• Cell Death
    • Guido Kroemer
    • Guido Kroemer: Influence Statistics

      Guido Kroemer

      Guido Kroemer

      Show email address

      Equipe Labellisée Par La Ligue Contre Le Cancer, Université de Paris, Sorbonne Université, INSERM UMR1138, Centre de Recherche des Cordeliers, Paris, France | Pôle de ...

      Is this your profile? manage_accounts Claim your profile content_copy Copy URL code Embed Link to your profile

      Guido Kroemer:Expert Impact

      Concepts for whichGuido Kroemerhas direct influence:Cell death,Cancer cells,Immunogenic cell death,Trial watch,Tumor cells,Cystic fibrosis,Cancer therapy.

      Guido Kroemer:KOL impact

      Concepts related to the work of other authors for whichfor which Guido Kroemer has influence:Cell death,Oxidative stress,Breast cancer,Mitochondrial dysfunction,Gene expression,Tumor microenvironment,Dna damage.

      KOL Resume for Guido Kroemer


      Equipe Labellisée Par La Ligue Contre Le Cancer, Université de Paris, Sorbonne Université, INSERM UMR1138, Centre de Recherche des Cordeliers, Paris, France

      Karolinska Institutet, Department of Women's and Children's Health, Karolinska University Hospital, Stockholm, Sweden

      Metabolomics and Cell Biology Platforms, Institut Gustave Roussy, Villejuif,

      Suzhou Institute for Systems Medicine, Chinese Academy of Medical Sciences, Suzhou 215163, China

      Department of Pathology, Dalhousie University, Halifax, NS B3H 1V8, Canada

      Sign-in to see all concepts, it's free!
      Sample of concepts for which Guido Kroemer is among the top experts in the world.
      Concept World rank
      unwarranted cell death #1
      kpc cells mice #1
      chchd4 aif #1
      apoptosis aza #1
      effects teta #1
      nuclear dna loss #1
      hct116rev2 #1
      nfkappab inhibition #1
      diploid counterparts #1
      resveratrol aspirin #1
      cell death signals #1
      p53 tetraploid cells #1
      ptpc ptpc opening #1
      humans immunogenic #1
      metabolic diseases ferritinophagy #1
      comprehensive glossary #1
      lps lps ru38486 #1
      caloric restriction mimetics #1
      alterations early pcd #1
      protein vmia #1
      70 antagonizes #1
      cddp cisplatin #1
      mtx atg4b mice #1
      trasformare #1
      early irreversible step #1
      lps ru38486 lps #1
      chchd4 haploinsufficiency #1
      thiol oxidation status #1
      hct116s #1
      catastrophe mitotic #1
      redaporfin tumor cells #1
      mmp csa #1
      apoptosis lnd #1
      “silent #1
      trial watch mabs #1
      ant bax #1
      igf type ppp #1
      acbp acbp dbi #1
      mlkl dfna5 #1
      aurka ripk1 #1
      ep300 aspirin #1
      icd trial watch #1
      ant baxbh3 #1
      ca9 panc1 #1
      reversine response #1
      hiv‐1 protein vpr #1
      acbp dbi #1
      aif cell death #1
      elusive hunger factor #1
      employing cytokines #1
      Sign-in to see all concepts, it's free!

      Prominent publications by Guido Kroemer

      KOL-Index: 18511

      The anti-apoptotic transcription factor nuclear factor-κB (NF-κB) is constitutively activated in CD34+ myeloblasts from high-risk myelodysplastic syndrome (MDS) and acute myeloid leukemia (AML) patients. Inhibition of NF-κB by suppressing the canonical NF-κB activation pathway, for instance by knockdown of the three subunits of the inhibitor of NF-κB (IκB) kinase (IKK) complex (IKK1, IKK2 and NEMO) triggers apoptosis in such cells. Here, we show that an MDS/AML model cell line exhibits a ...

      Known for Myeloid Leukemia | Atm Nemo | Κb Activation | Tumor Cells | Proteins Cell
      KOL-Index: 16380

      Caspase-independent programmed cell death can exhibit either an apoptosis-like or a necrosis-like morphology. The ABL kinase inhibitor, imatinib mesylate, has been reported to induce apoptosis of BCR-ABL-positive cells in a caspase-dependent fashion. We investigated whether caspases alone were the mediators of imatinib mesylate-induced cell death. In contrast to previous reports, we found that a broad caspase inhibitor, zVAD-fmk, failed to prevent the death of imatinib mesylate-treated ...

      Known for Imatinib Mesylate | Cell Death | Serine Protease | Myelogenous Chronic | Apoptosis Necrosis
      KOL-Index: 14933

      Following the screening of a battery of distinct small-interfering RNAs that target various components of the apoptotic machinery, we found that knockdown of the voltage-dependent anion channel 1 (VDAC1) was particularly efficient in preventing cell death induced by cisplatin (CDDP) in non-small cell lung cancer cells. Both the downregulation of VDAC1 and its chemical inhibition with 4,4′-diisothiocyanatostilbene-2,2′-disulfonic acid reduced the apoptosis-associated modifications induced ...

      Known for Cell Death | Vdac1 Bax | Cddp Induced | Bcl2 Protein | Apoptotic Machinery
      KOL-Index: 14732

      Erlotinib and gefitinib, two inhibitors of the epidermal growth factor receptor (EGFR), can stimulate apoptosis and differentiation of myeloid cell lines that lack EGFR, unveiling a novel, therapeutically exploitable off-target effect of tyrosine kinase inhibitors. Here, we performed a side-by-side comparison of erlotinib and gefitinib effects on a broad spectrum of malignant myeloid cell lines, as well as on primary myeloblasts freshly purified from the bone marrow of patients with ...

      Known for Erlotinib Gefitinib | Acute Myeloid Leukemia | Myelodysplastic Syndrome | Mds Aml | Differentiation Cell
      KOL-Index: 14500

      The molecular mechanisms responsible for the evolution from the preleukemic entities of low-risk myelodysplastic syndrome (MDS) to the less favorable forms of high-risk MDS, as well as those enabling transformation to acute myeloid leukemia (AML), are still incompletely understood. Abundant evidence from solid tumors demonstrates that preneoplastic lesions activate signaling pathways of a DNA damage response (DDR), which functions as an ‘anticancer barrier’ hindering tumorigenesis. ...

      Known for Myeloid Leukemia | Dna Damage Response | Mds Aml | Myelodysplastic Syndrome | Proteins Cell
      KOL-Index: 14484

      Anucleate cells can be induced to undergo programmed cell death (PCD), indicating the existence of a cytoplasmic PCD pathway that functions independently from the nucleus. Cytoplasmic structures including mitochondria have been shown to participate in the control of apoptotic nuclear disintegration. Before cells exhibit common signs of nuclear apoptosis (chromatin condensation and endonuclease-mediated DNA fragmentation), they undergo a reduction of the mitochondrial transmembrane ...

      Known for Nuclear Apoptosis | Mitochondrial Control | Chromatin Condensation | Pharmacological Agents | Protooncogene Proteins
      KOL-Index: 14304

      One critical step of the apoptotic process is the opening of the mitochondrial permeability transition (PT) pore leading to the disruption of mitochondrial membrane integrity and to the dissipation of the inner transmembrane proton gradient (Delta Psim). The mitochondrial PT pore is a polyprotein structure which is inhibited by the apoptosis-inhibitory oncoprotein Bcl-2 and which is closely associated with the mitochondrial benzodiazepine receptor (mBzR). Here we show that PK11195, a ...

      Known for Benzodiazepine Receptor | Apoptosis Induction | Delta Psim | Mbzr Pk11195 | Chemotherapeutic Agents
      KOL-Index: 14274

      The anti-apoptotic proteins Bcl-2 and Bcl-X(L) bind and inhibit Beclin-1, an essential mediator of autophagy. Here, we demonstrate that this interaction involves a BH3 domain within Beclin-1 (residues 114-123). The physical interaction between Beclin-1 and Bcl-X(L) is lost when the BH3 domain of Beclin-1 or the BH3 receptor domain of Bcl-X(L) is mutated. Mutation of the BH3 domain of Beclin-1 or of the BH3 receptor domain of Bcl-X(L) abolishes the Bcl-X(L)-mediated inhibition of ...

      Known for Autophagy Beclin1 | Bh3 Domain | Physical Interaction | Bcl2 Bclxl | Western Cells
      KOL-Index: 14184

      High-risk myelodysplastic syndrome (MDS) and acute myeloid leukemia (AML) are characterized by the activation of the anti-apoptotic transcription factor NFκB, via the IKK complex. Here, we show that constitutive activation of the receptor tyrosine kinase Flt3 is responsible for IKK activation. Chemical inhibition or knockdown of Flt3 with small interfering RNAs reduced NFκB activation in MDS and AML cell lines, as well as in primary CD34+ bone marrow cells from patients, causing ...

      Known for Acute Myeloid Leukemia | Nfκb Activation | Flt3 Inhibition | Mds Aml | Myeloid Tyrosine Kinase
      KOL-Index: 13997

      An increasing number of experimental chemotherapeutic agents induce apoptosis by directly triggering mitochondrial membrane permeabilization (MMP). Here we examined MMP induced by lonidamine, arsenite, and the retinoid derivative CD437. Cells overexpressing the cytomegalovirus-encoded protein vMIA, a protein which interacts with the adenine nucleotide translocator, were strongly protected against the MMP-inducing and apoptogenic effects of lonidamine, arsenite, and CD437. In a cell-free ...

      Known for Mitochondrial Membrane | Lonidamine Cd437 | Adenine Nucleotide | Inhibition Glycolysis | Induced Cell
      KOL-Index: 13818

      BACKGROUND & AIMS: Induction of nonapoptotic cell death could be an approach to eliminate apoptosis-resistant tumors. We investigated necroptosis-based therapies in mouse models of pancreatic ductal adenocarcinoma cancer (PDAC).

      METHODS: We screened 273 commercially available kinase inhibitors for cytotoxicity against a human PDAC cell line (PANC1). We evaluated the ability of the aurora kinase inhibitor CCT137690 to stimulate necroptosis in PDAC cell lines (PANC1, PANC2.03, CFPAC1, ...

      Known for Aurora Kinase | Pdac Cells | Nude Mice | Ripk3 Mlkl | Pancreatic Cancer
      KOL-Index: 13632

      Apoptosis in response to cellular stress such as treatment with cytotoxic drugs is mediated by effector caspases (caspase-3) which can be activated by different initiator pathways. Here, we report on a cell type specific triggering of death receptor and/or mitochondrial pathways upon drug treatment. In type I cells (BJAB), both the receptor and the mitochondrial pathway were activated upon drug treatment, since blockade of either the receptor pathway by overexpression of dominant ...

      Known for Death Receptor | Mitochondrial Pathway | Type Cells | Induced Apoptosis | Cytotoxic Drugs
      KOL-Index: 13382

      Caspase-independent death mechanisms have been shown to execute apoptosis in many types of neuronal injury. P53 has been identified as a key regulator of neuronal cell death after acute injury such as DNA damage, ischemia, and excitotoxicity. Here, we demonstrate that p53 can induce neuronal cell death via a caspase-mediated process activated by apoptotic activating factor-1 (Apaf1) and via a delayed onset caspase-independent mechanism. In contrast to wild-type cells, Apaf1-deficient ...

      Known for Neuronal Cell Death | Inducing Factor | Survival Cells | Caspase Independent | Dna Damage
      KOL-Index: 13252

      Bcl-2 family protein including anti-apoptotic (Bcl-2) or pro-apoptotic (Bax) members can form ion channels when incorporated into synthetic lipid bilayers. This contrasts with the observation that Bcl-2 stabilizes the mitochondrial membrane barrier function and inhibits the permeability transition pore complex (PTPC). Here we provide experimental data which may explain this apparent paradox. Bax and adenine nucleotide translocator (ANT), the most abundant inner mitochondrial membrane ...

      Known for Bcl2 Bax | Channel Activity | Rats Rats | Nucleotide Translocator | Ant Ptpc

      Key People For Cell Death

      Top KOLs in the world
      Guido Kroemer
      cell death trial watch cystic fibrosis
      Douglas R Green
      cell death dna fragmentation caspase activation
      Jun‐Ying Yuan
      cell death rip1 kinase ripk1 activation
      John C Reed
      cell death proteins bcl2 apoptosis protein
      cell death tumor necrosis factor protein kinase
      Stanley J Korsmeyer
      cell death proteins bcl2 proto oncogene

      Equipe Labellisée Par La Ligue Contre Le Cancer, Université de Paris, Sorbonne Université, INSERM UMR1138, Centre de Recherche des Cordeliers, Paris, France | Pôle de Biologie, Hôpital Européen Georges Pompidou, Paris, France. | Metabolomics and Cell

    Download on the App StoreGet it on Google Play

    Copyright © 2023 Key Opinion Leaders, LLC.