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Ylva Lindqvist

Ylva Lindqvist

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Biology and Biochemistry
Sweden
2023

D-Index & Metrics

Biology and Biochemistry

D-Index
65
Citations
15276
World Ranking
9136
National Ranking
123

Research.com Recognitions

  • 2023 - Research.com Biology and Biochemistry in Sweden Leader Award

Overview

Ylva Lindqvist is a researcher affiliated with the Karolinska Institute in Sweden, contributing to the fields of biochemistry, genetics, and molecular biology. Their work spans several overlapping disciplines, including biochemistry, spectroscopy, and molecular biology.

Their research primarily addresses areas related to lipid metabolism and biosynthesis, mass spectrometry techniques and applications, as well as glycosylation and glycoproteins research.

  • Regioselectivity mechanism of the Thunbergia alata Δ6-16:0-acyl carrier protein desaturase (2021, PLANT PHYSIOLOGY)

Lindqvist has collaborated with multiple coauthors during their research activities, with frequent partnerships involving Jodie E. Guy, Yuanheng Cai, Marcel D. Baer, Edward Whittle, and Jin Chai.

Their publications have appeared predominantly in the journal PLANT PHYSIOLOGY, reinforcing a focus on plant biochemistry within molecular biology contexts.

Best Publications

  • Conversion of a beta-ketoacyl synthase to a malonyl decarboxylase by replacement of the active-site cysteine with glutamine.

    Andrzej Witkowski;Anil K. Joshi;Ylva Lindqvist;Stuart Smith

  • Structure of human pro-matrix metalloproteinase-2: activation mechanism revealed.

    Ekaterina Morgunova;Ari Tuuttila;Ulrich Bergmann;Mikhail Isupov

  • Crystal structure of delta9 stearoyl-acyl carrier protein desaturase from castor seed and its relationship to other di-iron proteins.

    Y. Lindqvist;W. Huang;G. Schneider;J. Shanklin

  • Three-dimensional structure of transketolase, a thiamine diphosphate dependent enzyme, at 2.5 A resolution.

    Ylva Lindqvist;Gunter Schneider;Ulrich Ermler;Michael Sundström

  • Three-dimensional structure of a mammalian thioredoxin reductase: Implications for mechanism and evolution of a selenocysteine-dependent enzyme

    Tatyana Sandalova;Liangwei Zhong;Ylva Lindqvist;Arne Holmgren

  • The manifold of vitamin B6 dependent enzymes

    Gunter Schneider;Helena Käck;Ylva Lindqvist

  • Crystal structure of nitrile hydratase reveals a novel iron centre in a novel fold

    Weijun Huang;Jia Jia;John Cummings;Mark Nelson

  • Crystal structure of the active site of ribulose-bisphosphate carboxylase

    Inger Andersson;Stefan Knight;Gunter Schneider;Ylva Lindqvist

  • Structure of the complex between the antibiotic cerulenin and its target, beta-ketoacyl-acyl carrier protein synthase.

    Martin Moche;Gunter Schneider;Patricia Edwards;Katayoon Dehesh

  • A thiamin diphosphate binding fold revealed by comparison of the crystal structures of transketolase, pyruvate oxidase and pyruvate decarboxylase

    Yves A Muller;Yves A Muller;Ylva Lindqvist;Ylva Lindqvist;William Furey;William Furey;Georg E Schulz;Georg E Schulz

  • Crystal Structure and Catalysis of the Selenoprotein Thioredoxin Reductase 1

    Qing Cheng;Tatyana Sandalova;Ylva Lindqvist;Elias S. J. Arnér

  • Crystal structure of beta-ketoacyl-acyl carrier protein synthase II from E.coli reveals the molecular architecture of condensing enzymes.

    Weijun Huang;Jia Jia;Patricia Edwards;Katayoon Dehesh

  • Redesign of soluble fatty acid desaturases from plants for altered substrate specificity and double bond position

    Edgar B. Cahoon;Ylva Lindqvist;Gunter Schneider;John Shanklin

  • Three-dimensional structure of ribulose-1,5-bisphosphate carboxylase/oxygenase from Rhodospirillum rubrum at 2.9 Å resolution

    Gunter Schneider;Ylva Lindqvist;Carl-Ivar Brändén;George Lorimer

  • Refined structure of spinach glycolate oxidase at 2 A resolution.

    Ylva Lindqvist

  • Circular permutations of natural protein sequences: structural evidence.

    Ylva Lindqvist;Gunter Schneider

  • The crystal structure of phenol hydroxylase in complex with FAD and phenol provides evidence for a concerted conformational change in the enzyme and its cofactor during catalysis

    Cristofer Enroth;Halina Neujahr;Gunter Schneider;Ylva Lindqvist

  • Desaturases: Emerging Models for Understanding Functional Diversification of Diiron-containing Enzymes

    John Shanklin;Jodie E. Guy;Girish Mishra;Ylva Lindqvist

  • Three-dimensional structure of a mammalian purple acid phosphatase at 2.2 A resolution with a mu-(hydr)oxo bridged di-iron center.

    Ylva Lindqvist;Eva Johansson;Helena Kaija;Pirkko Vihko;Pirkko Vihko

  • The enzymes of oxalate metabolism: unexpected structures and mechanisms.

    Draženka Svedružić;Stefán Jónsson;Cory G. Toyota;Laurie A. Reinhardt

Frequent Co-Authors

Gunter Schneider
Gunter Schneider Karolinska Institute
John Shanklin
John Shanklin Brookhaven National Laboratory
Pirkko Vihko
Pirkko Vihko University of Helsinki
George H. Lorimer
George H. Lorimer University of Maryland, College Park
Georg A. Sprenger
Georg A. Sprenger University of Stuttgart
Katayoon Dehesh
Katayoon Dehesh University of California, Riverside
Hermann Sahm
Hermann Sahm Forschungszentrum Jülich
Elias S.J. Arnér
Elias S.J. Arnér Karolinska Institute
Eva Johansson
Eva Johansson Swedish University of Agricultural Sciences
Ute Römling
Ute Römling Karolinska Institute

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