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Research.com Recognitions

  • 2019 - Fellow, National Academy of Inventors

Overview

Michael Blaber is a researcher affiliated with Florida State University in the United States. Their work spans multiple fields within biochemistry, genetics, molecular biology, and materials science. The research focus notably covers molecular biology and materials chemistry as principal subfields.

The scientist's research topics include:

  • Enzyme Structure and Function
  • Protein Structure and Dynamics
  • Porphyrin Metabolism and Disorders
  • Botanical Research and Chemistry
  • Biochemical and Structural Characterization
  • Corneal Surgery and Treatments
  • Proteoglycans and glycosaminoglycans research

Frequent publication venues for Michael Blaber's work are:

  • Protein Science
  • Frontiers in Molecular Biosciences
  • Journal of Proteins and Proteomics
  • Growth Factors

Notable recent papers authored or co-authored by Michael Blaber include:

  • "Ab initio folding of a trefoil-fold motif reveals structural similarity with a β-propeller blade motif," 2020, Protein Science
  • "Regenerative responses of rabbit corneal endothelial cells to stimulation by fibroblast growth factor 1 (FGF1) derivatives, TTHX1001 and TTHX1114," 2021, Growth Factors
  • "Conserved buried water molecules enable the β-trefoil architecture," 2020, Protein Science
  • "A bell-shaped dose-response of topical FGF-1 in accelerating dermal wound healing in aged female BALB/cByJ mice," 2020, Journal of Proteins and Proteomics
  • "The ubiquitous buried water in the beta-trefoil architecture contributes to the folding nucleus and ~20% of the folding enthalpy," 2021, Protein Science

Michael Blaber often collaborates with a network of co-authors, including:

  • Connie A. Tenorio
  • Joseph B. Parker
  • Jessica Weant
  • David Eveleth
  • Amuthakannan Subramaniam

In recognition of professional contributions, Michael Blaber was named a Fellow of the National Academy of Inventors in 2019.

Best Publications

  • Response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect.

    A. E. Eriksson;W. A. Baase;X. J. Zhang;D. W. Heinz

  • Structural basis of amino acid alpha helix propensity.

    Michael Blaber;Xue Jun Zhang;Brian W. Matthews

  • Cloning and Expression of the Gene for Pro-urokinase in Escherichia coli

    William E. Holmes;Diane Pennica;Mike Blaber;Michael W. Rey

  • Activation of plasminogen by pro-urokinase. I. Mechanism.

    H R Lijnen;C Zamarron;M Blaber;M E Winkler

  • Proteinase-activated receptors, targets for kallikrein signaling.

    Katerina Oikonomopoulou;Kristina K. Hansen;Mahmoud Saifeddine;Illa Tea

  • Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme.

    Michael Blaber;Xue-jun Zhang;Joel D. Lindstrom;Sheila D. Pepiot

  • X-RAY CRYSTAL STRUCTURE OF HUMAN ACIDIC FIBROBLAST GROWTH FACTOR

    Michael Blaber;Jerry DiSalvo;Kenneth A. Thomas

  • Crystal Structure and Biochemical Characterization of Human Kallikrein 6 Reveals That a Trypsin-like Kallikrein Is Expressed in the Central Nervous System

    Matthew J. Bernett;Sachiko I. Blaber;Isobel A. Scarisbrick;Pushparani Dhanarajan

  • Activation Profiles and Regulatory Cascades of the Human Kallikrein-related Peptidases

    Hyesook Yoon;Gurunathan Laxmikanthan;Jihun Lee;Sachiko I. Blaber

  • A comprehensive nomenclature for serine proteases with homology to tissue kallikreins

    Åke Lundwall;Vimla Band;Michael Blaber;Judith A. Clements

  • Disordered water within a hydrophobic protein cavity visualized by x-ray crystallography

    B. Yu;M. Blaber;A. M. Gronenborn;G. M. Clore

  • Structure and function of 1-tetrahydrocannabinolic acid (THCA) synthase, the enzyme controlling the psychoactivity of Cannabis sativa

    Yoshinari Shoyama;Taro Tamada;Kazuo Kurihara;Ayako Takeuchi

  • Activity of a newly identified serine protease in CNS demyelination.

    Isobel A. Scarisbrick;S. I. Blaber;C. F. Lucchinetti;C. P. Genain

  • Kallikrein-mediated cell signalling: targeting proteinase-activated receptors (PARs).

    Katerina Oikonomopoulou;Kristina K. Hansen;Mahmoud Saifeddine;Nathalie Vergnolle

  • Experimental support for the evolution of symmetric protein architecture from a simple peptide motif.

    Jihun Lee;Michael Blaber

  • Biological and thrombolytic properties of proenzyme and active forms of human urokinase--III. Thrombolytic properties of natural and recombinant urokinase in rabbits with experimental jugular vein thrombosis.

    Desire Collen;Jean-Marie Stassen;M Blaber;M Winkler

  • The protease inhibitory properties of the Alzheimer's beta-amyloid precursor protein.

    S Sinha;H F Dovey;P Seubert;P J Ward

  • Targeting kallikrein 6-proteolysis attenuates CNS inflammatory disease

    Sachiko I. Blaber;Bogoljub Ciric;George P. Christophi;Matthew J. Bernett

  • Energetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozyme.

    Michael Blaber;Joel D. Lindstrom;Nadine Gassner;Jian Xu

  • Substrate Specificity of Human Kallikrein 6 SALT AND GLYCOSAMINOGLYCAN ACTIVATION EFFECTS

    Pedro Francisco Angelo;Aurelio Resende Lima;Fabiana M. Alves;Sachiko I. Blaber

Frequent Co-Authors

Maria A. Juliano
Maria A. Juliano Federal University of Sao Paulo
Ralph A. Bradshaw
Ralph A. Bradshaw University of California, Irvine
Luiz Juliano
Luiz Juliano Federal University of Sao Paulo
David M. Ornitz
David M. Ornitz Washington University in St. Louis
Michael Downes
Michael Downes Salk Institute for Biological Studies
Jochen Hess
Jochen Hess University Hospital Heidelberg
Stephen Anderson
Stephen Anderson Rutgers, The State University of New Jersey
Morley D. Hollenberg
Morley D. Hollenberg University of Calgary
Peter Angel
Peter Angel Karlsruhe Institute of Technology
Eric M. Shooter
Eric M. Shooter Stanford University

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