MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it http://mint.bio.uniroma2.it/mint anonymous-2014s-1 Peptides Derived from HIV-1 gp120 Co-receptor Binding Domain Form Amyloid Fibrils and Enhance HIV-1 Infection in vitro In vitro fluorescence fluorescence technology fluorescence predetermined predetermined participant predetermined liusw@smu.edu.cn 2014 imex curation Tan S., Li L., Lu L., Pan C., Lu H., Oksov Y., Tang X., Jiang S., Liu S. FEBS Lett. (0014-5793) Only protein-protein interactions anonymous-2014j-2 Peptides Derived from HIV-1 gp120 Co-receptor Binding Domain Form Amyloid Fibrils and Enhance HIV-1 Infection in vitro In vitro tem transmission electron microscopy tem predetermined predetermined participant predetermined liusw@smu.edu.cn 2014 imex curation Tan S., Li L., Lu L., Pan C., Lu H., Oksov Y., Tang X., Jiang S., Liu S. FEBS Lett. (0014-5793) Only protein-protein interactions env_hv1mn Envelope glycoprotein gp160 env Env polyprotein protein protein hv1mn Human immunodeficiency virus type 1 group M subtype B (isolate MN) MRVKGIRRNYQHWWGWGTMLLGLLMICSATEKLWVTVYYGVPVWKEATTTLFCASDAKAYDTEVHNVWATQACVPTDPNPQEVELVNVTENFNMWKNNMVEQMHEDIISLWDQSLKPCVKLTPLCVTLNCTDLRNTTNTNNSTANNNSNSEGTIKGGEMKNCSFNITTSIRDKMQKEYALLYKLDIVSIDNDSTSYRLISCNTSVITQACPKISFEPIPIHYCAPAGFAILKCNDKKFSGKGSCKNVSTVQCTHGIRPVVSTQLLLNGSLAEEEVVIRSENFTDNAKTIIVHLNESVQINCTRPNYNKRKRIHIGPGRAFYTTKNIIGTIRQAHCNISRAKWNDTLRQIVSKLKEQFKNKTIVFNQSSGGDPEIVMHSFNCGGEFFYCNTSPLFNSTWNGNNTWNNTTGSNNNITLQCKIKQIINMWQEVGKAMYAPPIEGQIRCSSNITGLLLTRDGGKDTDTNDTEIFRPGGGDMRDNWRSELYKYKVVTIEPLGVAPTKAKRRVVQREKRAAIGALFLGFLGAAGSTMGAASVTLTVQARLLLSGIVQQQNNLLRAIEAQQHMLQLTVWGIKQLQARVLAVERYLKDQQLLGFWGCSGKLICTTTVPWNASWSNKSLDDIWNNMTWMQWEREIDNYTSLIYSLLEKSQTQQEKNEQELLELDKWASLWNWFDITNWLWYIKIFIMIVGGLVGLRIVFAVLSIVNRVRQGYSPLSLQTRPPVPRGPDRPEGIEEEGGERDRDTSGRLVHGFLAIIWVDLRSLFLFSYHHRDLLLIAARIVELLGRRGWEVLKYWWNLLQYWSQELKSSAVSLLNATAIAVAEGTDRVIEVLQRAGRAILHIPTRIRQGLERALL ppap_human Prostatic acid phosphatase ACP3 5'-nucleotidase ACPP Acid phosphatase 3 Ecto-5'-nucleotidase Thiamine monophosphatase Protein tyrosine phosphatase ACP3 protein protein human Homo sapiens Human MRAAPLLLARAASLSLGFLFLLFFWLDRSVLAKELKFVTLVFRHGDRSPIDTFPTDPIKESSWPQGFGQLTQLGMEQHYELGEYIRKRYRKFLNESYKHEQVYIRSTDVDRTLMSAMTNLAALFPPEGVSIWNPILLWQPIPVHTVPLSEDQLLYLPFRNCPRFQELESETLKSEEFQKRLHPYKDFIATLGKLSGLHGQDLFGIWSKVYDPLYCESVHNFTLPSWATEDTMTKLRELSELSLLSLYGIHKQKEKSRLQGGVLVNEILNHMKRATQIPSYKKLIMYSAHDTTVSGLQMALDVYNGLLPPYASCHLTELYFEKGEYFVEMYYRNETQHEPYPLMLPGCSPSCPLERFAELVGPVIPQDWSTECMTTNSHQGTEDSTD env-env-1 1511813 n/a EP1 1511815 peptide synthesis peptide synthesis unspecified role unspecified role neutral component neutral component purified purified binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false n/a EP1 1511815 peptide synthesis peptide synthesis unspecified role unspecified role neutral component neutral component purified purified binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false direct interaction direct interaction false false false f2a f2b It was found that the solutions of EPs were turbid. Thus, we speculated that EPs might form amyloid fibrils that were water insoluble. As shown in Figure 2, EPs could bind to the amyloid-specific dyes Congo red and ThT in a dose-dependent manner (Fig. 2A and 2B). Notably, unlike SEVI, which fibril formation requires specific conditions, including agitation, a suitable salt concentration and pH of the solution [19], EPs could spontaneously form amyloid fibrils. env-env-2 1511813 n/a EP2 1511815 peptide synthesis peptide synthesis unspecified role unspecified role neutral component neutral component purified purified binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false n/a EP2 1511815 peptide synthesis peptide synthesis unspecified role unspecified role neutral component neutral component purified purified binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false direct interaction direct interaction false false false f2a f2b f5a f5b It was found that the solutions of EPs were turbid. Thus, we speculated that EPs might form amyloid fibrils that were water insoluble. As shown in Figure 2, EPs could bind to the amyloid-specific dyes Congo red and ThT in a dose-dependent manner (Fig. 2A and 2B). Notably, unlike SEVI, which fibril formation requires specific conditions, including agitation, a suitable salt concentration and pH of the solution [19], EPs could spontaneously form amyloid fibrils. We incubated freshly dissolved EP2 with EGCG, and the formation of the β-sheet structures was monitored. The freshly dissolved peptide could readily bind to ThT, implying a spontaneous process of fibril formation (Fig. 5A). During the incubation period of EP2 and EGCG, the ThT fluorescence intensity decreased in time- and dose-dependent manners, while the signals slightly increased during incubation of EP2 alone (Fig. 5A). Next, we exposed preformed EP2 fibrils to various concentrations of EGCG and monitored the degradation of the fibrillar structures over time via ThT staining. The preformed EP2 amyloid fibrils (550 µM) were highly stable in PBS for a period of 72 h. In contrast, the preformed amyloid fibrils were clearly degraded in the presence of EGCG (Fig. 5B). env-env-3 1511813 n/a EP3 1511815 peptide synthesis peptide synthesis unspecified role unspecified role neutral component neutral component purified purified binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false n/a EP3 1511815 peptide synthesis peptide synthesis unspecified role unspecified role neutral component neutral component purified purified binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false direct interaction direct interaction false false false f2a f2b It was found that the solutions of EPs were turbid. Thus, we speculated that EPs might form amyloid fibrils that were water insoluble. As shown in Figure 2, EPs could bind to the amyloid-specific dyes Congo red and ThT in a dose-dependent manner (Fig. 2A and 2B). Notably, unlike SEVI, which fibril formation requires specific conditions, including agitation, a suitable salt concentration and pH of the solution [19], EPs could spontaneously form amyloid fibrils. acpp-acpp 1511813 n/a SEVI 1511816 peptide synthesis peptide synthesis unspecified role unspecified role unspecified role unspecified role purified purified binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false n/a SEVI 1511816 peptide synthesis peptide synthesis unspecified role unspecified role neutral component neutral component purified purified binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false direct interaction direct interaction false false false f2a f2b Peptides derived from prostatic acidic phosphatase (PAP, predominant component PAP248-286) in semen, designated as semen-derived enhancer of viral infection (SEVI), significantly enhanced HIV-1 infection via the formation of amyloid fibrils env-env-4 1511814 n/a EP1 1511815 peptide synthesis peptide synthesis unspecified role unspecified role neutral component neutral component purified purified binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false n/a EP1 1511815 peptide synthesis peptide synthesis unspecified role unspecified role neutral component neutral component purified purified binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false direct interaction direct interaction false false false f2c Next, we performed transmission microscopy to examine the morphology of amyloid fibrils composed of EPs. Interestingly, the amyloid fibril structures of EPs are different from that of SEVI (Fig. 2C). EPs form short and soft amyloid-like fibrils, while SEVI forms long and rigid amyloid fibrils. env-env-5 1511814 n/a EP2 1511815 peptide synthesis peptide synthesis unspecified role unspecified role neutral component neutral component purified purified binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false n/a EP2 1511815 peptide synthesis peptide synthesis unspecified role unspecified role neutral component neutral component purified purified binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false direct interaction direct interaction false false false f2c Next, we performed transmission microscopy to examine the morphology of amyloid fibrils composed of EPs. Interestingly, the amyloid fibril structures of EPs are different from that of SEVI (Fig. 2C). EPs form short and soft amyloid-like fibrils, while SEVI forms long and rigid amyloid fibrils. env-env-6 1511814 n/a EP3 1511815 peptide synthesis peptide synthesis unspecified role unspecified role neutral component neutral component purified purified binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false n/a EP3 1511815 peptide synthesis peptide synthesis unspecified role unspecified role neutral component neutral component purified purified binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false direct interaction direct interaction false false false f2c Next, we performed transmission microscopy to examine the morphology of amyloid fibrils composed of EPs. Interestingly, the amyloid fibril structures of EPs are different from that of SEVI (Fig. 2C). EPs form short and soft amyloid-like fibrils, while SEVI forms long and rigid amyloid fibrils. acpp-acpp-1 1511814 n/a SEVI 1511816 peptide synthesis peptide synthesis unspecified role unspecified role neutral component neutral component purified purified binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false n/a SEVI 1511816 peptide synthesis peptide synthesis unspecified role unspecified role unspecified role unspecified role purified purified binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false direct interaction direct interaction false false false f2c Next, we performed transmission microscopy to examine the morphology of amyloid fibrils composed of EPs. Interestingly, the amyloid fibril structures of EPs are different from that of SEVI (Fig. 2C). EPs form short and soft amyloid-like fibrils, while SEVI forms long and rigid amyloid fibrils.