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Natalie C. J. Strynadka

Natalie C. J. Strynadka

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Chemistry
Canada
2025
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Biology and Biochemistry
Canada
2023

D-Index & Metrics

Biology and Biochemistry

D-Index
84
Citations
23225
World Ranking
3354
National Ranking
104

Chemistry

D-Index
83
Citations
22444
World Ranking
2974
National Ranking
67

Natalie C. J. Strynadka publication distribution in Chemistry in 2026

The chart shows the distribution of publications by all Research.com ranked scientists in the field of Chemistry in 2026. The highlighted bar marks where Natalie C. J. Strynadka sits on this spectrum.

61–80 publications: 66 scientists 81–100 publications: 302 scientists 101–120 publications: 623 scientists 121–140 publications: 918 scientists 141–160 publications: 1,218 scientists 161–180 publications: 1,350 scientists 181–200 publications: 1,344 scientists 201–220 publications: 1,281 scientists 221–240 publications: 1,216 scientists 241–260 publications: 1,100 scientists 261–280 publications: 979 scientists 281–300 publications: 939 scientists 301–320 publications: 764 scientists 321–340 publications: 643 scientists 341–360 publications: 628 scientists 361–380 publications: 522 scientists 381–400 publications: 459 scientists 401–420 publications: 397 scientists 421–440 publications: 327 scientists 441–460 publications: 270 scientists 461–480 publications: 265 scientists 481–500 publications: 252 scientists 501–520 publications: 201 scientists 521–540 publications: 185 scientists 541–560 publications: 148 scientists 561–580 publications: 148 scientists 581–600 publications: 132 scientists 601–620 publications: 114 scientists 621–640 publications: 104 scientists 641–660 publications: 91 scientists 661–680 publications: 92 scientists 681–700 publications: 73 scientists 701–720 publications: 57 scientists 721–740 publications: 54 scientists 741–760 publications: 67 scientists 761–780 publications: 45 scientists 781–800 publications: 46 scientists 801–820 publications: 39 scientists 821–840 publications: 32 scientists 841–860 publications: 36 scientists 861–880 publications: 29 scientists 881–900 publications: 26 scientists 901–920 publications: 24 scientists 921–940 publications: 14 scientists 941–960 publications: 23 scientists 961–980 publications: 28 scientists 981–1,000 publications: 15 scientists 1,001–1,020 publications: 29 scientists 1,021–1,040 publications: 12 scientists 1,041–1,060 publications: 19 scientists 1,061–1,080 publications: 12 scientists 1,081–1,100 publications: 6 scientists 1,101–1,120 publications: 8 scientists 1,121–1,140 publications: 12 scientists 1,141–1,160 publications: 5 scientists 1,161–1,180 publications: 6 scientists 1,181–1,200 publications: 14 scientists 1,201–1,220 publications: 7 scientists 1,221–1,240 publications: 2 scientists 1,241–1,260 publications: 6 scientists 1,261–1,280 publications: 4 scientists 1,281–1,294 publications: 6 scientists 1,295+ publications: 100 scientists
61 publications 1,295+

This scientist: 465 publications — 86th percentile

86% of scientists in this discipline score the same or lower.

The last bar groups every scientist with 1,295 publications or more.

Natalie C. J. Strynadka D-index placement in Chemistry in 2026

The chart shows the D-index (discipline H-index) distribution of Chemistry scientists ranked by Research.com in 2026. The highlighted bar marks where Natalie C. J. Strynadka sits on this spectrum.

40–41 D-Index: 289 scientists 42–43 D-Index: 612 scientists 44–45 D-Index: 808 scientists 46–47 D-Index: 776 scientists 48–49 D-Index: 835 scientists 50–51 D-Index: 861 scientists 52–53 D-Index: 872 scientists 54–55 D-Index: 933 scientists 56–57 D-Index: 1,051 scientists 58–59 D-Index: 930 scientists 60–61 D-Index: 882 scientists 62–63 D-Index: 834 scientists 64–65 D-Index: 731 scientists 66–67 D-Index: 775 scientists 68–69 D-Index: 683 scientists 70–71 D-Index: 646 scientists 72–73 D-Index: 561 scientists 74–75 D-Index: 501 scientists 76–77 D-Index: 437 scientists 78–79 D-Index: 388 scientists 80–81 D-Index: 354 scientists 82–83 D-Index: 292 scientists 84–85 D-Index: 275 scientists 86–87 D-Index: 254 scientists 88–89 D-Index: 235 scientists 90–91 D-Index: 185 scientists 92–93 D-Index: 192 scientists 94–95 D-Index: 155 scientists 96–97 D-Index: 163 scientists 98–99 D-Index: 125 scientists 100–101 D-Index: 105 scientists 102–103 D-Index: 105 scientists 104–105 D-Index: 112 scientists 106–107 D-Index: 88 scientists 108–109 D-Index: 68 scientists 110–111 D-Index: 69 scientists 112–113 D-Index: 65 scientists 114–115 D-Index: 79 scientists 116–117 D-Index: 61 scientists 118–119 D-Index: 44 scientists 120–121 D-Index: 37 scientists 122–123 D-Index: 40 scientists 124–125 D-Index: 33 scientists 126–127 D-Index: 26 scientists 128–129 D-Index: 34 scientists 130–131 D-Index: 35 scientists 132–133 D-Index: 25 scientists 134–135 D-Index: 27 scientists 136–137 D-Index: 17 scientists 138–139 D-Index: 16 scientists 140–141 D-Index: 20 scientists 142–143 D-Index: 20 scientists 144–145 D-Index: 15 scientists 146–147 D-Index: 9 scientists 148–149 D-Index: 9 scientists 150–151 D-Index: 16 scientists 152–153 D-Index: 11 scientists 154–155 D-Index: 9 scientists 156–157 D-Index: 3 scientists 158 D-Index: 3 scientists 159+ D-Index: 98 scientists
40 D-Index 159+

This scientist: 83 D-Index — 84th percentile

84% of scientists in this discipline score the same or lower.

The last bar groups every scientist with 159 D-Index or more.

Research.com Recognitions

  • 2025 - Research.com Chemistry in Canada Leader Award
  • 2023 - Research.com Biology and Biochemistry in Canada Leader Award
  • 2022 - Research.com Chemistry in Canada Leader Award
  • 2015 - Fellow of the Royal Society, United Kingdom
  • 2006 - Fellow of the Royal Society of Canada Academy of Science

Overview

What is she best known for?

The fields of study she is best known for:

  • Enzyme
  • Gene
  • Amino acid

Her primary scientific interests are in Biochemistry, Stereochemistry, Enzyme, Hydrolase and Binding site. Her study in Glycosyltransferase, Escherichia coli, Transferase, Oxidoreductase and Mutant is done as part of Biochemistry. Her Stereochemistry study combines topics in areas such as Crystallography, Protein structure, Cofactor and Active site.

Her work in Enzyme addresses issues such as Antibiotic resistance, which are connected to fields such as Penicillin and Lactam. Her Hydrolase research integrates issues from Cleavage, Covalent bond, Beta-lactam, New Delhi metallo-beta-lactamase and Nucleophile. Her studies in Binding site integrate themes in fields like Virulence, Secretion and Effector, Cell biology, Protein folding.

Her most cited work include:

  • Crystal structures of the helix-loop-helix calcium-binding proteins. (735 citations)
  • Molecular structure of the acyl-enzyme intermediate in β-lactam hydrolysis at 1.7 Å resolution (426 citations)
  • Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A (368 citations)

What are the main themes of her work throughout her whole career to date?

Natalie C. J. Strynadka mainly investigates Biochemistry, Stereochemistry, Enzyme, Secretion and Crystal structure. Peptidoglycan, Protein structure, Mutant, Escherichia coli and Sialic acid are the subjects of her Biochemistry studies. Her Stereochemistry research also works with subjects such as

  • Active site and related Binding site,
  • Transferase and related Glycosyltransferase.

As a member of one scientific family, Natalie C. J. Strynadka mostly works in the field of Enzyme, focusing on Staphylococcus aureus and, on occasion, Antibiotic resistance. Her study in Secretion is interdisciplinary in nature, drawing from both Transport protein, Effector, Cell biology, Virulence and Biophysics. Her work deals with themes such as Type three secretion system and Enteropathogenic Escherichia coli, which intersect with Effector.

She most often published in these fields:

  • Biochemistry (40.53%)
  • Stereochemistry (32.95%)
  • Enzyme (17.80%)

What were the highlights of her more recent work (between 2017-2021)?

  • Crystal structure (13.64%)
  • Biophysics (9.47%)
  • Peptidoglycan (10.61%)

In recent papers she was focusing on the following fields of study:

Natalie C. J. Strynadka focuses on Crystal structure, Biophysics, Peptidoglycan, Bacterial cell structure and Secretion. Her Crystal structure research includes elements of Stereochemistry and Penicillin binding proteins. Her Stereochemistry research includes themes of Heptose, Pyrophosphate and Ceftobiprole.

Cell wall, Enzyme and Biochemistry are inherently bound to her Peptidoglycan studies. The concepts of her Bacterial cell structure study are interwoven with issues in Periplasmic space, Escherichia coli and Bacillus subtilis. Her research in Secretion intersects with topics in Transport protein, Effector, Cell biology, Flagellum and Type three secretion system.

Between 2017 and 2021, her most popular works were:

  • Cryo-EM analysis of the T3S injectisome reveals the structure of the needle and open secretin. (55 citations)
  • Cryo-EM structure of the homohexameric T3SS ATPase-central stalk complex reveals rotary ATPase-like asymmetry. (29 citations)
  • T3S injectisome needle complex structures in four distinct states reveal the basis of membrane coupling and assembly. (25 citations)

In her most recent research, the most cited papers focused on:

  • Enzyme
  • Gene
  • Amino acid

Her primary areas of study are Secretion, Bacterial cell structure, Peptidoglycan, Biophysics and Bacterial outer membrane. Her Secretion study combines topics from a wide range of disciplines, such as Transport protein, Cell biology, Host cell membrane and Virulence. Her Bacterial cell structure research integrates issues from Teichoic acid, Cell wall, Bacillus subtilis and Cytoplasm.

Her Teichoic acid research is classified as research in Biochemistry. Natalie C. J. Strynadka has included themes like Type three secretion system, Membrane, Inner membrane, Effector and Heptose in her Bacterial outer membrane study. In her work, Protein structure is strongly intertwined with Stereochemistry, which is a subfield of Hydrolase.

Best Publications

  • Crystal structures of the helix-loop-helix calcium-binding proteins.

    Natalie C. J. Strynadka;Michael N. G. James

  • Molecular structure of the acyl-enzyme intermediate in β-lactam hydrolysis at 1.7 Å resolution

    Natalie C. J. Strynadka;Hiroyuki Adachi;Susan E. Jensen;Kathy Johns

  • Structural basis for the |[beta]| lactam resistance of PBP2a from methicillin-resistant Staphylococcus aureus

    Daniel Lim;Natalie C.J. Strynadka

  • Beta-lactam antibiotic resistance: a current structural perspective.

    Mark S Wilke;Andrew L Lovering;Natalie C J Strynadka

  • Assembly, structure, function and regulation of type III secretion systems

    Wanyin Deng;Natalie C. Marshall;Jennifer L. Rowland;James M. McCoy

  • Aspergillomarasmine A overcomes metallo-β-lactamase antibiotic resistance

    Andrew M. King;Sarah A. Reid-Yu;Wenliang Wang;Dustin T. King

  • Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A

    Michela G Bertero;Richard A Rothery;Monica Palak;Cynthia Hou

  • Crystal structure of the retaining galactosyltransferase LgtC from Neisseria meningitidis in complex with donor and acceptor sugar analogs.

    Karina Persson;Hoa D. Ly;Manuela Dieckelmann;Warren W. Wakarchuk

  • Crystal structure of a bacterial signal peptidase in complex with a beta-lactam inhibitor.

    Mark Paetzel;Ross E. Dalbey;Natalie C. J. Strynadka

  • Crystal structure of enteropathogenic Escherichia coli intimin-receptor complex.

    Yu Luo;E. A. Frey;R. A. Pfuetzner;A. L. Creagh

  • Structural Perspective of Peptidoglycan Biosynthesis and Assembly

    Andrew L Lovering;Susan S Safadi;Natalie C J Strynadka

  • Structural insight into the transglycosylation step of bacterial cell-wall biosynthesis.

    Andrew L. Lovering;Liza H. de Castro;Daniel Lim;Natalie C. J. Strynadka

  • New Delhi metallo-β-lactamase: structural insights into β-lactam recognition and inhibition.

    Dustin T. King;Liam J. Worrall;Robert Gruninger;Natalie C. J. Strynadka

  • Calcium-binding sites in proteins: a structural perspective.

    Catherine A. McPhalen;Natalie C.J. Strynadka;Michael N.G. James

  • LYSOZYME REVISITED : CRYSTALLOGRAPHIC EVIDENCE FOR DISTORTION OF AN N-ACETYLMURAMIC ACID RESIDUE BOUND IN SITE D

    Natalie C.J. Strynadka;Michael N.G. James

  • Structural analysis of the sialyltransferase CstII from Campylobacter jejuni in complex with a substrate analog.

    Cecilia P C Chiu;Andrew G Watts;Luke L Lairson;Michel Gilbert

  • High-throughput screening methodology for the directed evolution of glycosyltransferases

    Amir Aharoni;Karena Thieme;Cecilia P C Chiu;Sabrina Buchini

  • Crystal structure of LexA: a conformational switch for regulation of self-cleavage.

    Yu Luo;Richard A. Pfuetzner;Steve Mosimann;Mark Paetzel

  • Crystal structure of New Delhi metallo-β-lactamase reveals molecular basis for antibiotic resistance.

    Dustin King;Natalie Strynadka;Natalie Strynadka

  • Studies of a ring-cleaving dioxygenase illuminate the role of cholesterol metabolism in the pathogenesis of Mycobacterium tuberculosis.

    Katherine C. Yam;Igor D'Angelo;Rainer Kalscheuer;Haizhong Zhu;Haizhong Zhu

  • Structural characterization of the molecular platform for type III secretion system assembly

    Calvin K. Yip;Tyler G. Kimbrough;Heather B. Felise;Marija Vuckovic

Frequent Co-Authors

B. Brett Finlay
B. Brett Finlay University of British Columbia
Stephen G. Withers
Stephen G. Withers University of British Columbia
Warren W. Wakarchuk
Warren W. Wakarchuk University of Alberta
Michael N. G. James
Michael N. G. James University of Alberta
Lindsay D. Eltis
Lindsay D. Eltis University of British Columbia
Lawrence P. McIntosh
Lawrence P. McIntosh University of British Columbia
Wanyin Deng
Wanyin Deng University of British Columbia
Ross E. Dalbey
Ross E. Dalbey The Ohio State University
Eric D. Brown
Eric D. Brown McMaster University
Susan E. Jensen
Susan E. Jensen University of Alberta

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