cometadata/datacite-titles-descriptions-related-identifiers huggingface dataset:
DOI: 10.5281/zenodo.17865543
title: Table 2 in Rhinolekos, a new genus with three new species of Hypoptopomatinae (Siluriformes: Loricariidae) from upper rio Paraná

description: Table 2. Frequency distribution of meristics for Rhinolekos britskii (DZSJRP 5614, 6514, 6884, 7018, 7022, 7036, 7042, 12190; MCP 44058; MNRJ 34128; MZUSP 103698).
CharacterFrequency distributionRangeModeDorsal plates24-2826right side24(1); 25(1); 26(2); 27(1); 28(1)left side25(1); 26(3); 27(1); 28(1)Mid-dorsal plates21-2421/22right side21(2); 22(2); 23(1); 24(1)left side21(2); 22(2); 23(1); 24(1)Median plates26-3027right side26(1); 27(2); 28(2); 30(1)left side26(1); 27(3); 28(2)Mid-ventral plates22-2522right side22(2); 23(3); 25(1)left side22(4); 23(1); 25(1)Ventral plates24-2926/27/28rigth side26(1); 27(1); 28(3); 29(1)left side24(1); 26(2); 27(2); 29(1)Premaxillary teeth19-2825right side20(1); 22(1); 23(2); 25(1); 28(1)left side19(1); 21(1); 22(1); 24(1); 25(2)Dentary teeth18-2520right side18(1); 19(1); 20(2); 23(1); 24(1)left side18(1); 19(1); 20(1); 21(1); 24(1); 25(1)Dorsal-fin branched rays6(4); 7(26)6-77Pectoral-fin branched rays6 (30)-30Pelvic-fin branched rays5 (30)-5Anal-fin branched rays5 (30)-5Caudal-fin branched rays14(30)-14Dorsal procurrent rays4(2); 5(2)4-5-Ventral procurrent rays4(4)44Vertebrae31(4)-31
description: Published as part of Martins, Fernanda de Oliveira & Langeani, Francisco, 2011, Rhinolekos, a new genus with three new species of Hypoptopomatinae (Siluriformes: Loricariidae) from upper rio Paraná, pp. 71 in Neotropical Ichthyology 9 (1) on page 71, DOI: 10.1590/S1679-62252011000100005, http://zenodo.org/record/5422809
DOI: 10.5281/zenodo.17865545
title: Table 3 in Rhinolekos, a new genus with three new species of Hypoptopomatinae (Siluriformes: Loricariidae) from upper rio Paraná

description: Table 3. Descriptive morphometrics of Rhinolekos garavelloi.Values given for holotype (H; DZSJRP 10479) and range of 30 specimens (DZSJRP 10477, 12191; MCP 44057; MNRJ 34127; MZUSP 103697); range includes holotype. SD = Standard deviation.
HMinimumMaximumMeanSDStandard length (mm)31.429.036.2--Percents of Standard lengthPredorsal length50.446.653.349.11.5Preanal length62.057.866.060.51.8Prepectoral length27.924.429.727.01.2Prepelvic length38.336.042.338.51.2Postanal length30.929.034.631.81.3Thoracic length20.318.120.819.50.8Abdominal length22.320.625.723.21.2Caudal-peduncle depth11.910.313.011.50.5Head length34.029.335.332.61.2Head width26.624.628.126.00.8Head depth16.113.216.215.10.6Base of dorsal-fin length10.19.312.611.00.9Folded dorsal-fin length23.422.425.723.50.8Pectoral-fin unbranched ray length20.116.621.119.41.1Pelvic-fin unbranched ray length20.215.221.118.71.6Snout-opercle length28.124.728.526.70.8Percents of Head lengthHead width78.369.987.179.73.2Head depth47.240.652.346.22.3Snout length51.348.559.652.92.6Orbital diameter14.312.916.815.11.0Interorbital length36.434.742.137.31.4Barbel length8.66.59.98.20.7Prenasal length32.632.542.235.52.1Internasal length9.59.514.411.51.0Suborbital depth26.722.328.125.71.5
description: Published as part of Martins, Fernanda de Oliveira & Langeani, Francisco, 2011, Rhinolekos, a new genus with three new species of Hypoptopomatinae (Siluriformes: Loricariidae) from upper rio Paraná, pp. 73 in Neotropical Ichthyology 9 (1) on page 73, DOI: 10.1590/S1679-62252011000100005, http://zenodo.org/record/5422809
DOI: 10.5281/zenodo.17865546
title: Table 3 in Rhinolekos, a new genus with three new species of Hypoptopomatinae (Siluriformes: Loricariidae) from upper rio Paraná

description: Table 3. Descriptive morphometrics of Rhinolekos garavelloi.Values given for holotype (H; DZSJRP 10479) and range of 30 specimens (DZSJRP 10477, 12191; MCP 44057; MNRJ 34127; MZUSP 103697); range includes holotype. SD = Standard deviation.
HMinimumMaximumMeanSDStandard length (mm)31.429.036.2--Percents of Standard lengthPredorsal length50.446.653.349.11.5Preanal length62.057.866.060.51.8Prepectoral length27.924.429.727.01.2Prepelvic length38.336.042.338.51.2Postanal length30.929.034.631.81.3Thoracic length20.318.120.819.50.8Abdominal length22.320.625.723.21.2Caudal-peduncle depth11.910.313.011.50.5Head length34.029.335.332.61.2Head width26.624.628.126.00.8Head depth16.113.216.215.10.6Base of dorsal-fin length10.19.312.611.00.9Folded dorsal-fin length23.422.425.723.50.8Pectoral-fin unbranched ray length20.116.621.119.41.1Pelvic-fin unbranched ray length20.215.221.118.71.6Snout-opercle length28.124.728.526.70.8Percents of Head lengthHead width78.369.987.179.73.2Head depth47.240.652.346.22.3Snout length51.348.559.652.92.6Orbital diameter14.312.916.815.11.0Interorbital length36.434.742.137.31.4Barbel length8.66.59.98.20.7Prenasal length32.632.542.235.52.1Internasal length9.59.514.411.51.0Suborbital depth26.722.328.125.71.5
description: Published as part of Martins, Fernanda de Oliveira & Langeani, Francisco, 2011, Rhinolekos, a new genus with three new species of Hypoptopomatinae (Siluriformes: Loricariidae) from upper rio Paraná, pp. 73 in Neotropical Ichthyology 9 (1) on page 73, DOI: 10.1590/S1679-62252011000100005, http://zenodo.org/record/5422809
DOI: 10.5281/zenodo.17865550
title: Table 4 in Rhinolekos, a new genus with three new species of Hypoptopomatinae (Siluriformes: Loricariidae) from upper rio Paraná

description: Table 4. Frequency distribution of meristics for Rhinolekos garavelloi (DZSJRP 10477, 12191; MCP 44057; MNRJ 34127; MZUSP 103697).
CharacterFrequency distributionRangeModeDorsal plates30-3534right side30(2); 31(1); 32(1); 34(2); 35(1)left side31(2); 32(2); 33(1); 34(2)Mid-dorsal plates23-2724/25right side24(2); 25(3); 26(2)left side23(1); 24(2); 25(1); 27(3)Median plates28-3230/31right side29(2); 30(1); 31(2); 32(2)left side28(1); 29(1); 30(3); 31(2)Mid-ventral plates24-2824right side24(2); 25(4); 28(1)left side24(4); 25(1); 27(2)Ventral plates27-3327right side27(1); 28(2); 30(2); 33(1)left side27(3); 28(1); 29(1); 32(1)Premaxillary teeth20-3420right side20(1); 24(2); 32(1); 33(1); 34(2)left side20(2); 22(1); 30(1); 31(1); 32(1); 33(1)Dentary teeth18-3118/28/29right side18(3); 27(1); 28(1); 29(1); 31(1)left side19(1); 20(2); 28(2); 29(2)Dorsal-fin branched rays6(9); 7(27)6-77Pectoral-fin branched rays6(36)--Pelvic-fin branched rays4(1); 5(35)4-55Anal-fin branched rays3(1); 4(1); 5(34)3-55Caudal-fin branched rays14(33); 15(3)14-1514Dorsal procurrent rays4(5); 5(1)4-54Ventral procurrent rays3(1); 4(2); 5(2); 6(1)3-64/5Vertebrae32(5)-32
description: Published as part of Martins, Fernanda de Oliveira & Langeani, Francisco, 2011, Rhinolekos, a new genus with three new species of Hypoptopomatinae (Siluriformes: Loricariidae) from upper rio Paraná, pp. 73 in Neotropical Ichthyology 9 (1) on page 73, DOI: 10.1590/S1679-62252011000100005, http://zenodo.org/record/5422809
DOI: 10.5281/zenodo.17865551
title: Table 4 in Rhinolekos, a new genus with three new species of Hypoptopomatinae (Siluriformes: Loricariidae) from upper rio Paraná

description: Table 4. Frequency distribution of meristics for Rhinolekos garavelloi (DZSJRP 10477, 12191; MCP 44057; MNRJ 34127; MZUSP 103697).
CharacterFrequency distributionRangeModeDorsal plates30-3534right side30(2); 31(1); 32(1); 34(2); 35(1)left side31(2); 32(2); 33(1); 34(2)Mid-dorsal plates23-2724/25right side24(2); 25(3); 26(2)left side23(1); 24(2); 25(1); 27(3)Median plates28-3230/31right side29(2); 30(1); 31(2); 32(2)left side28(1); 29(1); 30(3); 31(2)Mid-ventral plates24-2824right side24(2); 25(4); 28(1)left side24(4); 25(1); 27(2)Ventral plates27-3327right side27(1); 28(2); 30(2); 33(1)left side27(3); 28(1); 29(1); 32(1)Premaxillary teeth20-3420right side20(1); 24(2); 32(1); 33(1); 34(2)left side20(2); 22(1); 30(1); 31(1); 32(1); 33(1)Dentary teeth18-3118/28/29right side18(3); 27(1); 28(1); 29(1); 31(1)left side19(1); 20(2); 28(2); 29(2)Dorsal-fin branched rays6(9); 7(27)6-77Pectoral-fin branched rays6(36)--Pelvic-fin branched rays4(1); 5(35)4-55Anal-fin branched rays3(1); 4(1); 5(34)3-55Caudal-fin branched rays14(33); 15(3)14-1514Dorsal procurrent rays4(5); 5(1)4-54Ventral procurrent rays3(1); 4(2); 5(2); 6(1)3-64/5Vertebrae32(5)-32
description: Published as part of Martins, Fernanda de Oliveira & Langeani, Francisco, 2011, Rhinolekos, a new genus with three new species of Hypoptopomatinae (Siluriformes: Loricariidae) from upper rio Paraná, pp. 73 in Neotropical Ichthyology 9 (1) on page 73, DOI: 10.1590/S1679-62252011000100005, http://zenodo.org/record/5422809
DOI: 10.5281/zenodo.17865552
title: Table 5 in Rhinolekos, a new genus with three new species of Hypoptopomatinae (Siluriformes: Loricariidae) from upper rio Paraná

description: Table 5. Descriptive morphometrics of Rhinolekos schaeferi. Values given for holotype (H; MCP 26939) and ranges of 13 specimens (DZSJRP 12192; MCP 44056); range includes holotype. SD = Standard deviation.
HMinimumMaximumMeanSDStandard length (mm)35.427.238.5--Percents of Standard lengthPredorsal length47.745.550.147.81.5Preanal length56.555.258.556.51.1Prepectoral length26.023.727.525.61.0Prepelvic length34.434.336.635.30.7Postanal length38.335.741.337.91.6Thoracic length13.913.717.615.31.2Abdominal length22.119.822.220.90.9Caudal-peduncle depth8.67.78.78.20.3Head length30.029.032.230.71.1Head width20.820.522.921.60.9Head depth13.011.814.813.20.8Base of dorsal-fin length11.19.412.511.20.7Folded dorsal-fin length19.518.923.420.51.2Pectoral-fin unbranched ray length18.516.120.518.21.1Pelvic-fin unbranched ray length17.014.019.616.21.3Snout-opercle length25.123.926.225.10.8Percents of Head lengthHead width69.365.375.370.53.0Head depth43.339.446.343.02.3Snout length58.453.359.456.31.6Orbital diameter14.212.617.314.71.2Interorbital length39.232.340.035.92.0Barbel length5.83.76.65.20.8Prenasal length40.737.641.339.31.1Internasal length8.58.211.29.51.0Suborbital depth22.521.927.423.81.8
description: Published as part of Martins, Fernanda de Oliveira & Langeani, Francisco, 2011, Rhinolekos, a new genus with three new species of Hypoptopomatinae (Siluriformes: Loricariidae) from upper rio Paraná, pp. 76 in Neotropical Ichthyology 9 (1) on page 76, DOI: 10.1590/S1679-62252011000100005, http://zenodo.org/record/5422809
DOI: 10.5281/zenodo.17865553
title: Table 5 in Rhinolekos, a new genus with three new species of Hypoptopomatinae (Siluriformes: Loricariidae) from upper rio Paraná

description: Table 5. Descriptive morphometrics of Rhinolekos schaeferi. Values given for holotype (H; MCP 26939) and ranges of 13 specimens (DZSJRP 12192; MCP 44056); range includes holotype. SD = Standard deviation.
HMinimumMaximumMeanSDStandard length (mm)35.427.238.5--Percents of Standard lengthPredorsal length47.745.550.147.81.5Preanal length56.555.258.556.51.1Prepectoral length26.023.727.525.61.0Prepelvic length34.434.336.635.30.7Postanal length38.335.741.337.91.6Thoracic length13.913.717.615.31.2Abdominal length22.119.822.220.90.9Caudal-peduncle depth8.67.78.78.20.3Head length30.029.032.230.71.1Head width20.820.522.921.60.9Head depth13.011.814.813.20.8Base of dorsal-fin length11.19.412.511.20.7Folded dorsal-fin length19.518.923.420.51.2Pectoral-fin unbranched ray length18.516.120.518.21.1Pelvic-fin unbranched ray length17.014.019.616.21.3Snout-opercle length25.123.926.225.10.8Percents of Head lengthHead width69.365.375.370.53.0Head depth43.339.446.343.02.3Snout length58.453.359.456.31.6Orbital diameter14.212.617.314.71.2Interorbital length39.232.340.035.92.0Barbel length5.83.76.65.20.8Prenasal length40.737.641.339.31.1Internasal length8.58.211.29.51.0Suborbital depth22.521.927.423.81.8
description: Published as part of Martins, Fernanda de Oliveira & Langeani, Francisco, 2011, Rhinolekos, a new genus with three new species of Hypoptopomatinae (Siluriformes: Loricariidae) from upper rio Paraná, pp. 76 in Neotropical Ichthyology 9 (1) on page 76, DOI: 10.1590/S1679-62252011000100005, http://zenodo.org/record/5422809
DOI: 10.15468/dl.8spehw
title: Occurrence Download

description: A dataset containing 3483 species occurrences available in GBIF matching the query:
{
 "DatasetKey" : [
 "is Arthropod fauna in christmas tree plantations"
 ]
}

 The dataset includes 3483 records from 1 constituent datasets; see https://api.gbif.org/v1/occurrence/download/0040310-251120083545085/datasets/export for details.
 
Data from some individual datasets included in this download may be licensed under less restrictive terms.
DOI: 10.15468/dl.xavxus
title: Occurrence Download

description: A dataset containing 1932 species occurrences available in GBIF matching the query:
{
 "and" : [
 "TaxonKey is Fridericia callosa",
 "HasCoordinate is true",
 "HasGeospatialIssue is false"
 ]
}

 The dataset includes 1932 records from 12 constituent datasets; see https://api.gbif.org/v1/occurrence/download/0040311-251120083545085/datasets/export for details.
 
Data from some individual datasets included in this download may be licensed under less restrictive terms.
DOI: 10.5281/zenodo.15736571
title: Swallow-dataset-extended
DOI: 10.5281/zenodo.17861912
title: Swallow-dataset-extended
DOI: 10.17026/ar/otvyzq
title: PAN-00118601 - coin/coin-related, Lodewijk de Vrome (814-840), penning

description: &lt;p&gt;This find is registered at Portable Antiquities of the Netherlands with number PAN-00118601&lt;/p&gt;
description: Modified: 2025-10-21T08:42:25+02:00
DOI: 10.6084/m9.figshare.28448514
title: Biophysical and structural mechanisms of epilepsy-associated mutations in the S4-S5 Linker of KCNQ2 channels

description: Mutations in <i>KCNQ2</i> are linked to various neurological disorders, including neonatal-onset epilepsy. The severity of these conditions often correlates with the mutation’s location and the biochemical properties of the altered amino acid side chains. Two mutations affecting aspartate at position 212 (D212) in the S4-S5 linker of KCNQ2 have been identified. Interestingly, while the charge-conserved D212E mutation leads to severe neonatal-onset developmental and epileptic encephalopathy (DEE), the more dramatic substitution to glycine (D212G) results in self-limited familial neonatal epilepsy (SLFNE), a much milder pathology. To elucidate the underlying mechanisms, we performed electrophysiological studies and <i>in silico</i> simulations to investigate these mutations’ biophysical and structural effects. Our findings reveal that the D212E mutation stabilizes the channel in the voltage sensor down-state and destabilizes the up-state, leading to a rightward shift in the voltage-dependent activation curve, slower activation kinetics, and accelerated deactivation kinetics. This disruption in KCNQ2 voltage sensitivity persists even in the more physiologically relevant KCNQ2/3 heterotetrameric channels. In contrast, the D212G mutation primarily destabilizes the up-state, but its impact on voltage sensitivity is significantly reduced in KCNQ2/3 heterotetrameric channels. These findings provide key insights into the biophysical and structural basis of <i>KCNQ2</i> D212 mutations and their contribution to epilepsy-related symptoms, offering a clearer understanding of how these mutations drive the varied clinical outcomes observed in patients.
DOI: 10.6084/m9.figshare.28448514.v1
title: Biophysical and structural mechanisms of epilepsy-associated mutations in the S4-S5 Linker of KCNQ2 channels

description: Mutations in <i>KCNQ2</i> are linked to various neurological disorders, including neonatal-onset epilepsy. The severity of these conditions often correlates with the mutation’s location and the biochemical properties of the altered amino acid side chains. Two mutations affecting aspartate at position 212 (D212) in the S4-S5 linker of KCNQ2 have been identified. Interestingly, while the charge-conserved D212E mutation leads to severe neonatal-onset developmental and epileptic encephalopathy (DEE), the more dramatic substitution to glycine (D212G) results in self-limited familial neonatal epilepsy (SLFNE), a much milder pathology. To elucidate the underlying mechanisms, we performed electrophysiological studies and <i>in silico</i> simulations to investigate these mutations’ biophysical and structural effects. Our findings reveal that the D212E mutation stabilizes the channel in the voltage sensor down-state and destabilizes the up-state, leading to a rightward shift in the voltage-dependent activation curve, slower activation kinetics, and accelerated deactivation kinetics. This disruption in KCNQ2 voltage sensitivity persists even in the more physiologically relevant KCNQ2/3 heterotetrameric channels. In contrast, the D212G mutation primarily destabilizes the up-state, but its impact on voltage sensitivity is significantly reduced in KCNQ2/3 heterotetrameric channels. These findings provide key insights into the biophysical and structural basis of <i>KCNQ2</i> D212 mutations and their contribution to epilepsy-related symptoms, offering a clearer understanding of how these mutations drive the varied clinical outcomes observed in patients.
DOI: 10.6084/m9.figshare.29270580.v1
title: Structural and functional mapping of ion access pathways in the human K<sup>+</sup>-dependent Na<sup>+</sup>/Ca<sup>2+</sup> exchanger NCKX2 using cysteine scanning mutagenesis, thiol-modifying reagents, and homology modelling

description: K<sup>+</sup>-dependent Na<sup>+</sup>/Ca<sup>2+</sup> exchanger proteins (NCKX) are members of the CaCA superfamily with critical roles in vision, skin pigmentation, enamel formation, and neuronal functions. Despite their importance, the structural pathways governing cation transport remain unclear. To address this, we conducted a systematic study using cysteine scanning mutagenesis of human NCKX2 combined with the thiol-modifying reagents MTSET and MTSEA to probe the accessibility and functional significance of specific residues. We used homology models of outward-facing and inward-facing NCKX2 states and molecular dynamics (MD) simulations to compare and investigate residue accessibility in human NCKX2 based on the published structures of the archaeal NCK_Mj Na<sup>+</sup>/Ca<sup>2+</sup> exchanger and the human NCX1 Na<sup>+</sup>/Ca<sup>2+</sup> exchanger. Mutant NCKX2 proteins expressed in HEK293 cells revealed diverse effects of MTSET and MTSEA on Ca<sup>2+</sup> transport. Of the 146 cysteine substitutions analyzed, 35 exhibited significant changes in Ca<sup>2+</sup> transport activity upon treatment with MTSET, with 16 showing near-complete inhibition and six demonstrating increased activity. Residues within the cation binding sites and extracellular access channels were sensitive to modification, consistent with their critical role in ion transport, whereas intracellular residues showed minimal accessibility to MTSET but were inhibited by membrane-permeable MTSEA. Water accessibility maps from MD simulations corroborated these findings, providing a high-resolution view of water-accessible pathways. This study provides a comprehensive structural and functional map of NCKX2 ion access pathways, offering insights into the molecular basis of ion selectivity and transport. These findings highlight the key residues critical for cation binding and transport, advancing our understanding of the structural dynamics of NCKX2.
DOI: 10.6084/m9.figshare.29270580
title: Structural and functional mapping of ion access pathways in the human K<sup>+</sup>-dependent Na<sup>+</sup>/Ca<sup>2+</sup> exchanger NCKX2 using cysteine scanning mutagenesis, thiol-modifying reagents, and homology modelling

description: K<sup>+</sup>-dependent Na<sup>+</sup>/Ca<sup>2+</sup> exchanger proteins (NCKX) are members of the CaCA superfamily with critical roles in vision, skin pigmentation, enamel formation, and neuronal functions. Despite their importance, the structural pathways governing cation transport remain unclear. To address this, we conducted a systematic study using cysteine scanning mutagenesis of human NCKX2 combined with the thiol-modifying reagents MTSET and MTSEA to probe the accessibility and functional significance of specific residues. We used homology models of outward-facing and inward-facing NCKX2 states and molecular dynamics (MD) simulations to compare and investigate residue accessibility in human NCKX2 based on the published structures of the archaeal NCK_Mj Na<sup>+</sup>/Ca<sup>2+</sup> exchanger and the human NCX1 Na<sup>+</sup>/Ca<sup>2+</sup> exchanger. Mutant NCKX2 proteins expressed in HEK293 cells revealed diverse effects of MTSET and MTSEA on Ca<sup>2+</sup> transport. Of the 146 cysteine substitutions analyzed, 35 exhibited significant changes in Ca<sup>2+</sup> transport activity upon treatment with MTSET, with 16 showing near-complete inhibition and six demonstrating increased activity. Residues within the cation binding sites and extracellular access channels were sensitive to modification, consistent with their critical role in ion transport, whereas intracellular residues showed minimal accessibility to MTSET but were inhibited by membrane-permeable MTSEA. Water accessibility maps from MD simulations corroborated these findings, providing a high-resolution view of water-accessible pathways. This study provides a comprehensive structural and functional map of NCKX2 ion access pathways, offering insights into the molecular basis of ion selectivity and transport. These findings highlight the key residues critical for cation binding and transport, advancing our understanding of the structural dynamics of NCKX2.
DOI: 10.6084/m9.figshare.30210024
title: Inhibition of lipolysis in visceral adipose tissue from obese mice and humans prevents impairment of endothelial Kir2.1 channels

description: Accumulation of abdominal visceral adipose tissue (VAT) is a major risk factor for cardiovascular disease. Obesity-induced endothelial dysfunction is a precursor to severe disease, and we and others have shown that arteries embedded in VAT, but not subcutaneous adipose tissue, exhibit robust endothelial dysfunction. Using a mouse model of diet-induced obesity, we recently linked VAT from obese mice to the impairment of endothelial Kir2.1, a critical regulator of endothelial function. However, the mechanism by which VAT impairs Kir2.1 is unclear. As Kir2.1 impairment is dependent on endothelial CD36, we hypothesized that lipolytic VAT induces Kir2.1 impairment through fatty acids (FA). To test this, we first treated endothelial cells with palmitic acid (PA) to determine whether the addition of exogenous FAs recapitulated our original finding of Kir2.1 dysfunction when challenged with VAT. PA inhibited Kir2.1 assessed via whole-cell patch-clamp electrophysiology, an effect that was dependent on endothelial CD36. To determine whether inhibiting VAT lipolysis prevents Kir2.1 dysfunction in the presence of VAT in obese mice and humans, VAT was pretreated with small molecule inhibitors of adipose triglyceride lipase prior to incubating endothelial cells with adipose tissue. This approach also prevented VAT-induced impairment of endothelial Kir2.1 suggesting that VAT-derived FAs may play a role. Furthermore, inhibition of lipolysis in the VAT of obese mice and humans significantly reduced endothelial FA uptake, similar to that observed when CD36 was downregulated. These findings advance our understanding of the relationship between VAT and endothelial Kir2.1 impairment and place VAT-derived FAs as potential paracrine mediators. These findings advance our understanding of the role of VAT in mediating endothelial cell dysfunction by highlighting the impact of adipose lipolysis and FAs on Kir2.1 channels in obesity. The present findings, generated from a mouse model of diet-induced obesity and adipose tissue from humans with obesity, suggest that VAT-derived FA may promote endothelial Kir2.1 dysfunction, perhaps following elevated FA uptake, as an underlying mechanism governing obesity-induced endothelial dysfunction.