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    • Stephen P Gygi
    • Stephen P Gygi

      Stephen P Gygi

      Department of Cell Biology, Harvard Medical School, Boston, MA, USA | Department of Cell Biology, Blavatnik Institute, Harvard Medical School, Boston, MA, USA | Department of ...



      KOL Resume for Stephen P Gygi


      Department of Cell Biology, Harvard Medical School, Boston, MA, USA


      Department of Cell Biology, Harvard Medical School, Boston, Massachusetts, 02115, USA

      Harvard Medical School, Boston, United States


      Department of Cell Biology, Harvard Medical School, Boston, Massachusetts.

      Harvard Medical School, Boston, Massachusetts, 02115, United States


      Department of Cell Biology, Harvard Medical School, Boston, MA 02215, USA


      Department of Cell Biology, Harvard Medical School, Boston, MA, United States of America Medicine, Kitasato University, Aomori, Japan


      the Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115, and.

      Department of Cell Biology, Harvard Medical School, 240 Longwood Ave, Boston, MA 02115, USA

      Dept. of Cell Biology, Harvard Medical School, Boston, Massachusetts, United States of America


      Department of Cell Biology, Harvard Medical School, Boston, MA 02115, United States

      Harvard Medical School, 02115, Boston, Massachusetts, USA


      University of Harvard School of Medicine Department of Cell Biology Boston MA, USA

      Harvard Medical School, Department of Cell Biology, Boston, Massachusetts 02115, United States


      †Department of Cell Biology, Harvard Medical School, Boston, MA 02115, U.S.A.

      Taplin Biological Mass Spectrometry Facility, Harvard Medical School, Boston, Massachusetts 02115, USA;

      Harvard Medical School Department of Cell Biology Boston MA USA



      Stephen P Gygi: Influence Statistics

      Sample of concepts for which Stephen P Gygi is among the top experts in the world.
      Concept World rank
      chloramphenicol g418 #1
      k1158 #1
      targeted proteomics assays #1
      fitness survival #1
      expected alterations #1
      peg10 trim32 #1
      mek inhibitors gsk1120212 #1
      spheroid culture nrf2 #1
      tomahaqcompanion #1
      vcp complexes #1
      βzfp148ko islets #1
      paradoxical mitotic exit #1
      low oncogenic risk #1
      murf1 s5a ubiquitination #1
      2ko cells mrnas #1
      fancd2 uhrf1 uhrf2 #1
      pafa proteins #1
      protein tbmp48 #1
      dj1 recessive genes #1
      allele influenza #1
      cell growth skar #1
      ms3 strategies #1
      codeine incorporation #1
      proteins prxs #1
      tbmp81 tbmp63 #1
      mixtures proteomics #1
      flux cdc42 #1
      proteins shared function #1
      apc tome1 #1
      rv2125 rv2714 #1
      fob1 tof2 #1
      palliative5 #1
      stmn1 pdgfrα #1
      saccharomyces cells humans #1
      ligandable proteins cells #1
      repressive polycomb #1
      cdk1 cdk1 activation #1
      pdcd4 ptx #1
      proteins specimen #1
      ctrl csf proteomics #1
      tbmp52 acid motifs #1
      hap1wt #1
      skar cell growth #1
      poison frog physiology #1
      fulllength nlrp1 #1
      skar cell size #1
      gcp8 #1
      oximouse #1
      tko standard #1
      4ebp1 thr37 #1


      Prominent publications by Stephen P Gygi

      KOL-Index: 18757

      Tuberous sclerosis complex (TSC) is a genetic disorder caused by mutations in either of the two tumor suppressor genes TSC1 or TSC2, which encode hamartin and tuberin, respectively. Tuberin and hamartin form a complex that inhibits signaling by the mammalian target of rapamycin (mTOR), a critical nutrient sensor and regulator of cell growth and proliferation. Phosphatidylinositol 3-kinase (PI3K) inactivates the tumor suppressor complex and enhances mTOR signaling by means of ...

      Known for Phorbol Esters | Tumor Suppressor | S6 Kinase | Phosphorylation Tuberin | Sclerosis Complex
      KOL-Index: 17690

      The conserved TREX mRNA export complex is known to contain UAP56, Aly, Tex1, and the THO complex. Here, we carried out proteomic analysis of immunopurified human TREX complex and identified the protein CIP29 as the only new component with a clear yeast relative (known as Tho1). Tho1 is known to function in mRNA export, and we provide evidence that CIP29 likewise functions in this process. Like the known TREX components, a portion of CIP29 localizes in nuclear speckle domains, and its ...

      Known for Trex Complex | Aly Uap56 | Mrna Export | Proteins Rna | New Component
      KOL-Index: 16179

      The multisubunit eukaryotic translation initiation factor (eIF) 4F recruits 40S ribosomal subunits to the 5' end of mRNA. The eIF4F subunit eIF4E interacts directly with the mRNA 5' cap structure. Assembly of the eIF4F complex is inhibited by a family of repressor polypeptides, the eIF4E-binding proteins (4E-BPs). Binding of the 4E-BPs to eIF4E is regulated by phosphorylation: Hypophosphorylated 4E-BP isoforms interact strongly with eIF4E, whereas hyperphosphorylated isoforms do not. ...

      Known for Bp1 Phosphorylation | Frap Mtor | Proteins 4e | Alcohol Acceptor | Thr37 Thr46
      KOL-Index: 15963

      TSG101 and ALIX both function in HIV budding and in vesicle formation at the multivesicular body (MVB), where they interact with other Endosomal Sorting Complex Required for Transport (ESCRT) pathway factors required for release of viruses and vesicles. Proteomic analyses revealed that ALIX and TSG101/ESCRT-I also bind a series of proteins involved in cytokinesis, including CEP55, CD2AP, ROCK1, and IQGAP1. ALIX and TSG101 concentrate at centrosomes and are then recruited to the midbodies ...

      Known for Alix Proteins | Human Escrt | Transport Endosomes | Hiv Budding | Function Cytokinesis
      KOL-Index: 15848

      It is generally assumed that a specific ubiquitin ligase (E3) links protein substrates to polyubiquitin chains containing a single type of isopeptide linkage, and that chains composed of linkages through Lys(48), but not through Lys(63), target proteins for proteasomal degradation. However, when we carried out a systematic analysis of the types of ubiquitin (Ub) chains formed by different purified E3s and Ub-conjugating enzymes (E2s), we found, using Ub mutants and mass spectrometry, ...

      Known for Ubiquitin Chains | Conjugating Enzymes | Isopeptide Linkages | Proteasomal Degradation | Mass Spectrometry
      KOL-Index: 15563

      The BRCT repeats of the breast and ovarian cancer predisposition protein BRCA1 are essential for tumor suppression. Phosphopeptide affinity proteomic analysis identified a protein, Abraxas, that directly binds the BRCA1 BRCT repeats through a phospho-Ser-X-X-Phe motif. Abraxas binds BRCA1 to the mutual exclusion of BACH1 (BRCA1-associated C-terminal helicase) and CtIP (CtBP-interacting protein), forming a third type of BRCA1 complex. Abraxas recruits the ubiquitin-interacting motif ...

      Known for Brca1 Protein | Abraxas Rap80 | Dna Damage | Complex Required | Brct Repeats
      KOL-Index: 14751

      IFN-alpha/beta plays an essential role in innate immunity against viral and bacterial infection. Among the proteins induced by IFN-alpha/beta are the ubiquitin-like ISG15 protein and its E1- (Ube1L) and E2- (UbcH8) conjugating enzymes, leading to the conjugation of ISG15 to cellular proteins. It is likely that ISG15 conjugation plays an important role in antiviral response because a human virus, influenza B virus, inhibits ISG15 conjugation. However, the biological function of ISG15 ...

      Known for Isg15 Conjugation | Diverse Cellular Pathways | Interferon Type | Enzymes Ubiquitins | Cellular Proteins
      KOL-Index: 14322

      Transcriptional silencing at the budding yeast silent mating type (HM) loci and telomeric DNA regions requires Sir2, a conserved NAD-dependent histone deacetylase, Sir3, Sir4, histones H3 and H4, and several DNA-binding proteins. Silencing at the yeast ribosomal DNA (rDNA) repeats requires a complex containing Sir2, Net1, and Cdc14. Here we show that the native Sir2/Sir4 complex is composed solely of Sir2 and Sir4 and that native Sir3 is not associated with other proteins. We further ...

      Known for Silent Chromatin | Sir2 Sir4 | Hm Loci | Silencing Proteins | Fungal Gene Saccharomyces
      KOL-Index: 14002

      The effective use of targeted therapy is highly dependent on the identification of responder patient populations. Loss of FBW7, which encodes a tumour-suppressor protein, is frequently found in various types of human cancer, including breast cancer, colon cancer and T-cell acute lymphoblastic leukaemia (T-ALL). In line with these genomic data, engineered deletion of Fbw7 in mouse T cells results in T-ALL, validating FBW7 as a T-ALL tumour suppressor. Determining the precise molecular ...

      Known for Proteins Cell | Box Protein | 3 Humans | Glycogen Synthase Kinase | Human Cancer
      KOL-Index: 13874

      Nucleotide-binding domain and leucine-rich repeat pyrin-domain containing protein 1 (NLRP1) is an inflammasome sensor that mediates the activation of caspase-1 to induce cytokine maturation and pyroptosis1–4. Gain-of-function mutations of NLRP1 cause severe inflammatory diseases of the skin4–6. NLRP1 contains a function-to-find domain that auto-proteolyses into noncovalently associated subdomains7–9, and proteasomal degradation of the repressive N-terminal fragment of NLRP1 releases its ...

      Known for Inflammasome Activation | Vbp Nlrp1 | Dpp8 Dpp9 | Dipeptidyl Peptidases | Ternary Complex
      KOL-Index: 13728

      Phosphorylation of G protein-coupled receptors (GPCRs, which are also known as seven-transmembrane spanning receptors) by GPCR kinases (GRKs) plays essential roles in the regulation of receptor function by promoting interactions of the receptors with β-arrestins. These multifunctional adaptor proteins desensitize GPCRs, by reducing receptor coupling to G proteins and facilitating receptor internalization, and mediate GPCR signaling through β-arrestin-specific pathways. Detailed mapping ...

      Known for Phosphorylation Sites | Tertiary Receptors | Adrenergic Receptor | Individual Grks | Signal Transduction
      KOL-Index: 13705

      Mutations in the RNA binding protein FUS cause amyotrophic lateral sclerosis (ALS), a fatal adult motor neuron disease. Decreased expression of SMN causes the fatal childhood motor neuron disorder spinal muscular atrophy (SMA). The SMN complex localizes in both the cytoplasm and nuclear Gems, and loss of Gems is a cellular hallmark of fibroblasts in patients with SMA. Here, we report that FUS associates with the SMN complex, mediated by U1 snRNP and by direct interactions between FUS and ...

      Known for Smn Protein | Motor Neuron Diseases | Sma Fus | Muscular Atrophy | Hela Cells
      KOL-Index: 13474

      Entry into mitosis requires the activation of cdk1/cyclin B, while mitotic exit is achieved when the same kinase activity decreases, as cyclin B is degraded. Cyclin B proteolysis is mediated by the anaphase promoting complex, or APC, an E3 ligase that is active at anaphase in mitosis through G1. We have identified a G1 substrate of the APC that we have termed Tome-1, for trigger of mitotic entry. Tome-1 is a cytosolic protein required for proper activation of cdk1/cyclin B and mitotic ...

      Known for Mitotic Entry | Cdk1 Cyclin | Tome1 Apc | Anaphase Mitosis | Protein Kinase
      KOL-Index: 13300

      RNAi-mediated heterochromatin assembly in fission yeast requires the RNA-induced transcriptional silencing (RITS) complex and a putative RNA-directed RNA polymerase (Rdp1). Here we show that Rdp1 is associated with two conserved proteins, Hrr1, an RNA helicase, and Cid12, a member of the polyA polymerase family, in a complex that has RNA-directed RNA polymerase activity (RDRC, RNA-directed RNA polymerase complex). RDRC physically interacts with RITS in a manner that requires the Dicer ...

      Known for Rnai Complexes | Fungal Rna | Rits Rdrc | Noncoding Centromeric | Proteins Cell
      KOL-Index: 13283

      PIASy is a small ubiquitin-related modifier (SUMO) ligase that modifies chromosomal proteins in mitotic Xenopus egg extracts and plays an essential role in mitotic chromosome segregation. We have isolated a novel SUMO-2/3-modified mitotic chromosomal protein and identified it as poly(ADP-ribose) polymerase 1 (PARP1). PARP1 was robustly conjugated to SUMO-2/3 on mitotic chromosomes but not on interphase chromatin. PIASy promotes SUMOylation of PARP1 both in egg extracts and in vitro ...

      Known for Mitotic Chromosomes | Sumoylation Parp1 | Sumo2 3 | Xenopus Proteins | Egg Extracts

      Key People For Mass Spectrometry

      Top KOLs in the world
      Matthias Matthias
      mass spectrometry quantitative proteomics cell culture
      Ruedi H Aebersold
      mass spectrometry protein complexes quantitative proteomics
      Richard D Smith
      mass spectrometry electrospray ionization ion mobility
      Robert Graham Graham Cooks
      mass spectrometry electrospray ionization ion trap
      John RR Yates III
      mass spectrometry gene expression proteomic analysis
      Michael Karas
      mass spectrometry laser desorption human milk

      Stephen P Gygi:Expert Impact

      Concepts for whichStephen P Gygihas direct influence:Mass spectrometry,  Gene expression,  Quantitative proteomics.

      Stephen P Gygi:KOL impact

      Concepts related to the work of other authors for whichfor which Stephen P Gygi has influence:Mass spectrometry,  Gene expression,  Dna damage,  Cell cycle,  Skeletal muscle,  Oxidative stress,  Adipose tissue.



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      Department of Cell Biology, Harvard Medical School, Boston, MA, USA | Department of Cell Biology, Blavatnik Institute, Harvard Medical School, Boston, MA, USA | Department of Biological Chemistry and Molecular Pharmacology, Blavatnik Institute, Harva

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