-30N-CGAGAACGTTTCTCTCCTCTCCCTATAGTGAGTCGTATTA-3'
Pool random region: 30
Binding buffer/conditions: Delection buffer (EBSS with 1 mM MgCl2)
Binding buffer for binding Assay (binding buffer [4.5 g/l glucose, 1 mM MgCl2, 0.1 mg/ml yeast tRNA, and 1 mg/ml BSA in EBSS] 
Divalent salt: MgCl
Buffer type: Other Buffers
Molecular weight of target: Not reported
Post-SELEX modifications: Truncation: "For the truncated form of XEO2, hereinafter referred to as XEO2mini, a total of 43 nucleotides were removed from its parent XEO2 Apt."
Application as quoted in the referenced paper: Drug Delivery:"Rather than isolating high-affinity Apts as reported in previous selection processes, our selection strategy was designed to enrich cancer-cell specific internalizing Apts. A similar cell-uptake selection strategy may be used to develop specific internalizing ligands for a myriad of other diseases and can potentially facilitate delivering various molecules, including drugs and siRNAs, into cells."
Additional information: The starting RNA Apt candidate library was composed of 77 base long degradation-resistant RNA oligonucleotides incorporating 2'-OMe modified ATP, CTP, and UTP.24 The partly 2'-OMe-modified oligonucleotides were initially incubated with counter-selection cell line
DNA library/pool was used as a template to generate the RNA pool used in the selection. A T7 promoter sequence might be necessary to use this DNA library/pool as a template to generate the RNA pool in the selection..
Reference (2012,ACS Nano): Xiao, Z., Levy-Nissenbaum, E., Alexis, F., Lupták, A., Teply, B. A., Chan, J. M., Shi, J., Digga, E., Cheng, J., Langer, R., & Farokhzad, O. C. (2012). Engineering of targeted nanoparticles for cancer therapy using internalizing aptamers isolated by cell-uptake selection. ACS nano, 6(1), 696–704. https://doi.org/10.1021/nn204165v
Aptamer: AS1411 (also known as AGRO100)
Target: Nucleolin
Type of nucleic acid: ssDNA
Sequence: 5'GGTGGTGGTGGTTGTGGTGGTGGTGG3'
Sequence length: 26
GC content: 0.6538461538461539
Affinity: Not reported
Pool type: Not reported
Binding buffer/conditions: HEPES binding buffer (25 mmHEPES, pH 7.9, 4 mm KCl, 3 mmMgCl2)
Divalent salt: MgCl
Buffer type: Other Buffers
pH: 7.9
Molecular weight of target: 106-kDa
Post-SELEX modifications: Truncation: "removed the 5' 3T cap and 3'aminoalkyl because they were found to be unnecessary for serum stability and protection from nuclease activity resulting in the AS1411/AGRO100 sequence"
Application as quoted in the referenced paper: Therapeutic: " We present strong evidence that this protein is nucleolin, a multifunctional phos- phoprotein whose levels are related to the rate of cell proliferation. Our results indicate that binding of G-rich oligonucleotides to nucleolin may be responsible for their non-sequence-specific effects. Furthermore, these oligonucleotides represent a new class of potentially therapeutic agents with a novel mechanism of action"
Additional information: 3′-Modified oligonucleotides were purchased from Oligos Etc. (Wilsonville, OR) or synthesized at the University of Alabama at Birmingham using 3′-C3-amine CPG columns from Glen Research (Sterling, VA). Unmodified oligonucleotides were purchased from Life Technologies, Inc. 
Both 29A-OH (a 3′-unmodified analog of GRO29A) and TEL inhibited the growth of cells
One notable early modification made to the GRO29A sequence (Node 1A) removed the 5' 3T cap and 3'aminoalkyl because they were found to be unnecessary for serum stability and protection from nuclease activity resulting in the AS1411/AGRO100 sequence
Reference (1999, J Biol Chem ): Bates, P. J., Kahlon, J. B., Thomas, S. D., Trent, J. O., & Miller, D. M. (1999). Antiproliferative activity of G-rich oligonucleotides correlates with protein binding. The Journal of biological chemistry, 274(37), 26369–26377. https://doi.org/10.1074/jbc.274.37.26369
Aptamer: Sgc8c
Target: Protein Tyrosine Kinase-7 (PTK7)
Type of nucleic acid: ssDNA
Sequence: 5'ATCTAACTGCTGCGCCGCCGGGAAAATACTGTACGGTTAGA3'
Sequence length: 41
GC content: 0.5121951219512195
Affinity: Kd:0.8 nM
Pool type: 5'-ATACCAGCTTATTCAATT-52N-AGATAGTAAGTGCAATCT-3'
Pool random region: 52
Binding buffer/conditions: 4.5 g/liter glucose and 5 mM MgCl2 in Dulbecco's PBS with calcium chloride and magnesium chloride (Sigma) and adding yeast tRNA (0.1 mg/ml; Sigma) and BSA (1 mg/ml; Fisher)
Divalent salt: MgCl 
Buffer type: PBS/phosphate buffers
pH: 7.4
Molecular weight of target: 118 kDa
Post-SELEX modifications: Truncation: "An optimized and truncated DNA sequence of sgc8, sgc8c, which had identical binding properties as sgc815 and which had previously been labeled with a biotin tag at the 5′-end, was incubated with the solubilized membrane proteins. The binding complex of sgc8 and its target was then extracted using streptavidin-coated magnetic beads."
Application as quoted in the referenced paper: Biosensor: "One of the selected aptamers, sgc8, showed high specificity and affinity for surface target on most of the T-ALL cells and acute myeloid leukemia (AML) cells, as well as some B-cell acute lymphoblastic leukemia (B-ALL) cells. However, sgc8 did not show a comparable detectable level of binding to either lymphoma cells or normal human bone marrow cells. The elevated expression of the target of sgc8 on leukemia cells, especially on T-ALL cells and AML cells, seems, therefore, to imply its importance in the development of leukemia and, significantly, to indicate, as well, a cell-specific membrane biomarker. In this paper, this biomarker was subsequently determined and confirmed to be protein tyrosine kinase-7 (PTK7), a receptor protein tyrosine kinase-like molecule."
Additional information: Pool information and binding buffer obtained from 2006 paper (https://doi.org/10.1073/pnas.0602615103)

more information on this aptamer in this paper (https://pubmed.ncbi.nlm.nih.gov/21168488/)
Reference (2008,J Proteome Res
): Shangguan, D., Cao, Z., Meng, L., Mallikaratchy, P., Sefah, K., Wang, H., Li, Y., & Tan, W. (2008). Cell-specific aptamer probes for membrane protein elucidation in cancer cells. Journal of proteome research, 7(5), 2133–2139. https://doi.org/10.1021/pr700894d
Aptamer: 2-2(t)
Target: Epidermal growth factor receptor 2, Human (ErbB-2/HER2)
Type of nucleic acid: ssDNA
Sequence: 5'GCAGCGGTGTGGGGGCAGCGGTGTGGGGGCAGCGGTGTGGGG3'
Sequence length: 42
GC content: 0.7857142857142857
Affinity: Not reported
Pool type: 5′-ATACCAGCTTATTCAATT-N40-AGATAGTAAGTGCAATCT-3′
Pool random region: 40
Binding buffer/conditions: Not Reported 
Buffer type: Not Reported
Molecular weight of target: Not reported
Application as quoted in the referenced paper: Inhibition: "The antitumor effect of the aptamer was nearly twofold stronger than that of a monoclonal anti–ErbB-2/HER2 antibody. Consistent with aptamer-induced intracellular degradation of ErbB-2/HER2, incubation of gastric cancer cells with the trimeric aptamer promoted translocation of ErbB-2/HER2 from the cell surface to cytoplasmic puncta. This translocation was associated with a lysosomal hydrolase-dependent clearance of the ErbB-2/HER2 protein from cell extracts. We conclude that targeting ErbB-2/HER2 with DNA aptamers might retard the tumorigenic growth of gastric cancer by means of accelerating lysosomal degradation of the oncoprotein. This work exemplifies the potential pharmacological utility of aptamers directed at cell surface proteins, and it highlights an endocytosis-mediated mechanism of tumor inhibition."
Additional information: "As shown in Fig. 2A, strong binding of monomeric aptamer 2-2 was detected only at the higher amount (20 μg) but not at the 10-fold lower amount of spotted cell lysate. However, the trimeric version of the aptamer clearly displayed specific binding with extracts derived from N87 cells at both high and low amounts of cell lysates. The relatively low level of ErbB-2 expressed by A431 cells likely underlies the minor signal we observed with these cells. Flow cytometry analyses similarly supported enhanced binding by the trimeric aptamer. Biotin-labeled trimeric aptamers 2-2(t) and PR(t) were incubated with N87 cells, before treatment with phycoerythrin streptavidin and fluorescence-based cell analysis. As indicated by Fig. 2B, the trimeric aptamer 2-2(t) was able to efficiently bind with ErbB-2–overexpressing cells, whereas the controls demonstrated no binding."

The aptamer sequence was contructed by putting together three 2-2 aptamer together. The paper mentined 2-2 aptamer is 14 nucleotide and 2-2(t) is 42 nucleotide. (3 x14 = 42)

However, the paper notes that the pool has a "50-nucleotide random sequence."
Reference (2013,Proc Natl Acad Sci U S A): Mahlknecht, G., Maron, R., Mancini, M., Schechter, B., Sela, M., & Yarden, Y. (2013). Aptamer to ErbB-2/HER2 enhances degradation of the target and inhibits tumorigenic growth. Proceedings of the National Academy of Sciences of the United States of America, 110(20), 8170–8175. https://doi.org/10.1073/pnas.1302594110
Aptamer: S1.3/S2.2
Target: Mucin 1 (MUC1)
Type of nucleic acid: ssDNA
Sequence: 5'GGGAGACAAGAATAAACGCTCAAGCAGTTGATCCTTTGGATACCCTGGTTCGACAGGAGGCTCACAACAGGC3'
Sequence length: 72
GC content: 0.5138888888888888
Affinity: kd: 0.135 nM
Pool type: 5'-GGGAGACAAGAATAAACGCTCAA-25N-TTCGACAGGAGGCTCACAACAGGC-3'
Pool random region: 25
Binding buffer/conditions: 0.2 M NaHCO 3 , 0.5 M NaCl, pH 7.4
Buffer type: Other Buffers
pH: 7.4
Molecular weight of target: Not reported
Application as quoted in the referenced paper: Diagnostic: "Selected aptamers have been evaluated for the binding affi nity and selectivity against MUC1 and MUC1 isoforms and have been compared to those of a previously described anti-MUC1 antibody. A range of techniques, including affi nity chromatography, enzyme_x0002_linked immunosorbent assay (ELISA) and surface plas_x0002_mon resonance (SPR), have been utilised for the study of  the aptamer affi nity to MUC1, and their characteristic ability to pinpoint single amino acid changes in the MUC1 sequence. Furthermore, the potential application of such aptamers in diagnostic assays has been evaluated using fluorescent-labelled aptamers against MUC1-expressing breast tumour cells (MCF-7 breast cancer cell line) stud_x0002_ied by fl uorescent microscopy."
Reference (2006,Tumour Biol
): Ferreira, C. S., Matthews, C. S., & Missailidis, S. (2006). DNA aptamers that bind to MUC1 tumour marker: design and characterization of MUC1-binding single-stranded DNA aptamers. Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine, 27(6), 289–301. https://doi.org/10.1159/000096085
Aptamer: J18
Target: Epithelial Growth Factor Receptor (EGFR)
Type of nucleic acid: ssRNA
Sequence: 5'GGCGCUCCGACCUUAGUCUCUGCAAGAUAAACCGUGCUAUUGACCACCCUCAACACACUUAUUUAAUGUAUUGAACGGACCUACGAACCGUGUAGCACAGCAGA3'
Sequence length: 104
GC content: 0.4807692307692308
Affinity: kd: 7 nM
Pool type: 5'-GGCGCTCCGACCTTAGTCTCTG-62N-GAACCGTGTAGCACAGCAGAGAATTAAATGCCCGCCATGACCAG-3'
Pool random region: 62
Binding buffer/conditions: Flow Sytometry Binding Buffer:DPBS with 5 mM MgCl2(Sigma Aldrich, St. Louis, MO) 
Divalent salt: MgCl 
Buffer type: PBS/phosphate buffers
Molecular weight of target: 118 kDa
Application as quoted in the referenced paper: Not reported
Additional information: DNA library/pool was used as a template to generate the RNA pool used in the selection. A T7 promoter sequence might be necessary to use this DNA library/pool as a template to generate the RNA pool in the selection..
Reference (2009,J Proteome Res): Li, N., Ebright, J. N., Stovall, G. M., Chen, X., Nguyen, H. H., Singh, A., Syrett, A., & Ellington, A. D. (2009). Technical and biological issues relevant to cell typing with aptamers. Journal of proteome research, 8(5), 2438–2448. https://doi.org/10.1021/pr801048z
Aptamer: ARC1091 (SEQ ID NO 17)
Target: Prostate-specific membrane antigen (PSMA) of prostate cancer cells
Type of nucleic acid: 2'-fluoro/O-Me-RNA
Sequence: 5'AGAGGAGAGAACGUUCUACUAUGGGUGGCUGGGAGGGG3'
Sequence length: 38
GC content: 0.5789473684210527
Affinity: Kd: 3.1 nM
Pool type: TBD
Binding buffer/conditions: 0.1% BSA, 0.2 mg/mL salmon sperm DNA, 0.2 mg/mL yeast tRNA in 0.9xPBS
Divalent salt: MgCl 
Buffer type: PBS/phosphate buffers
pH: 7.4
Molecular weight of target: TBD
Post-SELEX modifications: TBD
Application as quoted in the referenced paper: TBD
Additional information: TBD
Reference (2006,Not Applicable): Diener, J. L. et al. (2006). Stabilized Aptamers To PSMA  and Their Use As Prostate Cancer Therapeutics. US Patent # US20090105172A1
Aptamer: E07.min
Target: Epidermal growth factor receptor (EGFR)
Type of nucleic acid: 2'-fluoro-RNA
Sequence: 5′GGACGGAUUUAAUCGCCGUAGAAAGCAUGUCAAAGCCGGAACCGUCC3′
Sequence length: 47
GC content: 0.5319148936170213
Affinity: TBD
Pool type: 5'-GGCGCTCCGACCTTAGTCTCTG-N62-GAACCGTGTAGCACAGCAGA-3′
Pool random region: 62
Binding buffer/conditions: 1X DPBS and 5 mM MgCl3
Divalent salt: MgCl
Buffer type: PBS/phosphate buffers
pH: 7.4
Molecular weight of target: Not reported
Post-SELEX modifications: TBD
Application as quoted in the referenced paper: TBD
Additional information: TBD
Reference (2014,Not Applicable): B. R., Xu, L., Levy, M. (2014, October 13). Targeting multiple receptors on a cell surface for specific cell targeting. US Patent # US9636419B2
Aptamer: IR-A43
Target: Recombinant insulin receptor extracellular domain (His-Tagged)
Type of nucleic acid: 5-uracil-modified-DNA
Sequence: 5’GCCTGUAUCCGCAGUAUCGGCAUUCAGCGAC3’



Sequence length: 31
GC content: 0.5806451612903226
Affinity: Kd: 2.85 nM via filter binding assay
Pool type: 5′-TATGAGTGACCGTCCGCCTG-N40-CAGCCACACCACCAGCCAAA-3
Pool random region: 40
Binding buffer/conditions: 40 mM HEPES (pH 7.5), 102 mM NaCl, 5 mM KCl, 5 mM MgCl2, and 0.05% Tween-20
Divalent salt: MgCl
Buffer type: Other Buffers
pH: 7.5
Molecular weight of target: Not reported
Post-SELEX modifications: This is the truncated form of the full length IR-A43F (100-00-1355) aptamer sequence.
Application as quoted in the referenced paper: Therapeutic: " Allosteric Modulator - Our study implies that aptamers are promising reagents for the development of allosteric modulators that discriminate a specific conformation of a target receptor. Studies of allosteric modulators are not only important to reveal mechanisms of receptor activation, but also to discover new drug candidates. IR-A43 acts as a ‘wedge' to stabilize the insulin-induced active conformation of the receptor to enhance insulin binding to the insulin receptor. Our model is a plausible explanation for the mutual positive cooperativity that occurs when insulin and IR-A43 bind to the insulin receptor. To confirm this model, further studies of the structure of the insulin receptor and IR-A43 complex are required."
Additional information: Modified nucleobase 5-[N-(1-naphthylmethyl)carboxamide]-2′-deoxyuridine (Nap-dU) was used in this sequence
Reference (2021, Nucleic Acids Res ): Yunn, N. O., Park, M., Park, S., Lee, J., Noh, J., Shin, E., & Ryu, S. H. (2021). A hotspot for enhancing insulin receptor activation revealed by a conformation-specific allosteric aptamer. Nucleic acids research, 49(2), 700–712. https://doi.org/10.1093/nar/gkaa1247
Aptamer: FB4 (truncated version)
Target: Mouse transferrin receptor (TfR-ECD)
Type of nucleic acid: ssRNA
Sequence: 5'GGACGGAUUGCGGCCGUUGUCUGUGGCGUCCGUUCG3'
Sequence length: 36
GC content: 0.6666666666666666
Affinity: Not reported
Pool type: 5'-TAATACGACTCACTATAGGGCGAATTCCGCGTGTGC-49N-GTCCGTTCGGGATCCTC-3'
Pool random region: 49
Binding buffer/conditions: DNA binding buffer PBS containing 1 mM MgCl2 (PBSM)
Divalent salt: MgCl 
Buffer type: PBS/phosphate buffers
pH: 7.4
Molecular weight of target: Not reported
Post-SELEX modifications: Truncation: "Based on the predicted secondary structure (29) of the five aptamers that shared part of the primary sequence, a truncated version (Fig. S1, boxed) was generated and synthesized. The folded structures of full-length aptamer “FB4” and of its truncated form are shown in Fig. 1A."
Application as quoted in the referenced paper: Research:". In this study, we chose an RNA and a DNA aptamer binding to the extracellular domain of mouse TfR (TfR-ECD) and demonstrated their ability to deliver streptavi_x0002_din to Ltk_x0002_ cells. We then showed the ability of the DNA aptamer to deliver a lysosomal enzyme into deficient mouse fibroblasts and correct the defective glycosaminoglycan (GAG) degradation in these cells
Additional information: After characterization in the model system, the DNA aptamer was conjugated to a lysosomal enzyme, α-l-iduronidase, from which mannose 6-phosphate had been removed. The aptamer had been modified by attachment of terminal glycerol for oxidation by periodate and reaction of the resulting aldehyde with amino groups on the protein.
Reference (2008,Proc Natl Acad Sci U S A): Chen, C. H., Dellamaggiore, K. R., Ouellette, C. P., Sedano, C. D., Lizadjohry, M., Chernis, G. A., Gonzales, M., Baltasar, F. E., Fan, A. L., Myerowitz, R., & Neufeld, E. F. (2008). Aptamer-based endocytosis of a lysosomal enzyme. Proceedings of the National Academy of Sciences of the United States of America, 105(41), 15908–15913. https://doi.org/10.1073/pnas.0808360105