cometadata/datacite-titles-descriptions-related-identifiers huggingface dataset:
DOI: 10.13130/rd_unimi/uoloji/bzmv6b
title: Maggio_1936_Pagina_100.jpg

description: Bulletin of 1936/05/25
DOI: 10.13130/rd_unimi/uoloji/sqv1eg
title: Maggio_1936_Pagina_099.jpg

description: Bulletin of 1936/05/25
DOI: 10.13130/rd_unimi/uoloji/klwrut
title: Maggio_1936_Pagina_101.jpg

description: Bulletin of 1936/05/26
DOI: 10.13130/rd_unimi/uoloji/omeurt
title: Maggio_1936_Pagina_102.jpg

description: Bulletin of 1936/05/26
DOI: 10.15468/dl.t2ub3t
title: Occurrence Download

description: A dataset containing 184 species occurrences available in GBIF matching the query:
{
 "DatasetKey" : [
 "is Swedish Malaise Trap Project (SMTP) - Macrolepidoptera"
 ]
}

 The dataset includes 184 records from 1 constituent datasets; see https://api.gbif.org/v1/occurrence/download/0053571-251120083545085/datasets/export for details.
 
Data from some individual datasets included in this download may be licensed under less restrictive terms.
DOI: 10.13130/rd_unimi/uoloji/2zyxa4
title: Maggio_1936_Pagina_104.jpg

description: Bulletin of 1936/05/26
DOI: 10.13130/rd_unimi/uoloji/32eojz
title: Maggio_1936_Pagina_103.jpg

description: Bulletin of 1936/05/26
DOI: 10.13130/rd_unimi/uoloji/8ht7nv
title: Maggio_1936_Pagina_105.jpg

description: Bulletin of 1936/05/27
DOI: 10.13130/rd_unimi/uoloji/kpb75m
title: Maggio_1936_Pagina_106.jpg

description: Bulletin of 1936/05/27
DOI: 10.13130/rd_unimi/uoloji/brldwu
title: Maggio_1936_Pagina_107.jpg

description: Bulletin of 1936/05/27
DOI: 10.13130/rd_unimi/uoloji/hboxwb
title: Maggio_1936_Pagina_109.jpg

description: Bulletin of 1936/05/28
DOI: 10.13130/rd_unimi/uoloji/iv3p9h
title: Maggio_1936_Pagina_108.jpg

description: Bulletin of 1936/05/27
DOI: 10.13130/rd_unimi/uoloji/h4rwmb
title: Maggio_1936_Pagina_110.jpg

description: Bulletin of 1936/05/28
DOI: 10.13130/rd_unimi/uoloji/wqyosy
title: Maggio_1936_Pagina_111.jpg

description: Bulletin of 1936/05/28
DOI: 10.13130/rd_unimi/uoloji/66iq3z
title: Maggio_1936_Pagina_112.jpg

description: Bulletin of 1936/05/28
DOI: 10.13130/rd_unimi/uoloji/igsqiq
title: Maggio_1936_Pagina_113.jpg

description: Bulletin of 1936/05/29
DOI: 10.13130/rd_unimi/uoloji/4r8wu5
title: Maggio_1936_Pagina_114.jpg

description: Bulletin of 1936/05/29
DOI: 10.13130/rd_unimi/uoloji/3ievbc
title: Maggio_1936_Pagina_115.jpg

description: Bulletin of 1936/05/29
DOI: 10.13130/rd_unimi/uoloji/gu3pt7
title: Maggio_1936_Pagina_116.jpg

description: Bulletin of 1936/05/29
DOI: 10.13130/rd_unimi/uoloji/j2byxe
title: Maggio_1936_Pagina_117.jpg

description: Bulletin of 1936/05/30
DOI: 10.13130/rd_unimi/uoloji/7rvmh6
title: Maggio_1936_Pagina_118.jpg

description: Bulletin of 1936/05/30
DOI: 10.13130/rd_unimi/uoloji/3egiyt
title: Maggio_1936_Pagina_119.jpg

description: Bulletin of 1936/05/30
DOI: 10.13130/rd_unimi/uoloji/vzhhoz
title: Maggio_1936_Pagina_120.jpg

description: Bulletin of 1936/05/30
DOI: 10.13130/rd_unimi/uoloji/cjlufx
title: Maggio_1936_Pagina_121.jpg

description: Bulletin of 1936/05/31
DOI: 10.13130/rd_unimi/uoloji/zkwp7j
title: Maggio_1936_Pagina_122.jpg

description: Bulletin of 1936/05/31
DOI: 10.13130/rd_unimi/uoloji/fsvtng
title: Maggio_1936_Pagina_124.jpg

description: Bulletin of 1936/05/31
DOI: 10.13130/rd_unimi/uoloji/mstedk
title: Maggio_1936_Pagina_123.jpg

description: Bulletin of 1936/05/31
DOI: 10.13130/rd_unimi/uoloji/1fulka
title: Marzo_1936_Pagina_001.jpg

description: Bulletin of 1936/03/01
DOI: 10.13130/rd_unimi/uoloji/xqtra1
title: Marzo_1936_Pagina_002.jpg

description: Bulletin of 1936/03/01
DOI: 10.13130/rd_unimi/uoloji/6gdbnc
title: Marzo_1936_Pagina_003.jpg

description: Bulletin of 1936/03/01
DOI: 10.13130/rd_unimi/uoloji/bkqsj9
title: Marzo_1936_Pagina_004.jpg

description: Bulletin of 1936/03/01
DOI: 10.13130/rd_unimi/uoloji/gukuy2
title: Marzo_1936_Pagina_005.jpg

description: Bulletin of 1936/03/02
DOI: 10.13130/rd_unimi/uoloji/t5uhwg
title: Marzo_1936_Pagina_006.jpg

description: Bulletin of 1936/03/02
DOI: 10.13130/rd_unimi/uoloji/msay4u
title: Marzo_1936_Pagina_007.jpg

description: Bulletin of 1936/03/02
DOI: 10.13130/rd_unimi/uoloji/8oz1yn
title: Marzo_1936_Pagina_009.jpg

description: Bulletin of 1936/03/03
DOI: 10.13130/rd_unimi/uoloji/twhvzn
title: Marzo_1936_Pagina_008.jpg

description: Bulletin of 1936/03/02
DOI: 10.13130/rd_unimi/uoloji/szggnn
title: Marzo_1936_Pagina_010.jpg

description: Bulletin of 1936/03/03
DOI: 10.13130/rd_unimi/uoloji/fyennx
title: Marzo_1936_Pagina_011.jpg

description: Bulletin of 1936/03/03
DOI: 10.6084/m9.figshare.28130026
title: The new thiazolidine-2,4-dione-based hybrids with promising antimycobacterial activity: design, synthesis, biological evaluation, and drug interaction analysis

description: The ever-increasing drug-resistant tuberculosis (TB) has invigorated the focus on the discovery and development of novel therapeutic agents and treatment options. Thiazolidinone-based compounds have shown good antitubercular properties <i>in vitro</i>. Here, we report the design and synthesis of a number of new derivatives inspired by the structure of thiazolidine-2,4-dione (TZD). The TZD-based hybrids with the thiosemicarbazone or the pyridinecarbohydrazone moiety were synthesised and their antimycobacterial activity was investigated against the reference H<sub>37</sub>Rv and two wild <i>Mycobacterium tuberculosis</i> (<i>Mtb</i>) strains. In further studies, a two-drug interaction analysis was also performed for assessing their synergism with the current first-line drugs used for the treatment of TB. It was found that some of the compounds showed high antimycobacterial activity with MICs (0.078–0.283 µM) and a synergistic effect with isoniazid or rifampicin, thereby demonstrating their potential as a promising scaffold for the development of novel coadjuvants for the effective treatment of TB.
DOI: 10.6084/m9.figshare.28130026.v1
title: The new thiazolidine-2,4-dione-based hybrids with promising antimycobacterial activity: design, synthesis, biological evaluation, and drug interaction analysis

description: The ever-increasing drug-resistant tuberculosis (TB) has invigorated the focus on the discovery and development of novel therapeutic agents and treatment options. Thiazolidinone-based compounds have shown good antitubercular properties <i>in vitro</i>. Here, we report the design and synthesis of a number of new derivatives inspired by the structure of thiazolidine-2,4-dione (TZD). The TZD-based hybrids with the thiosemicarbazone or the pyridinecarbohydrazone moiety were synthesised and their antimycobacterial activity was investigated against the reference H<sub>37</sub>Rv and two wild <i>Mycobacterium tuberculosis</i> (<i>Mtb</i>) strains. In further studies, a two-drug interaction analysis was also performed for assessing their synergism with the current first-line drugs used for the treatment of TB. It was found that some of the compounds showed high antimycobacterial activity with MICs (0.078–0.283 µM) and a synergistic effect with isoniazid or rifampicin, thereby demonstrating their potential as a promising scaffold for the development of novel coadjuvants for the effective treatment of TB.
DOI: 10.13130/rd_unimi/uoloji/nvllkg
title: Marzo_1936_Pagina_012.jpg

description: Bulletin of 1936/03/03
DOI: 10.6084/m9.figshare.29070439
title: Activity guided discovery of dual inhibitors of α-glucosidase and β-glucuronidase from the leaves of <i>Millettia pachycarpa</i> Benth

description: Type 2 diabetes mellitus (T2DM) and cancers are two globally prevalent diseases which can increase the incidence of each other. Intestinal α-glucosidase and β-glucuronidase are key targets for glycaemic control and chemotherapy detoxification, respectively. This study first found that the leaf methanol extract of <i>Millettia pachycarpa</i> displayed dual inhibition to the two enzymes. The dually active constituents were then isolated and identified as two prenylated isoflavones of 6,8-diprenylorobol and 6,8-diprenylgenistein. Diprenylorobol exhibits competitive inhibition to both the two enzymes with <i>K<sub>i</sub></i> values of 21.6 μM (α-glucosidase) and 1.41 μM (β-glucuronidase). Diprenylgenistein is an uncompetitive inhibitor of α-glucosidase (<i>K<sub>i</sub></i> = 11.4 μM) but a competitive inhibitor of β-glucuronidase (<i>K<sub>i</sub></i> = 1.69 μM). Molecular docking studies showed that both the two isoflavones tightly bind into the active pockets via various hydrogen bonds and hydrophobic interactions. In summary, the current study identifies two promising dual inhibitors of α-glucosidase and β-glucuronidase from the leaves of <i>Millettia pachycarpa</i>.
DOI: 10.6084/m9.figshare.29070439.v1
title: Activity guided discovery of dual inhibitors of α-glucosidase and β-glucuronidase from the leaves of <i>Millettia pachycarpa</i> Benth

description: Type 2 diabetes mellitus (T2DM) and cancers are two globally prevalent diseases which can increase the incidence of each other. Intestinal α-glucosidase and β-glucuronidase are key targets for glycaemic control and chemotherapy detoxification, respectively. This study first found that the leaf methanol extract of <i>Millettia pachycarpa</i> displayed dual inhibition to the two enzymes. The dually active constituents were then isolated and identified as two prenylated isoflavones of 6,8-diprenylorobol and 6,8-diprenylgenistein. Diprenylorobol exhibits competitive inhibition to both the two enzymes with <i>K<sub>i</sub></i> values of 21.6 μM (α-glucosidase) and 1.41 μM (β-glucuronidase). Diprenylgenistein is an uncompetitive inhibitor of α-glucosidase (<i>K<sub>i</sub></i> = 11.4 μM) but a competitive inhibitor of β-glucuronidase (<i>K<sub>i</sub></i> = 1.69 μM). Molecular docking studies showed that both the two isoflavones tightly bind into the active pockets via various hydrogen bonds and hydrophobic interactions. In summary, the current study identifies two promising dual inhibitors of α-glucosidase and β-glucuronidase from the leaves of <i>Millettia pachycarpa</i>.
DOI: 10.13130/rd_unimi/uoloji/k4mpny
title: Marzo_1936_Pagina_014.jpg

description: Bulletin of 1936/03/04
DOI: 10.13130/rd_unimi/uoloji/nba9a0
title: Marzo_1936_Pagina_013.jpg

description: Bulletin of 1936/03/04
DOI: 10.13130/rd_unimi/uoloji/3zhg7y
title: Marzo_1936_Pagina_015.jpg

description: Bulletin of 1936/03/04
DOI: 10.13130/rd_unimi/uoloji/nejmdu
title: Marzo_1936_Pagina_016.jpg

description: Bulletin of 1936/03/04
DOI: 10.13130/rd_unimi/uoloji/qmhtpi
title: Marzo_1936_Pagina_017.jpg

description: Bulletin of 1936/03/05
DOI: 10.13130/rd_unimi/uoloji/euqhxg
title: Marzo_1936_Pagina_018.jpg

description: Bulletin of 1936/03/05
DOI: 10.13130/rd_unimi/uoloji/ctcgh4
title: Marzo_1936_Pagina_019.jpg

description: Bulletin of 1936/03/05
DOI: 10.13130/rd_unimi/uoloji/sifkpq
title: Marzo_1936_Pagina_020.jpg

description: Bulletin of 1936/03/05
DOI: 10.6084/m9.figshare.30884765
title: Dataset for ECI paper

description: This is data used for my ecological footprint and economic development of Africa paper. You can use it as and when you want.
DOI: 10.6084/m9.figshare.30884765.v1
title: Dataset for ECI paper

description: This is data used for my ecological footprint and economic development of Africa paper. You can use it as and when you want.
DOI: 10.13130/rd_unimi/uoloji/t9goip
title: Marzo_1936_Pagina_021.jpg

description: Bulletin of 1936/03/06
DOI: 10.13130/rd_unimi/uoloji/tt1wod
title: Marzo_1936_Pagina_022.jpg

description: Bulletin of 1936/03/06
DOI: 10.13130/rd_unimi/uoloji/evd37a
title: Marzo_1936_Pagina_023.jpg

description: Bulletin of 1936/03/06
DOI: 10.13130/rd_unimi/uoloji/sl6cgf
title: Marzo_1936_Pagina_024.jpg

description: Bulletin of 1936/03/06
DOI: 10.13130/rd_unimi/uoloji/psqyeo
title: Marzo_1936_Pagina_025.jpg

description: Bulletin of 1936/03/07
DOI: 10.6084/m9.figshare.30884637
title: Study on the phosphorylation of NAD<sup>+</sup>-specific isocitrate dehydrogenase in the pathogenic bacteria <i>Stenotrophomonas maltophilia</i> and <i>Xanthomonas sacchari</i>

description: Isocitrate dehydrogenases (IDHs) regulate the distribution of carbon flux between the TCA cycle and glyoxylate shunt through reversible phosphorylation that influences pathogen virulence. Current studies only indicate that NADP<sup>+</sup>-specific IDHs (NADP-IDHs) can be phosphorylated. Whether NAD<sup>+</sup>-specific IDHs (NAD-IDHs) are susceptible to phosphorylation remains unknown. In this study, two NAD-IDHs and their regulation by phosphorylation from <i>Stenotrophomonas maltophilia</i> and <i>Xanthomonas sacchari</i> were characterised for the first time. Ser80 was identified by mass spectrometry as the phosphorylation site in SmIDH, which was functionally validated through site-directed mutagenesis. Acetate induction led to an approximately 78% decrease in the ratio of IDH/ICL specific enzyme activity, consistent with phosphorylation-mediated regulation. By modifying key recognition regions in XsIDH and XsAceK, the phosphorylation efficiency of XsIDH was improved, revealing evolutionary insights. It may enable further investigations for the new antibacterial drug targets in <i>S. maltophilia</i> and <i>X. sacchari</i>.
DOI: 10.6084/m9.figshare.30884637.v1
title: Study on the phosphorylation of NAD<sup>+</sup>-specific isocitrate dehydrogenase in the pathogenic bacteria <i>Stenotrophomonas maltophilia</i> and <i>Xanthomonas sacchari</i>

description: Isocitrate dehydrogenases (IDHs) regulate the distribution of carbon flux between the TCA cycle and glyoxylate shunt through reversible phosphorylation that influences pathogen virulence. Current studies only indicate that NADP<sup>+</sup>-specific IDHs (NADP-IDHs) can be phosphorylated. Whether NAD<sup>+</sup>-specific IDHs (NAD-IDHs) are susceptible to phosphorylation remains unknown. In this study, two NAD-IDHs and their regulation by phosphorylation from <i>Stenotrophomonas maltophilia</i> and <i>Xanthomonas sacchari</i> were characterised for the first time. Ser80 was identified by mass spectrometry as the phosphorylation site in SmIDH, which was functionally validated through site-directed mutagenesis. Acetate induction led to an approximately 78% decrease in the ratio of IDH/ICL specific enzyme activity, consistent with phosphorylation-mediated regulation. By modifying key recognition regions in XsIDH and XsAceK, the phosphorylation efficiency of XsIDH was improved, revealing evolutionary insights. It may enable further investigations for the new antibacterial drug targets in <i>S. maltophilia</i> and <i>X. sacchari</i>.
DOI: 10.13130/rd_unimi/uoloji/0oxpmy
title: Marzo_1936_Pagina_026.jpg

description: Bulletin of 1936/03/07
DOI: 10.13130/rd_unimi/uoloji/j1c5ax
title: Marzo_1936_Pagina_027.jpg

description: Bulletin of 1936/03/07
DOI: 10.6084/m9.figshare.30406383
title: Targeting MED8 enhances sorafenib sensitivity in hepatocellular carcinoma by disrupting epithelial–mesenchymal transition mechanisms

description: HCC is a highly lethal cancer characterised by significant sorafenib resistance, leading to poor patient outcomes. Recent studies have suggested that MED8 plays a role in enhancing tumour resistance to drugs, but its role in drug resistance in HCC has not yet been reported. This study found significantly higher MED8 expression in HCC tissues compared to adjacent noncancerous tissues. Increased MED8 expression in HCC correlates with poorer overall survival. Functional assays demonstrated that reduced MED8 expression inhibited HCC cell proliferation and epithelial–mesenchymal transition, promoted apoptosis, and increased sensitivity to sorafenib. Overexpression of MED8 elevated TRIP4 protein levels. TRIP4 overexpression negated the effects of MED8 knockdown, whereas TRIP4 suppression inhibited MED8-driven EMT. Mechanistically, MED8 interacts with TRIP4, reducing its ubiquitination and stabilising TRIP4 protein levels. Our findings indicate that the MED8–TRIP4 axis plays a role in sorafenib resistance in HCC and could serve as a therapeutic target for HCC treatment. Elevated MED8 is closely associated with sorafenib resistance in HCC cells. MED8 contributes to sorafenib resistance of HCC by enhancing TRIP4-mediated EMT. MED8 interacts with TRIP4’s N-terminal (aa 1–150) and C-terminal (aa 301–581) domains.
DOI: 10.6084/m9.figshare.30406383.v1
title: Targeting MED8 enhances sorafenib sensitivity in hepatocellular carcinoma by disrupting epithelial–mesenchymal transition mechanisms

description: HCC is a highly lethal cancer characterised by significant sorafenib resistance, leading to poor patient outcomes. Recent studies have suggested that MED8 plays a role in enhancing tumour resistance to drugs, but its role in drug resistance in HCC has not yet been reported. This study found significantly higher MED8 expression in HCC tissues compared to adjacent noncancerous tissues. Increased MED8 expression in HCC correlates with poorer overall survival. Functional assays demonstrated that reduced MED8 expression inhibited HCC cell proliferation and epithelial–mesenchymal transition, promoted apoptosis, and increased sensitivity to sorafenib. Overexpression of MED8 elevated TRIP4 protein levels. TRIP4 overexpression negated the effects of MED8 knockdown, whereas TRIP4 suppression inhibited MED8-driven EMT. Mechanistically, MED8 interacts with TRIP4, reducing its ubiquitination and stabilising TRIP4 protein levels. Our findings indicate that the MED8–TRIP4 axis plays a role in sorafenib resistance in HCC and could serve as a therapeutic target for HCC treatment. Elevated MED8 is closely associated with sorafenib resistance in HCC cells. MED8 contributes to sorafenib resistance of HCC by enhancing TRIP4-mediated EMT. MED8 interacts with TRIP4’s N-terminal (aa 1–150) and C-terminal (aa 301–581) domains.
DOI: 10.13130/rd_unimi/uoloji/srx7p9
title: Marzo_1936_Pagina_028.jpg

description: Bulletin of 1936/03/07
DOI: 10.6084/m9.figshare.29270132
title: Exploring structure–activity relationships of pyrrolyl diketo acid derivatives as non-nucleoside inhibitors of terminal deoxynucleotidyl transferase enzyme

description: Terminal deoxynucleotidyl transferase (TdT) is overexpressed in some cancer types, where it drives the mutagenic repair of double strand breaks through non canonical non-homologous end joining pathway. The TdT enzyme belongs to the X family of polymerases, together with the DNA polymerase λ (pol λ) and β (pol β). However, TdT exclusively displays template-independent nucleotide polymerisation. Pursuing our studies in developing TdT inhibitors, herein we deepened the structure-activity relationships of new structural analogues of our previously identified hit compounds. The diketo hexenoic acid derivatives here analysed showed high selectivity towards TdT and inhibition potencies spanning from the low micromolar range to the nanomolar. Docking studies highlighted the chemical features involved in the TdT binding, well contributing to the rationalisation of the structural requirements needed for the enzymatic inhibition.
DOI: 10.13130/rd_unimi/uoloji/sjpbu6
title: Marzo_1936_Pagina_029.jpg

description: Bulletin of 1936/03/08
DOI: 10.6084/m9.figshare.29270132.v1
title: Exploring structure–activity relationships of pyrrolyl diketo acid derivatives as non-nucleoside inhibitors of terminal deoxynucleotidyl transferase enzyme

description: Terminal deoxynucleotidyl transferase (TdT) is overexpressed in some cancer types, where it drives the mutagenic repair of double strand breaks through non canonical non-homologous end joining pathway. The TdT enzyme belongs to the X family of polymerases, together with the DNA polymerase λ (pol λ) and β (pol β). However, TdT exclusively displays template-independent nucleotide polymerisation. Pursuing our studies in developing TdT inhibitors, herein we deepened the structure-activity relationships of new structural analogues of our previously identified hit compounds. The diketo hexenoic acid derivatives here analysed showed high selectivity towards TdT and inhibition potencies spanning from the low micromolar range to the nanomolar. Docking studies highlighted the chemical features involved in the TdT binding, well contributing to the rationalisation of the structural requirements needed for the enzymatic inhibition.
DOI: 10.13130/rd_unimi/uoloji/n0uwgx
title: Marzo_1936_Pagina_030.jpg

description: Bulletin of 1936/03/08
DOI: 10.13130/rd_unimi/uoloji/e290ai
title: Marzo_1936_Pagina_031.jpg

description: Bulletin of 1936/03/08
DOI: 10.13130/rd_unimi/uoloji/hzkkqp
title: Marzo_1936_Pagina_032.jpg

description: Bulletin of 1936/03/08
DOI: 10.13130/rd_unimi/uoloji/stlryw
title: Marzo_1936_Pagina_033.jpg

description: Bulletin of 1936/03/09
DOI: 10.13130/rd_unimi/uoloji/gdvtkk
title: Marzo_1936_Pagina_034.jpg

description: Bulletin of 1936/03/09
DOI: 10.13130/rd_unimi/uoloji/jl2wj9
title: Marzo_1936_Pagina_035.jpg

description: Bulletin of 1936/03/09
DOI: 10.13130/rd_unimi/uoloji/hccrhn
title: Marzo_1936_Pagina_037.jpg

description: Bulletin of 1936/03/10
DOI: 10.13130/rd_unimi/uoloji/wlkwkg
title: Marzo_1936_Pagina_036.jpg

description: Bulletin of 1936/03/09
DOI: 10.13130/rd_unimi/uoloji/xxoyyx
title: Marzo_1936_Pagina_038.jpg

description: Bulletin of 1936/03/10