Bora Erdemli

Bora Erdemli

Zürich, Zürich, Schweiz
8277 Follower:innen 500+ Kontakte

Mitglied werden und folgen

Info

Bora is a principal at ZS, a global professional services firm that solves toughest…

Artikel von Bora Erdemli

Alle Artikel anzeigen

Aktivitäten

Anmelden, um alle Aktivitäten zu sehen

Berufserfahrung

  • ZS Grafik

    ZS

    Zurich, Switzerland

  • -

    Greater New York City Area

Ausbildung

Bescheinigungen und Zertifikate

Veröffentlichungen

  • The journey to making medical information a strategic asset

    Linkedin

    There’s no doubt that technology will continually support our society in the future; however, if pharma companies don’t evolve their Medical Information capabilities and teams from being operational to strategic, they will miss the vital insights needed to truly change the game.

    “Alexa, how will we access Medical Information in the next few years?"

    Andere Autor:innen
    Veröffentlichung anzeigen

  • Turning medical information into a strategic asset

    Linkedin

    how #medicalaffairs organizations have an opportunity to re-design their Medical Information capabilities to enhance patients’, physicians’ and healthcare professionals’ experiences while providing accurate and personalized information.

    Andere Autor:innen
    Veröffentlichung anzeigen

  • Beyond the Field: Evolving Field Engagement and Talent for the Future

    Medical Affairs Professionals Society

    At the MAPS EMEA 2020 Annual Meeting, 150+ delegates attended a special session that
    discussed how Field Medical engagement has evolved as a result of COVID-19. The group from
    a number of different Medical Affairs organizations also analyzed what the future of talent
    acquisition and retention is likely to look like moving forward. This report shares the key insights
    from the special session and provides further context from Medical Affairs colleagues who have
    first-hand knowledge…

    At the MAPS EMEA 2020 Annual Meeting, 150+ delegates attended a special session that
    discussed how Field Medical engagement has evolved as a result of COVID-19. The group from
    a number of different Medical Affairs organizations also analyzed what the future of talent
    acquisition and retention is likely to look like moving forward. This report shares the key insights
    from the special session and provides further context from Medical Affairs colleagues who have
    first-hand knowledge of the ever-changing Field Medical role.

    Andere Autor:innen
    Veröffentlichung anzeigen

  • Virtual engagement is hard, especially on soft skills

    The Active Ingredient - zs.com

    We finally know how to get online for virtual meetings, but do we actually know how to connect during those meetings?



    The originally planned multi-year roadmaps built by many companies to ramp up virtual engagement, ended up turning into short sprints. We now realize getting online is only the start of the journey. Even with rapid adjustments to the guidance and engagement plans, physicians’ availability and willingness to engage virtually varies globally. ZS believes virtual…

    We finally know how to get online for virtual meetings, but do we actually know how to connect during those meetings?



    The originally planned multi-year roadmaps built by many companies to ramp up virtual engagement, ended up turning into short sprints. We now realize getting online is only the start of the journey. Even with rapid adjustments to the guidance and engagement plans, physicians’ availability and willingness to engage virtually varies globally. ZS believes virtual field medical engagement will continue to increase and will perhaps grow even more in the coming months and years, which introduces another layer of uncertainty around how to effectively connect virtually.

    Andere Autor:innen
    Veröffentlichung anzeigen

  • What if medical affairs engaged its audiences like Netflix?

    The Active Ingredient - zs.com

    In this environment of rapid and constant change, our customers’ core need remains the same: access to unbiased, credible and timely scientific and clinical information. Medical affairs organizations have a unique opportunity to quickly adopt and execute across virtual channels. This will enable medical teams to drive value for their customers right now and, in the long term, it will be the foundation of a truly customer-centric digital strategy.

    Andere Autor:innen
    Veröffentlichung anzeigen

  • Predictions for the Next Era of Vaccines

    The Active Ingredient - zs.com

    From April 15-17, ZS attended the World Vaccine Congress in Washington, D.C. for the first time, where more than 1,500 leading vaccines professionals from the pharma industry, academia, government and NGOs gathered to discuss the global future of vaccines. Topics ranged from critical success factors of creating effective private-public partnerships, to deep dives on the clinical challenges behind developing a universal flu vaccine, to the innovation of using microgravity in space to support…

    From April 15-17, ZS attended the World Vaccine Congress in Washington, D.C. for the first time, where more than 1,500 leading vaccines professionals from the pharma industry, academia, government and NGOs gathered to discuss the global future of vaccines. Topics ranged from critical success factors of creating effective private-public partnerships, to deep dives on the clinical challenges behind developing a universal flu vaccine, to the innovation of using microgravity in space to support vaccine development.

    Andere Autor:innen
    Veröffentlichung anzeigen

  • The Digital Dynamic: Changing the Pharma-Physician Interaction

    PharmaExecutive

    The study was designed to determine how physicians prefer to access information from pharmaceutical companies today, what kind of interactions they have with pharma reps and how their relationships are evolving. The study also aims to understand how pharmaceutical companies can be more effective in leveraging their sales force and marketing strategy through different channels.

    Andere Autor:innen
    Veröffentlichung anzeigen

  • Targeting the Cell Wall of Mycobacterium tuberculosis: Structure and Mechanism of L, D-Transpeptidase 2

    Structure - Cell Press

    With multidrug-resistant cases of tuberculosis increasing globally, better antibiotic drugs and novel drug targets are becoming an urgent need. Traditional β-lactam antibiotics that inhibit D,D-transpeptidases are not effective against mycobacteria, in part because mycobacteria rely mostly on L,D-transpeptidases for biosynthesis and maintenance of their peptidoglycan layer. This reliance plays a major role in drug resistance and persistence of Mycobacterium tuberculosis (Mtb) infections. The…

    With multidrug-resistant cases of tuberculosis increasing globally, better antibiotic drugs and novel drug targets are becoming an urgent need. Traditional β-lactam antibiotics that inhibit D,D-transpeptidases are not effective against mycobacteria, in part because mycobacteria rely mostly on L,D-transpeptidases for biosynthesis and maintenance of their peptidoglycan layer. This reliance plays a major role in drug resistance and persistence of Mycobacterium tuberculosis (Mtb) infections. The crystal structure at 1.7 Å resolution of the Mtb L,D-transpeptidase LdtMt2 containing a bound peptidoglycan fragment, reported here, provides information about catalytic site organization as well as substrate recognition by the enzyme. Based on our structural, kinetic, and calorimetric data, we propose a catalytic mechanism for LdtMt2 in which both acyl-acceptor and acyl-donor substrates reach the catalytic site from the same, rather than different, entrances. Together, this information provides vital insights to facilitate development of drugs targeting this validated yet unexploited enzyme.

    Andere Autor:innen
    Veröffentlichung anzeigen

  • Structure, function, and mechanism of cytosolic quinone reductases

    Vitamins & Hormones

    Quinone reductases type 1 (QR1) are FAD-containing enzymes that catalyze the reduction of many quinones, including menadione (Vit K3), to hydroquinones using reducing equivalents provided by NAD(P)H. The reaction proceeds with a ping-pong mechanism in which the NAD(P)H and the substrate occupy alternatively overlapping regions of the same binding site and participate in a double hydride transfer: one from NAD(P)H to the FAD of the enzyme, and one from the FADH(2) of the enzyme to the quinone…

    Quinone reductases type 1 (QR1) are FAD-containing enzymes that catalyze the reduction of many quinones, including menadione (Vit K3), to hydroquinones using reducing equivalents provided by NAD(P)H. The reaction proceeds with a ping-pong mechanism in which the NAD(P)H and the substrate occupy alternatively overlapping regions of the same binding site and participate in a double hydride transfer: one from NAD(P)H to the FAD of the enzyme, and one from the FADH(2) of the enzyme to the quinone substrate. The main function of QR1 is probably the detoxification of dietary quinones but it may also contribute to the reduction of vitamin K for its involvement in blood coagulation. In addition, the same reaction that QR1 uses in the detoxification of quinones, activates some compounds making them cytotoxic. Since QR1 is elevated in many tumors, this property has encouraged the development of chemotherapeutic compounds that become cytotoxic after reduction by QR1. The structures of QR1 alone, and in complexes with substrates, inhibitors, and chemotherapeutic prodrugs, combined with biochemical and mechanistic studies have provided invaluable insight into the mechanism of the enzyme as well as suggestions for the improvements of the chemotherapeutic prodrugs. Similar information is beginning to accumulate about another related enzyme, QR2.

    Andere Autor:innen
    Veröffentlichung anzeigen

  • Restricted mobility of conserved residues in protein-protein interfaces in molecular simulations

    Biophysical Journal

    Conserved residues in protein-protein interfaces correlate with residue hot-spots. To obtain insight into their roles, we have studied their mobility. We have performed 39 explicit solvent simulations of 15 complexes and their monomers, with the interfaces varying in size, shape, and function. The dynamic behavior of conserved residues in unbound monomers illustrates significantly lower flexibility as compared to their environment, suggesting that already before binding they are constrained in…

    Conserved residues in protein-protein interfaces correlate with residue hot-spots. To obtain insight into their roles, we have studied their mobility. We have performed 39 explicit solvent simulations of 15 complexes and their monomers, with the interfaces varying in size, shape, and function. The dynamic behavior of conserved residues in unbound monomers illustrates significantly lower flexibility as compared to their environment, suggesting that already before binding they are constrained in a boundlike configuration. To understand this behavior, we have analyzed the inter- and intrachain hydrogen-bond residence-time in the interfaces. We find that conserved residues are not involved significantly in hydrogen bonds across the interface as compared to nonconserved. However, the monomer simulations reveal that conserved residues contribute dominantly to hydrogen-bond formation before binding. Packing of conserved residues across the trajectories is significantly higher before and after the binding, rationalizing their lower mobility. Backbone torsional angle distributions show that conserved residues assume restricted regions of space and the most visited conformations in the bound and unbound trajectories are similar, suggesting that conserved residues are preorganized. Combined with previous studies, we conclude that conserved residues, hot spots, anchor, and interface-buried residues may be similar residues, fulfilling similar roles.

    Andere Autor:innen
    Veröffentlichung anzeigen
Mitglied werden, um alle Veröffentlichungen anzuzeigen

Weitere Aktivitäten von Bora Erdemli

Bora Erdemlis vollständiges Profil ansehen

  • Herausfinden, welche gemeinsamen Kontakte Sie haben
  • Sich vorstellen lassen
  • Bora Erdemli direkt kontaktieren
Mitglied werden. um das vollständige Profil zu sehen

Weitere ähnliche Profile

Weitere Beiträge entdecken

Weitere Mitglieder, die Bora Erdemli heißen

Es gibt auf LinkedIn 1 weitere Person, die Bora Erdemli heißt.

Weitere Mitglieder anzeigen, die Bora Erdemli heißen

Entwickeln Sie mit diesen Kursen neue Kenntnisse und Fähigkeiten

Alle Kurse anzeigen