D. Nikolov

发表

Ephrin-B2 and ephrin-B3 as functional henipavirus receptors.

C. Broder, Kai Xu, D. Nikolov, 2012, Seminars in cell & developmental biology.

Crystal structure of an Eph receptor–ephrin complex

Martin Lackmann, Chad A. Cowan, M. Lackmann, 2001, Nature.

RNA polymerase II transcription initiation: a structural view.

S. Burley, D. Nikolov, Stephen K. Burley, 1997, Proceedings of the National Academy of Sciences of the United States of America.

Structural features of the Nogo receptor signaling complexes at the neuron/myelin interface

D. Nikolov, N. Saha, M. Kolev, 2014, Neuroscience Research.

High-level expression of a full-length Eph receptor.

D. Grandy, H. Erdjument-Bromage, S. Paavilainen, 2013, Protein expression and purification.

X-ray crystallographic studies of eukaryotic transcription factors.

A. Ferré-D’Amaré, S. Burley, K. L. Clark, 1993, Cold Spring Harbor symposia on quantitative biology.

Structure‐Based Enzyme Engineering and Its Impact on In Vitro Glycorandomization

J. Thorson, D. Nikolov, D. Hoffmeister, 2004, Chembiochem : a European journal of chemical biology.

Crystal Structure of the Hendra Virus Attachment G Glycoprotein Bound to a Potent Cross-Reactive Neutralizing Human Monoclonal Antibody

C. Broder, D. Dimitrov, H. Feldmann, 2013, PLoS pathogens.

Crystal structure of the ligand-binding domain of the receptor tyrosine kinase EphB2

D. Nikolov, J. Himanen, M. Henkemeyer, 1998, Nature.

Ephrin-A1 and the sheddase ADAM12 are upregulated in COVID-19

D. Nikolov, J. Himanen, P. Premsrirut, 2021, Heliyon.

Preferential Antibody and Drug Conjugate Targeting of the ADAM10 Metalloprotease in Tumours

P. W. Janes, D. Nikolov, L. Hii, 2022, Cancers.

Kinetic analysis of the binding of monomeric and dimeric ephrins to Eph receptors: Correlation to function in a growth cone collapse assay

Chen Li, D. Nikolov, J. Himanen, 2007, Protein science : a publication of the Protein Society.

Tie1-Tie2 interactions mediate functional differences between angiopoietin ligands.

D. Nikolov, T. Seegar, W. Barton, 2010, Molecular cell.

Cell Surface Multimeric Assemblies Regulate Canonical and Noncanonical EphA2 Receptor Tyrosine Kinase Signaling

M. Buck, K. Sossey-Alaoui, V. Varadan, 2021, bioRxiv.

Substrate specificity of NovM: implications for novobiocin biosynthesis and glycorandomization.

J. Thorson, D. Nikolov, J. Biggins, 2003, Organic letters.

Ligand recognition by A‐class Eph receptors: crystal structures of the EphA2 ligand‐binding domain and the EphA2/ephrin‐A1 complex

M. Buck, Y. Goldgur, K. Rajashankar, 2009, EMBO reports.

Adam Meets Eph: An ADAM Substrate Recognition Module Acts as a Molecular Switch for Ephrin Cleavage In trans

C. Blobel, E. Nievergall, P. W. Janes, 2005, Cell.

Purification, crystallization and preliminary characterization of an Eph-B2/ephrin-B2 complex.

D. Nikolov, J. Himanen, 2002, Acta crystallographica. Section D, Biological crystallography.

Dissecting the EphA3/Ephrin-A5 Interactions Using a Novel Functional Mutagenesis Screen*

Ke Chen, Andrew W Boyd, Martin Lackmann, 2004, Journal of Biological Chemistry.

Crystal structure of a human TATA box-binding protein/TATA element complex.

S K Burley, S. Burley, R. Roeder, 1996, Proceedings of the National Academy of Sciences of the United States of America.

Co-crystal structure of TBP recognizing the minor groove of a TATA element

Stephen K. Burley, S. Burley, D. Nikolov, 1993, Nature.

Crystal structure of a TFIIB–TBP–TATA-element ternary complex

S. Burley, R. Roeder, E. Halay, 1995, Nature.

Expanding pyrimidine diphosphosugar libraries via structure-based nucleotidylyltransferase engineering

Jon S Thorson, Jiqing Jiang, J. Thorson, 2002, Proceedings of the National Academy of Sciences of the United States of America.

Structure, mechanism and engineering of a nucleotidylyltransferase as a first step toward glycorandomization

P. Jeffrey, J. Thorson, K. Rajashankar, 2001, Nature Structural Biology.

Structural and functional analyses reveal promiscuous and species specific use of ephrin receptors by Cedar virus

C. Broder, R. Cattaneo, Kai Xu, 2019, Proceedings of the National Academy of Sciences.

Henipavirus Mediated Membrane Fusion, Virus Entry and Targeted Therapeutics

C. Broder, D. Nikolov, K. Xu, 2012, Viruses.

Crystal structure of eukaryotic DNA ligase-adenylate illuminates the mechanism of nick sensing and strand joining.

S. Shuman, D. Nikolov, M. Odell, 2000, Molecular cell.

ADAM proteases: Emerging role and targeting of the non-catalytic domains.

D. Nikolov, J. Himanen, N. Saha, 2019, Cancer letters.

Crystal structures of Lgr4 and its complex with R-spondin1.

K. Rajashankar, Kai Xu, D. Nikolov, 2013, Structure.

Structure of the Semaphorin-3A Receptor Binding Module

Min Lu, A. Püschel, V. Nardi-Dei, 2003, Neuron.

Cell-cell signaling via Eph receptors and ephrins.

D. Nikolov, J. Himanen, N. Saha, 2007, Current opinion in cell biology.

Tie2 and Eph receptor tyrosine kinase activation and signaling.

D. Nikolov, J. Himanen, T. Seegar, 2014, Cold Spring Harbor perspectives in biology.

A semisynthetic Eph receptor tyrosine kinase provides insight into ligand-induced kinase activation.

T. Muir, H. Erdjument-Bromage, D. Nikolov, 2011, Chemistry & biology.

Eph receptors and ephrins.

D. Nikolov, J. Himanen, Juha-Pekka Himanen, 2003, The international journal of biochemistry & cell biology.

Structural Basis for Regulated Proteolysis by the α-Secretase ADAM10

S. Blacklow, P. W. Janes, A. Kruse, 2017, Cell.

Structures of netrin-1 bound to two receptors provide insight into its axon guidance mechanism

N. Renier, Zhuhao Wu, M. Tessier-Lavigne, 2014, Science.

Homotypic receptor-receptor interactions regulating Eph signaling

Kai Xu, D. Nikolov, J. Himanen, 2014, Cell adhesion & migration.

Structures of axon guidance molecules and their neuronal receptors.

D. Nikolov, J. Himanen, W. Barton, 2004, Advances in protein chemistry.

Eph signaling: a structural view

D. Nikolov, J. Himanen, 2003, Trends in Neurosciences.

Crystal structure of the ligand-binding domain of the promiscuous EphA4 receptor reveals two distinct conformations.

Y. Goldgur, S. Paavilainen, D. Nikolov, 2010, Biochemical and biophysical research communications.

Immunization strategies against henipaviruses.

C. Broder, K. N. Bossart, Kai Xu, 2012, Current topics in microbiology and immunology.

A treatment for and vaccine against the deadly Hendra and Nipah viruses.

C. Broder, D. Dimitrov, Zhongyu Zhu, 2013, Antiviral research.

Crystal Structure of the Pre-fusion Nipah Virus Fusion Glycoprotein Reveals a Novel Hexamer-of-Trimers Assembly

C. Broder, Z. Zhou, G. Skiniotis, 2015, PLoS pathogens.

Biochemical, Conformational, and Immunogenic Analysis of Soluble Trimeric Forms of Henipavirus Fusion Glycoproteins

C. Broder, G. Skiniotis, Min Lu, 2012, Journal of Virology.

Host cell recognition by the henipaviruses: Crystal structures of the Nipah G attachment glycoprotein and its complex with ephrin-B3

Kai Xu, C. Broder, K. Rajashankar, 2008, Proceedings of the National Academy of Sciences.

Binding of EphrinA5 to RET receptor tyrosine kinase: An in vitro study

A. Goldman, D. Nikolov, J. Himanen, 2018, PloS one.

2.1 Å resolution refined structure of a TATA box-binding protein (TBP)

S. Burley, D. Nikolov, 1994, Nature Structural Biology.

Highly efficient selenomethionine labeling of recombinant proteins produced in mammalian cells

H. Erdjument-Bromage, P. Tempst, D. Nikolov, 2006, Protein science : a publication of the Protein Society.

Structural and functional features of the Escherichia coli hydroperoxide resistance protein OsmC

D. Nikolov, W. Barton, Jacob Lesniak, 2003, Protein science : a publication of the Protein Society.

Structural and functional characterization of the Pseudomonas hydroperoxide resistance protein Ohr

D. Nikolov, W. Barton, Jacob Lesniak, 2002, The EMBO journal.

Crystal structure of TFIID TATA-box binding protein

A. Hoffmann, M. Horikoshi, S. Burley, 1992, Nature.

New Insights into the Hendra Virus Attachment and Entry Process from Structures of the Virus G Glycoprotein and Its Complex with Ephrin-B2

C. Broder, K. Rajashankar, Kai Xu, 2012, PloS one.

Architecture of Eph receptor clusters

P. W. Janes, M. Lackmann, J. Walker, 2010, Proceedings of the National Academy of Sciences.

Crystal structure of the human ephrin‐A5 ectodomain

M. Lackmann, P. Jeffrey, D. Nikolov, 2007, Protein science : a publication of the Protein Society.

GABARAP: Lessons for Synaptogenesis

D. Nikolov, J. Coyle, 2003, The Neuroscientist : a review journal bringing neurobiology, neurology and psychiatry.

Repelling class discrimination: ephrin-A5 binds to and activates EphB2 receptor signaling

Chen Li, Andrew W Boyd, Martin Lackmann, 2004, Nature Neuroscience.

Structural basis for angiopoietin-1–mediated signaling initiation

Y. Goldgur, K. Rajashankar, D. Nikolov, 2013, Proceedings of the National Academy of Sciences.

Crystal structures of the Tie2 receptor ectodomain and the angiopoietin-2–Tie2 complex

K. Rajashankar, D. Nikolov, J. Himanen, 2006, Nature Structural &Molecular Biology.

Site occupancy and glycan compositional analysis of two soluble recombinant forms of the attachment glycoprotein of Hendra virus.

Kai Xu, Michelle L Colgrave, C. Broder, 2012, Glycobiology.

Biological and Structural Characterization of Glycosylation on Ephrin-A1, a Preferred Ligand for EphA2 Receptor Tyrosine Kinase*

Y. Goldgur, W. Debinski, D. Nikolov, 2013, The Journal of Biological Chemistry.

Eph/ephrin recognition and the role of Eph/ephrin clusters in signaling initiation.

Kai Xu, D. Nikolov, J. Himanen, 2013, Biochimica et biophysica acta.

An activated form of ADAM10 is tumor selective and regulates cancer stem-like cells and tumor growth

S. Rafii, U. Kusebauch, R. Moritz, 2016, The Journal of experimental medicine.

Therapeutic potential of targeting the Eph/ephrin signaling complex.

D. Nikolov, J. Himanen, N. Saha, 2018, The international journal of biochemistry & cell biology.

Crystal structure of the ephrin-B1 ectodomain: implications for receptor recognition and signaling.

D. Nikolov, J. Himanen, W. Barton, 2005, Biochemistry.

Structure of the EphB6 receptor ectodomain

Y. Goldgur, A. Freywald, D. Nikolov, 2021, PloS one.

Structure of GABARAP in Two Conformations Implications for GABAA Receptor Localization and Tubulin Binding

K. Rajashankar, D. Nikolov, S. Qamar, 2002, Neuron.

From genetic data and structures to drug development: New approaches to target Eph receptors

D. Nikolov, J. Himanen, 2021 .

Identification of X-DING-CD4, a new member of human DING protein family that is secreted by HIV-1 resistant CD4(+) T cells and has anti-viral activity.

M. Simm, A. Lesner, D. Nikolov, 2009, Biochemical and biophysical research communications.

Monoubiquitinated histone H1B is required for antiviral protection in CD4(+)T cells resistant to HIV-1.

M. Simm, A. Kartvelishvili, A. Lesner, 2004, Biochemistry.

Insights into Eph receptor tyrosine kinase activation from crystal structures of the EphA4 ectodomain and its complex with ephrin-A5

Y. Goldgur, Kai Xu, D. Nikolov, 2013, Proceedings of the National Academy of Sciences.

Following experimental stroke, the recovering brain is vulnerable to lipoxygenase‐dependent semaphorin signaling

E. Lo, T. Holman, D. Nikolov, 2013, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

Structure and axon outgrowth inhibitor binding of the Nogo‐66 receptor and related proteins

A. Fournier, S. Strittmatter, P. Jeffrey, 2003, The EMBO journal.

The crystal structure of DR6 in complex with the amyloid precursor protein provides insight into death receptor activation

M. Tessier-Lavigne, Kai Xu, D. Nikolov, 2015, Genes & development.

Fully human monoclonal antibody targeting activated ADAM10 on colorectal cancer cells

D. Dimitrov, P. W. Janes, M. J. de la Cruz, 2023, Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie.

Structure of the angiopoietin-2 receptor binding domain and identification of surfaces involved in Tie2 recognition.

D. Nikolov, W. Barton, D. Tzvetkova, 2005, Structure.

Inhibitory monoclonal antibody targeting ADAM17 expressed on cancer cells

D. Dimitrov, E. de Stanchina, Zhongyu Zhu, 2021, Translational oncology.

Crystal structure of the Nogo‐receptor‐2

Y. Goldgur, D. Nikolov, J. Himanen, 2011, Protein science : a publication of the Protein Society.

Antibodies binding the ADAM10 substrate recognition domain inhibit Eph function

A. Scott, P. W. Janes, M. Lackmann, 2012, Journal of Cell Science.

Three Distinct Molecular Surfaces in Ephrin-A5 Are Essential for a Functional Interaction with EphA3*[boxs]

Andrew W Boyd, Martin Lackmann, M. Lackmann, 2005, Journal of Biological Chemistry.

Generation and characterization of a single-chain anti-EphA2 antibody

Y. Goldgur, E. Oricchio, H. Wendel, 2014, Growth factors.

Crystal structures of the Tie 2 receptor ectodomain and the angiopoietin-2 – Tie 2 complex

K. Rajashankar, D. Nikolov, J. Himanen, 2006 .

Angiopoietin-2 Receptor Binding Domain

D. Nikolov, W. Barton, D. Tzvetkova, 2005 .

The Ephb2 Receptor Uses Homotypic, Head-to-Tail Interactions within Its Ectodomain as an Autoinhibitory Control Mechanism

M. Dalva, Kai Xu, D. Nikolov, 2021, International journal of molecular sciences.

Molecules in focus Eph receptors and ephrins

D. Nikolov, J. Himanen, 2003 .