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D-Index & Metrics

Chemistry

D-Index
54
Citations
8863
World Ranking
12785
National Ranking
3383

Overview

Larry C. Sieker is affiliated with the University of Washington in the United States. Their academic profile currently highlights a focus on scientific research, although specific details about their fields of study, subfields, or main research topics are not provided.

There are no listed recent papers documenting Larry C. Sieker's scholarly output, including titles, publication years, or venues. Additionally, no information is available regarding frequent co-authors or recurring publication venues to further characterize their collaborative networks or preferred journals and conferences.

Larry C. Sieker does not have book publications recorded in the provided data, and there are no awards or honors documented in association with their name. This lack of detailed research records limits the scope for analyzing their contributions through bibliometric or subject-focused lenses.

Given the sparse dataset, no specific insights into Larry C. Sieker's research directions or academic impact can be drawn at this point. Nonetheless, their affiliation with a major research institution like the University of Washington positions them within a significant academic environment.

Best Publications

  • The Structure of a Bacterial Ferredoxin

    Elinor T. Adman;Larry C. Sieker;Lyle H. Jensen

  • A crystallographic model for azurin at 3 Å resolution

    Elinor T. Adman;Ronald E. Stenkamp;Larry C. Sieker;Lyle H. Jensen

  • A comparison of Fe 4 S 4 clusters in high-potential iron protein and in ferredoxin.

    C. W. Carter;J. Kraut;S. T. Freer;R. A. Alden

  • Structures of deoxy and oxy hemerythrin at 2.0 A resolution.

    M.A Holmes;I Le Trong;S Turley;L.C Sieker

  • Structure of a dioxygen reduction enzyme from Desulfovibrio gigas.

    Carlos Frazão;Gabriela G. F. Silva;Cláudio M. Gomes;Pedro Matias

  • Refinement of the model of a protein: rubredoxin at 1.5 Å resolution

    K. D. Watenpaugh;L. C. Sieker;J. R. Herriott;L. H. Jensen

  • The structure of rubredoxin at 1.2 Å resolution

    Keith D. Watenpaugh;Larry C. Sieker;Lyle H. Jensen

  • Crystallographic refinement of rubredoxin at 1 x 2 A degrees resolution.

    Keith D. Watenpaugh;Larry C. Sieker;Lyle H. Jensen

  • BINUCLEAR IRON COMPLEXES IN METHEMERYTHRIN AND AZIDOMETHEMERYTHRIN AT 2. 0-A RESOLUTION.

    Ronald E. Stenkamp;Larry C. Sieker;Lyle H. Jensen

  • The application of direct methods and Patterson interpretation to high-resolution native protein data.

    G. M. Sheldrick;Z. Dauter;K. S. Wilson;H. Hope

  • Structure of rubredoxin: an x-ray study to 2.5 A resolution.

    J.R. Herriott;L.C. Sieker;L.H. Jensen;W. Lovenberg

  • Refined crystal structure of ferredoxin II from Desulfovibrio gigas at 1·7 Å

    Charles R. Kissinger;Larry C. Sieker;Elinor T. Adman;Lyle H. Jensen

  • Zinc- and iron-rubredoxins from Clostridium pasteurianum at atomic resolution: a high-precision model of a ZnS4 coordination unit in a protein.

    Zbigniew Dauter;Keith S. Wilson;Larry C. Sieker;Jean-Marc Moulis

  • The Binding of Riboflavin-5′-Phosphate in a Flavoprotein: Flavodoxin at 2.0-Å Resolution

    K. D. Watenpaugh;L. C. Sieker;L. H. Jensen

  • Atomic resolution (0.94 A) structure of Clostridium acidurici ferredoxin. Detailed geometry of [4Fe-4S] clusters in a protein.

    Zbigniew Dauter;Keith S. Wilson;Larry C. Sieker;Jacques Meyer

  • Refinement of triclinic hen egg-white lysozyme at atomic resolution.

    Martin A. Walsh;Thomas R. Schneider;Larry C. Sieker;Zbigniew Dauter;Zbigniew Dauter

  • Active site structures of deoxyhemerythrin and oxyhemerythrin

    Ronald E. Stenkamp;Larry C. Sieker;L. H. Jensen;John D. McCallum

  • 26-10 Fab-digoxin complex: affinity and specificity due to surface complementarity

    Philip D. Jeffrey;Roland K. Strong;Larry C. Sieker;Chieh Ying Y. Chang

  • Structure of the Fe-S Complex in a Bacterial Ferredoxin

    L. C. Sieker;Elinor Adman;L. H. Jensen

  • Rubredoxin from Desulfovibrio gigas: A molecular model of the oxidized form at 1.4 Å resolution

    Michel Frey;Larry Sieker;Françoise Payan;Richard Haser

Frequent Co-Authors

Ronald E. Stenkamp
Ronald E. Stenkamp University of Washington
Jean LeGall
Jean LeGall University of Georgia
Maria Arménia Carrondo
Maria Arménia Carrondo Universidade Nova de Lisboa
Keith S. Wilson
Keith S. Wilson University of York
Roland Douce
Roland Douce Joseph Fourier University
Zbigniew Dauter
Zbigniew Dauter Brookhaven National Laboratory
Mireille Bruschi
Mireille Bruschi Centre national de la recherche scientifique, CNRS
Isabel Moura
Isabel Moura Universidade Nova de Lisboa
Gary P. Drobny
Gary P. Drobny University of Washington
George M. Sheldrick
George M. Sheldrick University of Göttingen

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