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Protecting Revenue With Safety Nets For Timely Filing Epic go-lives and other EHR transitions can be chaotic, high-stakes operations that push revenue cycle teams to the limit. When claim work queues go unattended—even for a few weeks—organizations can lose millions in timely filing denials. On this episode Stuart Newsome, VP of Marketing at Infinx, welcomes Tadd Miller, AR Manager at Ni2, an Infinx company, to share how his team averted disaster during a major Epic implementation by developing practical, real-world safety nets. Find all of our network podcasts on your favorite podcast platforms and be sure to subscribe and like us. Learn more at www.healthcarenowradio.com/listen/
Unlock the power of actionable data in revenue cycle management. Jason Adams, President of Ni2, an Infinx company, shares how AI-driven analytics, customized dashboards, and expert-driven clinical appeals can transform financial performance, enhance transparency, and ensure claims get paid.
In this episode of RCM Insights, we explore how GenAI Agents and automation are transforming prior authorization. Jason Adams, President of Ni2, and Navaneeth Nair, Chief Product Officer at Infinx, reveal how providers can use technology to stay ahead as payers scale AI-driven processes.
Talon Metals Vice President of Geology Etienne Dinel joined Steve Darling from Proactive to share news about a new discovery made by the company's drill teams. In a previously unexplored part of the Tamarack Intrusive Complex, Talon Metals has encountered a new area of semi-massive nickel sulphide. This discovery occurred at a shallow depth of approximately 296.3 meters within the newly named "Raptor Zone," situated between the Raptor's Head Area and the Raptor's Crest Area. Dinel informed Proactive that this newly identified zone contains high-grade massive nickel mineralization. Specifically, grades of up to 9.33% Ni1 and 9.95% Ni2 have been encountered in this area. Remarkably, the 1.5-kilometer distance between these mineralized zones had never been previously drilled, making this discovery all the more significant. The discovery of the Raptor Zone expands Talon Metals' understanding of the mineral potential within the Tamarack Intrusive Complex. The presence of high-grade nickel mineralization in this unexplored area highlights the exploration upside and the ongoing potential for further resource expansion. Talon Metals' commitment to advancing its exploration efforts and uncovering new mineralized zones demonstrates the company's dedication to maximizing the value of its assets. The Raptor Zone represents a significant addition to Talon Metals' exploration portfolio and contributes to the company's ongoing success in the nickel mining sector #proactiveinvestors #talonmetalscorp #tsx #tlo #otc #tloff #mining #nickel #copper #NickelMineralization #RaptorZoneDiscovery #GeologyNews #MiningIndustry #ExplorationUpdate #ResourceDrilling #MassiveSulfide #NetTexturedSulfides #MineralizationFind #GeologicalResearch #MineralExploration #ShallowDeposits #HighGradeMineralization #StepOutDrilling #DownholeElectromagneticSurvey #MineralizationGrowth #MineralizationPotential #GeologicalDiscoveries #ExcitingNews #MineralExplorationUpdate #GeologicalBreakthrough #ResourceExpansion #MineralizationPatterns #GeologicalSurveys #MineralDepositMapping#invest #investing #investment #investor #stockmarket #stocks #stock #stockmarketnews
In today's episode, Jeff Bond and William Smith host a conversation with Ken Ballou, Director, US Banking and Financial Services at Sensedia, an emerging technology company delivering API solutions for companies adopting a more digital, connected, and open strategy. This conversation was hosted at the TAG FinTech South 2022 Conference at the Georgia World Congress Center. Ken Bellou talks with Jeff and William about how technology has enabled smaller companies to compete with the bigger players, the importance of conscious leaders to contribute through capitalism to elevate humanity, and what he sees as the future of Fintech. More About Ken Ballou Ken Ballou is a senior technology executive and entrepreneur. His success in the software industry reflects a specialization in driving international business growth and market development. Throughout his career, Ken has successfully developed numbers of productive business relationships with a diverse array of global enterprises, including prominent banking and financial services firms and industry-leading technology corporations. Ken recently joined Sensedia, an emerging global leader providing Open API technology key in supporting a range of digital banking initiatives such as Banking as a Service (Baas) and Open Banking. His responsibilities include the development of business relationships with some of the most progressive and influential banking and financial services firms in the United States. Ken has previously held a number of entrepreneurial and business leadership positions in companies ranging from Computer Associates and HP Software, to Ni2, Camunda, Alfresco Software, Palantir, and Mobixell Networks. In 2004 Ken also co-founded an LLC named NewEnding, a business development and advisory services firm offering growth strategy and management guidance to organizations ranging from early stage to Fortune 500. RESOURCES RELATED TO THIS EPISODE Follow Ken on LinkedIn Visit https://www.sensedia.com/ CREDITS Theme Music
Fakultät für Biologie - Digitale Hochschulschriften der LMU - Teil 01/06
Das σ54-abhängige Regulatorprotein FhlA aktiviert die Transkription der für die Bildung eines funktionellen Formiat-Hydrogen-Lyase-Komplexes nötigen Gene. Hierfür weist es eine Reihe von Aktivitäten auf, nämlich ATP-Hydrolyse, Interaktion mit Eσ54 und Stimulierung der Transkription. Die Aktivität von FhlA wird durch Bindung von Formiat und von spezifischen DNA-Sequenzen (UAS) stimuliert und durch HycA negativ beeinflußt. Sequenzähnlichkeiten von FhlA zu anderen Transkriptionsaktivatoren lassen auf einen Aufbau aus drei Domänen schließen. Die in der vorliegenden Arbeit erfolgte Struktur- Funktions-Analyse lieferte wichtige Ergebnisse über die Domänenstruktur und den Wirkungsmechanismus von FhlA. In vivo- und in vitro-Analysen der C-terminalen Hälfte von FhlA (FhlA-C, Aminosäuren 379 bis 693 von FhlA), welche die Domänen B, C und D von FhlA umfaßt, zeigten, daß dieser Teil von FhlA sämtliche für die Transkriptionsaktivierung und ATP-Hydrolyse benötigten Bereiche enthält. Beide Aktivitäten von FhlA-C sind konstitutiv, bedürfen also nicht mehr der Aktivierung durch Formiat-Bindung. Durch die Bindung von DNA konnte die Aktivität von FhlA-C jedoch gesteigert werden, wobei bei spezifischer DNA ein stärkerer Effekt als bei unspezifischer zu beobachten war. Aus den Ergebnissen wurde ein Modell abgeleitet, in welchem die N-terminale Domäne von FhlA im nicht-induzierten Zustand einen hemmenden Einfluß auf die Aktivität des restlichen Proteins hat. Formiat-Bindung an die N-terminale Domäne hebt diese Hemmung auf und bewirkt eine Steigerung der Aktivität von FhlA durch Erhöhung der Affinität für ATP. Auch die HycA-Suszeptibilität konnte der N-terminalen Domäne zugeordnet werden. Darüberhinaus besitzt die N-terminale Domäne eine strukturelle Funktion, da sie für die Oligomerisierung von FhlA verantwortlich ist. Es konnte gezeigt werden, daß die Bindung von ATP an FhlA eine Änderung der Konformation oder des Oligomerisierungszustandes des Proteins zur Folge hat. Eine Studie zur Verbreitung des FhlA-Regulationssystems ergab, daß in mehreren Spezies der Familie Enterobacteriaceae sowohl ein zu FhlA orthologes Protein als auch Homologe zu hyc- oder hyp-Genen existieren. Die Sequenz von fhlA aus S. typhimurium, E. aerogenes und K. oxytoca wurde bestimmt. Sie zeigt über die gesamte Länge große Ähnlichkeit zu FhlA von E. coli, wobei der Grad der Identität der Gene und Proteine den phylogenetischen Verwandtschaftsverhältnissen entspricht. Die FhlA-Orthologe aus E. aerogenes und K. oxytoca können FhlA aus E. coli funktionell ersetzen und zeigen auch in ihrer Aktivität hinsichtlich der Stimulierbarkeit durch Formiat und Anaerobiose große Übereinstimmung. Desweiteren beeinflußt auch HycA von E. coli die Aktivität der orthologen Proteine, was wiederum die nahe Verwandtschaft der Regulationssysteme zeigt. Im Hauptteil dieser Arbeit konnte der Beweis erbracht werden, daß das HydH/G-Zwei- Komponenten-System die Expression von zraP aktiviert, einem stromaufwärts von hydH gelegenen, in divergierender Richtung orientierten Gen. Für gereinigtes HydG wurde durch Gelretardationsexperimente und DNase I Footprinting-Analyse eine Bindestelle identifiziert, die im intergenen Bereich zwischen hydHG und zraP liegt. Diese 55 bp lange Region umfaßt zwei jeweils 17 bp lange Bereiche mit der Sequenz GAGTAAAAATGACTCGC, die als inverted repeat angeordnet sind. Diese Bindestelle wirkt als UAS in beide Richtungen. Als auslösender Stimulus für die Expressionsaktivierung von zraP durch HydH/G konnte eine Zn2+-Konzentration im Medium von mehr als 0,5 mM identifiziert werden. Pb2+ war zu einem gewissen Grad in der Lage, Zn2+ in der Funktion als Induktor zu ersetzen, jedoch erfolgte keine Aktivierung durch Ni2+, Co2+, Mn2+, Fe2+, Mg2+, Cu2+, Cd2+ oder Hg2+. Gleichzeitig ist HydH/G einer positiven Autoregulation unterworfen, die durch die gleichen Metalle induziert wird. Sowohl für die durch HydH/G induzierte Expression von zraP als auch von hydHG konnte eine Abhängigkeit von σ54 gezeigt werden. Der Einfluß von HydH/G auf die Regulation der Gene für die Hydrogenase 3 tritt entgegen früherer Postulate nur bei Überproduktion des Regulators auf und ist auf "cross-talk" zurückzuführen. Zweidimensionale Gelelektrophorese erbrachte Hinweise auf weitere durch HydG in ihrer zellulären Konzentration beeinflußte Proteine. Obwohl zraP im Zusammenhang mit Zink- Toleranz identifiziert worden war, zeigten die Ergebnisse keinen Einfluß von HydH/G oder ZraP auf die Zink-Toleranz der Zellen.
The solubility of Ni in a silicate melt has been measured using a new, mechanically assisted equilibration technique over a wide range of controlled ƒO2 values. The melt composition corresponds to the 1 atm eutectic in the system CaAl2Si2O8-CaMgSi2O6 + 10 wt% CaO. The experiments were performed at 1300°C and over an ƒO2 range of 10−8.5 to 10−13.75, and over a temperature range of 1270 to 1390°C at a constant gas mixing ratio ( ). The experiment consists of a sample of melt contained within a crucible of Ni metal and held in a 1 atm gas mixing furnace. A Ni spindle is entered into the sample from above and continuously rotated at a constant angular velocity using a viscometer head. The stirring of the sample serves to accelerate the approach to equilibrium between the liquid sample and the metal crucible (and spindle). This arrangement allows relatively rapid equilibration of Ni content following changes to higher or lower ƒO2 values. Samples of the melt may be taken at any time for analysis and thus the equilibrium solubility of Ni in the silicate melt may be determined from unambiguous experimental reversals. The Ni contents of samples, analysed both by INAA and by ICP-AES, range from 25 to 5300 ppm. The data presented in this paper indicate that the oxidation state of Ni in the investigated melt is Ni2+ over the entire range of ƒO2 investigated. This conclusion contrasts with recent reports in the literature of an inflection in the ƒO2 dependence of Ni solubility, which has been interpreted as solution of neutral Ni at low ƒO2 (Morse et al., 1991; Colson, 1992; Ehlers et al., 1992). We also present data for the temperature dependence of Ni solubility in the investigated melt. The solubility decreases with increasing temperature at constant ƒO2. The present results are in good agreement with the metal-loop-equilibration experiments reported by Holzheid et al. (1994).
A novel prokaryotic expression vector pGEX-6T was designed for high-level expression of recombinant fusion protein with a histidine-hexapeptide and glutathione-S-transferase at its N-terminus and the recombinant human preproinsulin at its C-terminus. Efficiency of expression was investigated in the Escherichia coli strain CAG456. The synthesized protein was sequestered in an insoluble form in inclusion bodies and was purified to homogeneity by one-step affinity chromatography based on the specific complex formation of the histidine-hexapeptide and a chelating matrix which was charged with Ni2+ ions. The antigenic nature of the purified recombinant preproinsulin fusion protein was evaluated by ELISA screening for insulin autoantibodies in selected sera from patients with recent-onset type 1 (insulin-dependent) diabetes mellitus classified by the existence of additional autoantibodies reactive against glutamic acid decarboxylase. 14% of the tested sera (n=43) conttained insulin autoantibodies which strongly recognized the recombinant human preproinsulin. Comparable measurements with both recombinant human preproinsulin and mature insulin suggested that the observed autoantigenicity of preproinsulin was mediated by the C-peptide or/and signal peptide.
The molecular events underlying the inhibition of exocytosis by tetanus toxin were investigated in permeabilized adrenal chromaffin cells. We found that replacement of amino acid residues within the putative zinc binding domain of the tetanus toxin light chain such as of histidine (position 233) by cysteine or valine, or of glutamate (position 234) by glutamine completely abolished the effect of the light chains on Ca2+ induced catecholamine release. Dipicolinic acid, a strong chelating agent for zinc, also prevented the effect of the tetanus toxin light chain. Zn2+ and, less potently Cu2+ and Ni2+, but not Cd2+ and Co2+, restored the activity of the neurotoxin. These data show that zinc and the putative zinc binding domain constitute the active site of the tetanus toxin light chain. Neither captopril, an inhibitor of synaptobrevin cleavage nor peptides spanning the site of synaptobrevins cleaved by the tetanus toxin in neurons, prevented the inhibition of Ca2+ induced catecholamine release by the tetanus toxin light chain. This suggests that synaptobrevins are not a major target of tetanus toxin in adrenal chromaffin cells.