about
BMX, a novel nonreceptor tyrosine kinase gene of the BTK/ITK/TEC/TXK family located in chromosome Xp22.2Bruton's tyrosine kinase (Btk): function, regulation, and transformation with special emphasis on the PH domainMyasthenia gravis: studies on HL-A antigens and lymphocyte subpopulations in patients with myasthenia gravisOligonucleotide Therapies: The Past and the PresentLipid-based Transfection Reagents Exhibit Cryo-induced Increase in Transfection Efficiency.Solution structure of the SH3 domain from Bruton's tyrosine kinaseTargets for Ibrutinib Beyond B Cell MalignanciesHigh level of cannabinoid receptor 1, absence of regulator of G protein signalling 13 and differential expression of Cyclin D1 in mantle cell lymphomaFunctional interaction of caveolin-1 with Bruton's tyrosine kinase and BmxB Cell Receptor Activation Predominantly Regulates AKT-mTORC1/2 Substrates Functionally Related to RNA ProcessingDisruption of Higher Order DNA Structures in Friedreich's Ataxia (GAA)n Repeats by PNA or LNA TargetingSilencing of Bruton's tyrosine kinase (Btk) using short interfering RNA duplexes (siRNA)ANKRD54 preferentially selects Bruton's Tyrosine Kinase (BTK) from a Human Src-Homology 3 (SH3) domain libraryGenetic and demographic features of X-linked agammaglobulinemia in Eastern and Central Europe: a cohort study.Conformation of full-length Bruton tyrosine kinase (Btk) from synchrotron X-ray solution scattering.Phosphorylation of Bruton's tyrosine kinase by c-Abl.Both proline-rich sequences in the TH region of Bruton's tyrosine kinase stabilize intermolecular interactions with the SH3 domain.Intermolecular interactions between the SH3 domain and the proline-rich TH region of Bruton's tyrosine kinase.Bruton tyrosine kinase (BTK) in X-linked agammaglobulinemia (XLA).Rational design and purification of human Bruton's tyrosine kinase SH3-SH2 protein for structure-function studies.Thermal unfolding of small proteins with SH3 domain folding pattern.BTK, the tyrosine kinase affected in X-linked agammaglobulinemia.BTKbase, mutation database for X-linked agammaglobulinemia (XLA)Tec homology (TH) adjacent to the PH domain.Characterization of all possible single-nucleotide change caused amino acid substitutions in the kinase domain of Bruton tyrosine kinase.Transcriptional signatures of Itk-deficient CD3+, CD4+ and CD8+ T-cellsSignalling of Bruton's tyrosine kinase, Btk.Splice-correcting oligonucleotides restore BTK function in X-linked agammaglobulinemia modelThe cellular phenotype conditions Btk for cell survival or apoptosis signaling.Molecular cloning, characterization, and chromosomal localization of a human lymphoid tyrosine kinase related to murine Blk.Bruton's tyrosine kinase: cell biology, sequence conservation, mutation spectrum, siRNA modifications, and expression profiling.Polymyxins as inhibitors of polyclonal B-cell activators in murine lymphocyte cultures.Optimizing anti-gene oligonucleotide 'Zorro-LNA' for improved strand invasion into duplex DNA.Diagnostics of primary immunodeficiency diseases: a sequencing capture approachInhibitors of BTK and ITK: state of the new drugs for cancer, autoimmunity and inflammatory diseases.Clinical and molecular analysis of patients with defects in micro heavy chain gene.Splice-correction strategies for treatment of X-linked agammaglobulinemia.Extracellular vesicle in vivo biodistribution is determined by cell source, route of administration and targeting.In silico tools for signal transduction research.Adding functional entities to plasmids.
P50
Q24308348-6A2C3F65-D4F1-4E3B-8B4D-1171BA2B66E9Q24321955-34C2DD77-3AE0-4BFE-BCBE-C1141925E0EDQ24680629-E16094A7-37FF-4ED1-B3E4-D8373C500145Q27002403-EF7E19D6-310A-4655-8D3B-F7FF3DA3CC73Q27317260-44F0BD80-1CB5-473A-8AA5-AAABCD73D409Q27748889-11A5F6B1-2C2E-453D-BAD2-6EDDA3C676F5Q28087772-F5E34A1C-B3EA-4B7F-84E3-284ABD8ECAE3Q28206624-A18B68C4-E720-4F50-8FAB-C1885AA64F76Q28212744-DFF51661-FD56-49F8-B72E-539AB53C5931Q28553375-E689B589-F259-4F4A-957E-CA78140F78C6Q28553555-9F13FBBF-B972-46E3-9645-EB6DB0EEB862Q28569704-CAC5987B-8215-4EB8-AFD3-7DBDFA6102D3Q30008753-05F9BF9B-E197-4AE6-9E62-1CEEE20A9D06Q30157267-0E238AF7-E89D-4679-B23C-177F88571C60Q30164519-0E186399-3260-48F1-A35A-8CBC715761D9Q30165074-555CA8E5-1874-4D25-B19C-BB8E7DD6E19FQ30167787-6FF5EC89-28D5-4FBD-8940-688899DDB908Q30168418-BD93E2BD-BB4A-4D56-B3C7-5555804B5455Q30168594-D8DA8BB7-9F09-4A66-B932-BC346987439CQ30168608-EBAD63D8-63FE-4419-B6E4-42CA76A14013Q30176191-7648ABBB-2C7E-4C6C-8629-99B7CF27F560Q30176693-87C06BEA-E3E4-4DB2-AA8E-F1BEAFD7CF69Q30176696-E8F9507E-48EB-474E-976D-11FEA101D98DQ30194119-997C89DF-DA88-4EEC-9106-B0C7FF16E6A7Q30372772-B0A39DDD-E794-4470-9E80-1E8A12D4E00AQ33446486-619B4619-DE10-4C26-890D-195F44EEEB83Q33540721-AB42E608-3E91-45C0-A6B4-385F2235B217Q34117470-72D6758F-9D68-438D-956A-52395A9AE984Q34159340-BD2253F5-6D28-4E9C-A9B5-5CF118F4FD10Q34316073-1DC177F8-6A6E-4413-ACC7-3BBFD6EA67D6Q34386319-6466E6A9-2840-4C2E-B4CA-363F3BB05E20Q34406048-32E46071-EE5D-4930-91B2-35459A260FA2Q34559630-4EB8D753-FBD4-4D18-AB6C-8C202B3C89D3Q34681895-EFE988F7-0D3B-48DC-B7A6-DDF36697D160Q34722000-C2EBA240-C9ED-4EE5-8F14-F04C50874D91Q34798196-86672154-18A3-4426-AE5D-ABB75B0CDEDAQ35033817-6EC212F1-17FE-466C-BE00-0010FFA1E28DQ35516397-AD186639-892A-4420-B4DB-93AEC03BC150Q35629926-A24354DE-B267-4A84-8C21-04575CBB1236Q35673331-B7F0A3DA-805A-4CFD-BBF2-A32FC876DC69
P50
description
Zweeds onderzoeker
@nl
forsker
@nb
researcher ORCID ID = 0000-0003-1907-3392
@en
name
C. I. EDVARD SMITH
@ast
C. I. EDVARD SMITH
@nl
C. I. EDVARD SMITH
@sl
C. I. Edvard Smith
@en
C. I. Edvard Smith
@nb
Smith Cie
@es
type
label
C. I. EDVARD SMITH
@ast
C. I. EDVARD SMITH
@nl
C. I. EDVARD SMITH
@sl
C. I. Edvard Smith
@en
C. I. Edvard Smith
@nb
Smith Cie
@es
altLabel
C. I. EDVARD SMITH
@en
CIE Smith
@en
Smith CI
@en
Smith Cie
@en
prefLabel
C. I. EDVARD SMITH
@ast
C. I. EDVARD SMITH
@nl
C. I. EDVARD SMITH
@sl
C. I. Edvard Smith
@en
C. I. Edvard Smith
@nb
Smith Cie
@es
P106
P21
P27
P31
P496
0000-0003-1907-3392