BTKbase: the mutation database for X-linked agammaglobulinemia

The gene involved in X-linked agammaglobulinaemia is a member of the src family of protein-tyrosine kinases

Vetrie, D. L. P., Vořechovský, I., Sideras, P., Holland, J., Davies, A. F., Flinter, F. A., Hammarström, L. L. G., Kinnon, C., Levinsky, R. J., Bobrow, M., et al. (1993) · Nature · doi:10.1038/361226a0 · Cited by 1,460 · see citing works

Deficient expression of a B cell cytoplasmic tyrosine kinase in human X-linked agammaglobulinemia

Tsukada, S., Saffran, D. C., Rawlings, D. J., Parolini, O., Allen, R. C., Klisak, I. J., Sparkes, R. S., Kubagawa, H., Mohandas, T. K., Quan, S. G., et al. (1993) · Cell · doi:10.1016/0092-8674(93)90667-f · Cited by 1,326 · see citing works

Diagnostic Criteria for Primary Immunodeficiencies

Conley, M. E., Notarangelo, L. D., & Etzioni, A. (1999) · Clinical Immunology · doi:10.1006/clim.1999.4799 · Cited by 1,044 · see citing works

SNPs, protein structure, and disease

Wang, Z., & Moult, J. (2001) · Human Mutation · doi:10.1002/humu.22 · Cited by 726 · see citing works

Distinct specificity in the recognition of phosphoinositides by the pleckstrin homology domains of dynamin and Bruton's tyrosine kinase.

Salim, K., Bottomley, M. J., Querfurth, E., Zvelebil, M., Gout, I. T., Scaife, R. M., Margolis, R. L., Gigg, R., Smith, C. I., Driscoll, P. C., et al. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb01014.x · Cited by 558 · see citing works

Loss of Protein Structure Stability as a Major Causative Factor in Monogenic Disease

Yue, P., Li, Z. A., & Moult, J. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.08.020 · Cited by 518 · see citing works

Activation of BTK by a Phosphorylation Mechanism Initiated by SRC Family Kinases

Rawlings, D. J., Scharenberg, A. M., Park, H., Wahl, M. I., Lin, S., Kato, R. M., Fluckiger, A.-C., Witte, O. N., & Kinet, J. (1996) · Science · doi:10.1126/science.271.5250.822 · Cited by 444 · see citing works

Regulation of Btk Function by a Major Autophosphorylation Site Within the SH3 Domain

Park, H., Wahl, M. I., Afar, D., Turck, C. W., Rawlings, D. J., Tam, C. C., Scharenberg, A. M., Kinet, J., & Witte, O. N. (1996) · Immunity · doi:10.1016/s1074-7613(00)80417-3 · Cited by 323 · see citing works

The Tec family of cytoplasmic tyrosine kinases: mammalian Btk, Bmx, Itk, Tec, Txk and homologs in other species

Smith, C. I. E., Islam, T. C., Mattsson, P. T., Mohamed, A. J., Nore, B. F., & Vihinen, M. (2001) · BioEssays · doi:10.1002/bies.1062 · Cited by 316 · see citing works

Expression of Bruton's agammaglobulinemia tyrosine kinase gene, BTK, is selectively down-regulated in T lymphocytes and plasma cells.

Smith, C. I. E., Baskin, B., Humire-Greiff, P., Zhou, J., Olsson, P. G., Maniar, H. S., Kjellén, P., Lambris, J. D., Christensson, B., Hammarström, L. L. G., et al. (1994) · The Journal of Immunology · doi:10.4049/jimmunol.152.2.557 · Cited by 308 · see citing works

SRS—an indexing and retrieval tool for flat file data libraries

Etzold, T., & Argos, P. (1993) · Computer applications in the biosciences · doi:10.1093/bioinformatics/9.1.49 · Cited by 278 · see citing works

p53 Website and analysis of p53 gene mutations in human cancer: Forging a link between epidemiology and carcinogenesis

Soussi, T., Dehouche, K., & Béroud, C. (2000) · Human Mutation · doi:10.1002/(sici)1098-1004(200001)15:1 · Cited by 269 · see citing works

Structure of the PH domain and Btk motif from Bruton's tyrosine kinase: molecular explanations for X‐linked agammaglobulinaemia

Hyvönen, M., & Saraste, M. (1997) · The EMBO Journal · doi:10.1093/emboj/16.12.3396 · Cited by 241 · see citing works

Bruton's tyrosine kinase: cell biology, sequence conservation, mutation spectrum, siRNA modifications, and expression profiling

Lindvall, J. M., Blomberg, K. E. M., Väliaho, J., Vargas, L., Heinonen, J. E., Berglöf, A., Mohamed, A. J., Nore, B. F., Vihinen, M., & Smith, C. I. E. (2005) · Immunological Reviews · doi:10.1111/j.0105-2896.2005.00225.x · Cited by 199 · see citing works

X-Linked Hypogammaglobulinemia and Isolated Growth Hormone Deficiency

Fleisher, T. A., White, R. M., Broder, S. E., Nissley, S. P., Blaese, R. M., Mulvihill, J. J., Olive, G., & Waldmann, T. A. (1980) · New England Journal of Medicine · doi:10.1056/nejm198006263022601 · Cited by 177 · see citing works

A congenital mutation of the novel gene LRRC8 causes agammaglobulinemia in humans

Sawada, A., Takihara, Y., Kim, J. Y., Matsuda-Hashii, Y., Tokimasa, S., Fujisaki, H., Kubota, K., Endo, H., Onodera, T., Ohta, H., et al. (2003) · Journal of Clinical Investigation · doi:10.1172/jci18937 · Cited by 165 · see citing works

BTKbase, mutation database for X-linked agammaglobulinemia (XLA)

Vihinen, M. (1998) · Nucleic Acids Research · doi:10.1093/nar/26.1.242 · Cited by 149 · see citing works

Primary Immunodeficiency Diseases: A Molecular and Genetic Approach

Holland, S. M., & Fleisher, T. A. (1999) · Clinical Immunology · doi:10.1006/clim.1999.4715 · Cited by 146 · see citing works

Molecular and Cellular Aspects of X-Linked Agammaglobulinemia

Sideras, P., & Smith, C. I. E. (1995) · Advances in immunology · doi:10.1016/s0065-2776(08)60631-8 · Cited by 144 · see citing works

Interaction between the Btk PH Domain and Phosphatidylinositol-3,4,5-trisphosphate Directly Regulates Btk

Saito, K., Scharenberg, A. M., & Kinet, J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100873200 · Cited by 137 · see citing works

Mutation Screening of the BTK Gene in 56 Families With X-Linked Agammaglobulinemia (XLA): 47 Unique Mutations Without Correlation to Clinical Course

Holinski‐Feder, E., Weiss, M., Brandau, O., Jedele, K. B., Nore, B. F., Bäckesjö, C., Vihinen, M., Hubbard, S. R., Belohradsky, B. H., Smith, C. I. E., et al. (1998) · PEDIATRICS · doi:10.1542/peds.101.2.276 · Cited by 127 · see citing works

Immunodeficiency mutation databases (IDbases)

Piirilä, H., Väliaho, J., & Vihinen, M. (2006) · Human Mutation · doi:10.1002/humu.20405 · Cited by 124 · see citing works

Crystal Structure of Bruton's Tyrosine Kinase Domain Suggests a Novel Pathway for Activation and Provides Insights into the Molecular Basis of X-linked Agammaglobulinemia

Chen, M., Zhou, M., & Uckun, F. M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104828200 · Cited by 105 · see citing works

A genotype-phenotype correlation study in a group of 54 patients with X-linked agammaglobulinemia

López‐Granados, E., de Diego, R. P., Cerdán, A. F., Casariego, G. F., & Rodríguez, M. C. G. (2005) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2005.04.043 · Cited by 103 · see citing works

Genotype/phenotype correlations in X-linked agammaglobulinemia

Broides, A., Yang, W., & Conley, M. E. (2005) · Clinical Immunology · doi:10.1016/j.clim.2005.10.007 · Cited by 95 · see citing works

BTKbase: a database of XLA-causing mutations

Vihinen, M. (1995) · Immunology Today · doi:10.1016/0167-5699(95)80027-1 · Cited by 86 · see citing works

Structural basis for chromosome X-linked agammaglobulinemia: a tyrosine kinase disease.

Vihinen, M., Vetrie, D. L. P., Maniar, H. S., Ochs, H. D., Zhu, Q., Vořechovský, I., WEBSTER, A. D. B., Notarangelo, L. D., Nilsson, L., & Sowadski, J. M. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.26.12803 · Cited by 84 · see citing works

DNA-based mutation analysis of Bruton's tyrosine kinase gene in patients with X-linked agammaglobulinaemia

Vořechovský, I., Vihinen, M., Basile, G. D. S., Honsova, S., Hammarström, L. L. G., Müller, S., Nilsson, L., Fischer, A., & Smith, C. I. E. (1995) · Human Molecular Genetics · doi:10.1093/hmg/4.1.51 · Cited by 84 · see citing works

Deletion within the Src homology domain 3 of Bruton's tyrosine kinase resulting in X-linked agammaglobulinemia (XLA).

Zhu, Q., Zhang, M., Rawlings, D. J., Vihinen, M., Hagemann, T. L., Saffran, D. C., Kwan, S., Nilsson, L., Smith, C. I., Witte, O. N., et al. (1994) · The Journal of Experimental Medicine · doi:10.1084/jem.180.2.461 · Cited by 82 · see citing works

Conformation of full‐length Bruton tyrosine kinase (Btk) from synchrotron X‐ray solution scattering

Márquez, J. A., Smith, C. I. E., Petoukhov, M. V., Surdo, P. L., Mattsson, P. T., Knekt, M., Westlund, A., Scheffzek, K., Saraste†, M., & Svergun, D. I. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg448 · Cited by 77 · see citing works

Solution Structure of the SH3 Domain from Bruton's Tyrosine Kinase,

Hansson, H., Mattsson, P. T., Allard, P., Haapaniemi, P., Vihinen, M., Smith, C. I. E., & Härd, T. (1998) · Biochemistry · doi:10.1021/bi972409f · Cited by 76 · see citing works

Sequence specificity in CpG mutation hotspots

Ollila, J., Lappalainen, I., & Vihinen, M. (1996) · FEBS Letters · doi:10.1016/0014-5793(96)01075-7 · Cited by 70 · see citing works

KinMutBase: A registry of disease-causing mutations in protein kinase domains

Ortutay, C., Väliaho, J., Stenberg, K., & Vihinen, M. (2005) · Human Mutation · doi:10.1002/humu.20166 · Cited by 63 · see citing works

MUTbase: maintenance and analysis of distributed mutation databases.

Riikonen, P. T., & Vihinen, M. (1999) · Bioinformatics · doi:10.1093/bioinformatics/15.10.852 · Cited by 63 · see citing works

Structural Basis for Pleckstrin Homology Domain Mutations in X-Linked Agammaglobulinemia

Vihinen, M., Zvelebil, M., Zhu, Q., Brooimans, R. A., Ochs, H. D., ZEGERS, B. J. M., Nilsson, L., Waterfield, M. D., & Smith, C. I. E. (1995) · Biochemistry · doi:10.1021/bi00005a002 · Cited by 60 · see citing works

Identification of Btk mutations in 20 unrelated patients with X-Iinked agammaglobulinaemia (XLA)

Jin, H., WEBSTER, A. D. B., Vihinen, M., Sideras, P., Vorechovsky, L., Hammarström, L. L. G., Bernatowska, E. A., Smith, C. I. E., Bobrow, M., & Vetrie, D. L. P. (1995) · Human Molecular Genetics · doi:10.1093/hmg/4.4.693 · Cited by 56 · see citing works

Conservation and covariance in PH domain sequences: physicochemical profile and information theoretical analysis of XLA-causing mutations in the Btk PH domain

Shen, B., & Vihinen, M. (2004) · Protein Engineering Design and Selection · doi:10.1093/protein/gzh030 · Cited by 55 · see citing works

Lindvall, J. M. et al. Bruton's tyrosine kinase: cell biology, sequence conservation, mutation spectrum, siRNA modifications, and expression profiling. Immunol. Rev. 203, 200-215

Lindvall, J. M., Väliaho, J., Blomberg, K. E. M., Vargas, L., Heinonen, J. E., Berglöf, A., Mohamed, A. J., Nore, B. F., Vihinen, M., & Rjh, S. (2005) · Cited by 52 · see citing works

Regulation of Bruton Tyrosine Kinase by the Peptidylprolyl Isomerase Pin1

Yu, L., Mohamed, A. J., Vargas, L., Berglöf, A., Finn, G., Lu, K. P., & Smith, C. I. E. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603090200 · Cited by 49 · see citing works

Two novel mutations of theFMO3 gene in a proband with trimethylaminuria

Akerman, B. R., Forrest, S. M., Chow, L., Youil, R., Knight, M. A., & Treacy, E. P. (1999) · Human Mutation · doi:10.1002/(sici)1098-1004(1999)13:5 · Cited by 45 · see citing works

Structural Basis of SH2 Domain Mutations in X-Linked Agammaglobulinemia

Vihinen, M., Nilsson, L., & Smith, C. I. E. (1994) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1994.2802 · Cited by 44 · see citing works

Pleckstrin Homology Domains of Tec Family Protein Kinases

Okoh, M. P., & Vihinen, M. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.1407 · Cited by 42 · see citing works

Missense mutations affecting a conserved cysteine pair in the TH domain of Btk

Vihinen, M., Nore, B. F., Mattsson, P. T., Bäckesjö, C., Nars, M., Koutaniemi, S., Watanabe, C., Lester, T., Jones, A., Ochs, H. D., et al. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00912-5 · Cited by 41 · see citing works

BTKbase, mutation database for X-linked agammaglobulinemia (XLA)

Vihinen, M., Belohradsky, B. H., Haire, R. N., Holinski‐Feder, E., Kwan, S., Lappalainen, I., Lehväslaiho, H., Lester, T., Meindl, A., Ochs, H. D., et al. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.1.166 · Cited by 38 · see citing works

Six X-Linked Agammaglobulinemia-Causing Missense Mutations in the Src Homology 2 Domain of Bruton’s Tyrosine Kinase: Phosphotyrosine-Binding and Circular Dichroism Analysis

Mattsson, P. T., Lappalainen, I., Bäckesjö, C., Brockmann, E., Laurén, S., Vihinen, M., & Smith, C. I. E. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.164.8.4170 · Cited by 37 · see citing works

XLA Patients with BTK Splice-Site Mutations Produce Low Levels of Wild-Type BTK Transcripts

Noordzij, J. G., de Bruin-Versteeg, S., Hartwig, N. G., Weemaes, C. M. R., Gerritsen, E. J. A., Bernatowska, E. A., Lierde, S. V., de Groot, R., & van Dongen, J. J. M. (2002) · Journal of Clinical Immunology · doi:10.1023/a:1019982206951 · Cited by 33 · see citing works

X-linked agammaglobulinemia: lack of mature B lineage cells caused by mutations in the Btk kinase

Smith, C. I. E., B�ckesj�, C.-M., Bergl�f, A., Brandén, L. J., Islam, T., Mattsson, P. T., Mohamed, A. J., M�ller, S., Nore, B. F., & Vihinen, M. (1998) · Springer Seminars in Immunopathology · doi:10.1007/bf00792597 · Cited by 31 · see citing works

Genes required for B cell development

Conley, M. E. (2003) · Journal of Clinical Investigation · doi:10.1172/jci200320408 · Cited by 26 · see citing works

Immunodeficiency mutation databases

Väliaho, J., Hershfield, M. S., Notarangelo, L. D., Regueiro, Roos, D., Rjh, S., VILLA, A. M., & Vihinen, M. (2000) · Lund University Publications (Lund University) · Cited by 24 · see citing works

IDR: the ImmunoDeficiency Resource

Väliaho, J. (2002) · Nucleic Acids Research · doi:10.1093/nar/30.1.232 · Cited by 23 · see citing works

Molecular and Structural Characterization of Five Novel Mutations in the Bruton’s Tyrosine Kinase Gene from Patients with X-Linked Agammaglobulinemia

Saha, B. K., Curtis, S. K., Vogler, L. B., & Vihinen, M. (1997) · Molecular Medicine · doi:10.1007/bf03401694 · Cited by 22 · see citing works

Analysis of Btk Mutations in Patients with X‐Linked Agammaglobulinaemia (XLA) and Determination of Carrier Status in Normal Female Relatives: a Nationwide Study of Btk Deficiency in Greece

Speletas, M. G., Kanariou, M. G., Kanakoudi‐Tsakalidou, F., Papadopoulou‐Alataki, E., Arvanitidis, K. I., Pardali, E., Constantopoulos, A., Kartalis, G., Vihinen, M., Sideras, P., et al. (2001) · Scandinavian Journal of Immunology · doi:10.1046/j.1365-3083.2001.00967.x · Cited by 21 · see citing works

Online Registry of Genetic and Clinical Immunodeficiency Diagnostic Laboratories, IDdiagnostics

Samarghitean, C., Väliaho, J., & Vihinen, M. (2004) · Journal of Clinical Immunology · doi:10.1023/b:joci.0000018063.55963.0c · Cited by 21 · see citing works

Structural basis for X-linked agammaglobulinemia (XLA): mutations at interacting Btk residues R562, W563, and A582

Maniar, H. S., Vihinen, M., WEBSTER, A. D. B., Nilsson, L., & Smith, C. I. E. (1995) · Clinical Immunology and Immunopathology · doi:10.1016/s0090-1229(95)90216-3 · Cited by 11 · see citing works

Structure‐Function Effects in Primary Immunodeficiencies

Korpi, Väliaho, & Vihinen (2000) · Scandinavian Journal of Immunology · doi:10.1046/j.1365-3083.2000.00799.x · Cited by 10 · see citing works

Primary Immunodeficiencies: Genotype–Phenotype Correlations

Vihinen, M., & Durandy, A. (2005) · doi:10.1002/0470034092.ch20 · Cited by 10 · see citing works

B lymphocytes: how they develop and function

LeBien, T. W., & Tedder, T. F. (2008) · Blood · doi:10.1182/blood-2008-02-078071 · Cited by 1,400 · see citing works

Resistance Mechanisms for the Bruton's Tyrosine Kinase Inhibitor Ibrutinib

Woyach, J. A., Furman, R. R., Liu, T.-M., Ozer, H. G., Zapatka, M., Ruppert, A. S., Xue, L., Li, D. H.-H., Steggerda, S. M., Versele, M., et al. (2014) · New England Journal of Medicine · doi:10.1056/nejmoa1400029 · Cited by 1,275 · see citing works

Targeting Bruton's tyrosine kinase in B cell malignancies

Hendriks, R. W., Yuvaraj, S., & Kil, L. P. (2014) · Nature reviews. Cancer · doi:10.1038/nrc3702 · Cited by 564 · see citing works

Bruton’s tyrosine kinase (Btk): function, regulation, and transformation with special emphasis on the PH domain

Mohamed, A. J., Yu, L., Bäckesjö, C., Vargas, L., Faryal, R., Aints, A., Christensson, B., Berglöf, A., Vihinen, M., Nore, B. F., et al. (2009) · Immunological Reviews · doi:10.1111/j.1600-065x.2008.00741.x · Cited by 516 · see citing works

Primary B Cell Immunodeficiencies: Comparisons and Contrasts

Conley, M. E., Dobbs, K., Farmer, D. M., Kilic, S., Paris, K., Grigoriadou, S., Coustan‐Smith, E., Howard, V. C., & Campana, D. (2009) · Annual Review of Immunology · doi:10.1146/annurev.immunol.021908.132649 · Cited by 429 · see citing works

Bruton’s Tyrosine Kinase: An Emerging Key Player in Innate Immunity

Weber, A. N. R., Bittner, Z., Liu, X., Dang, T., Radsak, M. P., & Brunner, C. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.01454 · Cited by 271 · see citing works

Second-generation inhibitors of Bruton tyrosine kinase

Wu, J., Liu, C., Tsui, S. T., & Liu, D. (2016) · Journal of Hematology & Oncology · doi:10.1186/s13045-016-0313-y · Cited by 216 · see citing works

Bruton tyrosine kinase inhibitors for multiple sclerosis

Krämer, J., Bar-Or, A., Turner, T. J., & Wiendl, H. (2023) · Nature Reviews Neurology · doi:10.1038/s41582-023-00800-7 · Cited by 206 · see citing works

Recurrent somatic mutations affecting B-cell receptor signaling pathway genes in follicular lymphoma

Krysiak, K., Gomez, F., White, B. S., Matlock, M. K., Miller, C. A., Trani, L., Fronick, C. C., Fulton, R. S., Kreisel, F. H. C., Cashen, A. F., et al. (2016) · Blood · doi:10.1182/blood-2016-07-729954 · Cited by 183 · see citing works

The Genetic Theory of Infectious Diseases: A Brief History and Selected Illustrations

Casanova, J., & Abel, L. (2013) · Annual Review of Genomics and Human Genetics · doi:10.1146/annurev-genom-091212-153448 · Cited by 176 · see citing works

Structures of human Bruton's tyrosine kinase in active and inactive conformations suggest a mechanism of activation for TEC family kinases

Marcotte, D. J., Liu, Y., Arduini, R. M., Hession, C. A., Miatkowski, K., Wildes, C. P., Cullen, P. F., Hong, V. S., Hopkins, B. T., Mertsching, E., et al. (2010) · Protein Science · doi:10.1002/pro.321 · Cited by 158 · see citing works

The role of Bruton’s tyrosine kinase in autoimmunity and implications for therapy

Crofford, L. J., Nyhoff, L. E., Sheehan, J. H., & Kendall, P. L. (2016) · Expert Review of Clinical Immunology · doi:10.1586/1744666x.2016.1152888 · Cited by 142 · see citing works

Loss-of-function mutations within the IL-2 inducible kinase ITK in patients with EBV-associated lymphoproliferative diseases

Linka, R. M., Risse, S. L., Bienemann, K., Werner, M., Linka, Y., Krux, F., Synaeve, C., Deenen, R., Ginzel, S., Dvorský, R., et al. (2012) · Leukemia · doi:10.1038/leu.2011.371 · Cited by 136 · see citing works

Toll-Like Receptors and B-Cell Receptors Synergize to Induce Immunoglobulin Class-Switch DNA Recombination: Relevance to Microbial Antibody Responses

Pone, E. J., Zan, H., Zhang, J., Al-Qahtani, A. A., Xu, Z., & Casali, P. (2010) · Critical Reviews in Immunology · doi:10.1615/critrevimmunol.v30.i1.10 · Cited by 134 · see citing works

Dual Functions of Bruton’s Tyrosine Kinase and Tec Kinase during Fcγ Receptor-Induced Signaling and Phagocytosis

Jongstra‐Bilen, J., Cano, A. P., Hasija, M., Xiao, H., Smith, C. I. E., & Cybulsky, M. I. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.181.1.288 · Cited by 132 · see citing works

Spectrum of disease-causing mutations in protein secondary structures

Khan, S., & Vihinen, M. (2007) · BMC Structural Biology · doi:10.1186/1472-6807-7-56 · Cited by 125 · see citing works

Bruton's Tyrosine Kinase: From X-Linked Agammaglobulinemia Toward Targeted Therapy for B-Cell Malignancies

Ponader, S., & Burger, J. A. (2014) · Journal of Clinical Oncology · doi:10.1200/jco.2013.53.1046 · Cited by 123 · see citing works

Immunodeficiency mutation databases (IDbases)

Piirilä, H., Väliaho, J., & Vihinen, M. (2006) · Human Mutation · doi:10.1002/humu.20405 · Cited by 124 · see citing works

Primary Immunodeficiency and Autoimmunity: Lessons From Human Diseases

Arason, G. J., Jörgensen, G. H., & Ludviksson, B. R. (2010) · Scandinavian Journal of Immunology · doi:10.1111/j.1365-3083.2010.02386.x · Cited by 113 · see citing works

Bruton's tyrosine kinase—an integral protein of B cell development that also has an essential role in the innate immune system

López‐Herrera, G., Vargas‐Hernández, A., González-Serrano, M. E., Berrón‐Ruiz, L., Rodríguez‐Alba, J. C., Espinosa-Rosales, F. J., & Santos‐Argumedo, L. (2013) · Journal of Leukocyte Biology · doi:10.1189/jlb.0513307 · Cited by 107 · see citing works

Genetic predispositions to childhood leukemia

Stieglitz, E., & Loh, M. L. (2013) · Therapeutic Advances in Hematology · doi:10.1177/2040620713498161 · Cited by 101 · see citing works

Clinical Targeting of Mutated and Wild-Type Protein Tyrosine Kinases in Cancer

Drake, J. M., Lee, J. K., & Witte, O. N. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.01592-13 · Cited by 93 · see citing works

The Src module: an ancient scaffold in the evolution of cytoplasmic tyrosine kinases

Shah, N. H., Amacher, J. F., Nocka, L. M., & Kuriyan, J. (2018) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2018.1495173 · Cited by 91 · see citing works

Long-term follow-up of 168 patients with X-linked agammaglobulinemia reveals increased morbidity and mortality

Lougaris, V., Soresina, A., Baronio, M., Montin, D., Martino, S., Signa, S., Volpi, S., Zecca, M., Marinoni, M., Baselli, L. A., et al. (2020) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2020.03.001 · Cited by 86 · see citing works

Nationwide Survey of Patients with Primary Immunodeficiency Diseases in Japan

Ishimura, M., Takada, H., Doi, T., Imai, K., Sasahara, Y., Kanegane, H., Nishikomori, R., Morio, T., Heike, T., Kobayashi, M., et al. (2011) · Journal of Clinical Immunology · doi:10.1007/s10875-011-9594-7 · Cited by 86 · see citing works

Clinical Characteristics and Genotype-phenotype Correlation in 62 Patients with X-linked Agammaglobulinemia

Lee, P. P. W., Chen, T., Jiang, L., Chan, K. W., Yang, W., Lee, B.-W., Chiang, W.-C., Chen, X., Fok, S. F. S., Lee, T.-L., et al. (2009) · Journal of Clinical Immunology · doi:10.1007/s10875-009-9341-5 · Cited by 84 · see citing works

Sequence and Structure Signatures of Cancer Mutation Hotspots in Protein Kinases

Dixit, A., Yi, L., Gowthaman, R., Torkamani, A., Schork, N. J., & Verkhivker, G. M. (2009) · PLoS ONE · doi:10.1371/journal.pone.0007485 · Cited by 81 · see citing works

Inhibitors of BTK and ITK : State of the New Drugs for Cancer, Autoimmunity and Inflammatory Diseases

Vargas, L., Hamasy, A., Nore, B. F., & Smith, C. I. E. (2013) · Scandinavian Journal of Immunology · doi:10.1111/sji.12069 · Cited by 77 · see citing works

Primary B-cell immunodeficiencies

Smith, T., & Cunningham‐Rundles, C. (2018) · Human Immunology · doi:10.1016/j.humimm.2018.10.015 · Cited by 77 · see citing works

Structure-Function Relationships of Covalent and Non-Covalent BTK Inhibitors

Zain, R., & Vihinen, M. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.694853 · Cited by 74 · see citing works

Neutropenia and Primary Immunodeficiency Diseases

Rezaei, N., Moazzami, K., Aghamohammadi, A., & Klein, C. (2009) · International Reviews of Immunology · doi:10.1080/08830180902995645 · Cited by 67 · see citing works

Resistance Mutations to BTK Inhibitors Originate From the NF-κB but Not From the PI3K-RAS-MAPK Arm of the B Cell Receptor Signaling Pathway

Smith, C. I. E., & Burger, J. A. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.689472 · Cited by 68 · see citing works

Substitution scanning identifies a novel, catalytically active ibrutinib-resistant BTK cysteine 481 to threonine (C481T) variant

Hamasy, A., Wang, Q., Blomberg, K. E. M., Mohammad, D. K., Yu, L., Vihinen, M., Berglöf, A., & Smith, C. I. E. (2017) · Leukemia · doi:10.1038/leu.2016.153 · Cited by 62 · see citing works

Genome wide analysis of pathogenic SH2 domain mutations

Lappalainen, I., Thusberg, J., Shen, B., & Vihinen, M. (2008) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21970 · Cited by 61 · see citing works

SH2 Domains: Folding, Binding and Therapeutical Approaches

Diop, A., Santorelli, D., Malagrinò, F., Nardella, C., Pennacchietti, V., Pagano, L., Marcocci, L., Pietrangeli, P., Gianni, S., & Toto, A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232415944 · Cited by 60 · see citing works

The Energy Landscape Analysis of Cancer Mutations in Protein Kinases

Dixit, A., & Verkhivker, G. M. (2011) · PLoS ONE · doi:10.1371/journal.pone.0026071 · Cited by 56 · see citing works

From identification of the BTK kinase to effective management of leukemia

Smith, C. I. E. (2016) · Oncogene · doi:10.1038/onc.2016.343 · Cited by 56 · see citing works

Btk is a positive regulator in the TREM-1/DAP12 signaling pathway

Ormsby, T., Schlecker, E., Ferdin, J., Tessarz, A. S., Angelisová, P., Köprülü, A. D., Borte, M., Warnatz, K., Schulze, I., Ellmeier, W., et al. (2011) · Blood · doi:10.1182/blood-2010-11-317016 · Cited by 49 · see citing works

Increased expression of Bruton’s tyrosine kinase in peripheral blood is associated with lupus nephritis

Kong, W., Deng, W., Sun, Y., Huang, S., Zhang, Z., Shi, B., Chen, W., Tang, X., Yao, G., Feng, X., et al. (2017) · Clinical Rheumatology · doi:10.1007/s10067-017-3717-3 · Cited by 49 · see citing works

Millisecond dynamics of BTK reveal kinome-wide conformational plasticity within the apo kinase domain

Sultan, M. M., Denny, R., Unwalla, R., Lovering, F., & Pande, V. (2017) · Scientific Reports · doi:10.1038/s41598-017-10697-0 · Cited by 50 · see citing works

Splice-correcting oligonucleotides restore BTK function in X-linked agammaglobulinemia model

Bestas, B., Moreno, P. M. D., Blomberg, K. E. M., Mohammad, D. K., Saleh, A. F. A., Sütlü, T., Nordin, J. Z., Guterstam, P., Gustafsson, M. O., Kharazi, S., et al. (2014) · Journal of Clinical Investigation · doi:10.1172/jci76175 · Cited by 48 · see citing works

TEC family kinases in health and disease – loss‐of‐function of BTK and ITK and the gain‐of‐function fusions ITK–SYK and BTK–SYK

Hussain, A., Yu, L., Faryal, R., Mohammad, D. K., Mohamed, A. J., & Smith, C. I. E. (2011) · FEBS Journal · doi:10.1111/j.1742-4658.2011.08134.x · Cited by 50 · see citing works

BMX and Its Role in Inflammation, Cardiovascular Disease, and Cancer

Cenni, B., Gutmann, S., & Gottar, M. (2012) · International Reviews of Immunology · doi:10.3109/08830185.2012.663838 · Cited by 47 · see citing works

The structural basis of hyper IgM deficiency – CD40L mutations

Thusberg, J., & Vihinen, M. (2007) · Protein Engineering Design and Selection · doi:10.1093/protein/gzm004 · Cited by 46 · see citing works

Btk SH2-kinase interface is critical for allosteric kinase activation and its targeting inhibits B-cell neoplasms

Duarte, D., Lamontanara, A. J., Sala, G. L., Jeong, S., Sohn, Y., Panjkovich, A., Georgeon, S., Kükenshöner, T., Marcaida, M. J., Pojer, F., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-16128-5 · Cited by 46 · see citing works

Characterization of All Possible Single-Nucleotide Change Caused Amino Acid Substitutions in the Kinase Domain of Bruton Tyrosine Kinase

Väliaho, J., Faisal, I., Ortutay, C., Smith, C. I. E., & Vihinen, M. (2015) · Human Mutation · doi:10.1002/humu.22791 · Cited by 43 · see citing works

Elevated cytokine production restores bone resorption by human Btk-deficient osteoclasts

Danks, L., Workman, S., Webster, D., & Horwood, N. J. (2010) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.210 · Cited by 41 · see citing works

X-linked agammaglobulinemia diagnosed late in life: case report and review of the literature

Sigmon, J. R., Kasasbeh, E. S., & Krishnaswamy, G. A. (2008) · Clinical and Molecular Allergy · doi:10.1186/1476-7961-6-5 · Cited by 41 · see citing works

Contiguous X-chromosome Deletion Syndrome Encompassing the BTK, TIMM8A, TAF7L, and DRP2 Genes

Šedivá, A., Smith, C. I. E., Asplund, A. C., Hadač, J., Janda, A., Zeman, J., Hansíková, H., Dvořáková, L., Mrazova, L. S., Velbri, S., et al. (2007) · Journal of Clinical Immunology · doi:10.1007/s10875-007-9123-x · Cited by 41 · see citing works

Bruton's tyrosine kinase is dispensable for the Toll-like receptor-mediated activation of mast cells

Zorn, C. N., Keck, S., Hendriks, R. W., Leitges, M., Freudenberg, M. A., & Huber, M. (2008) · Cellular Signalling · doi:10.1016/j.cellsig.2008.09.010 · Cited by 38 · see citing works

Predominantly Antibody Deficiencies

Aghamohammadi, A., Lougaris, V., Plebani, A., Miyawaki, T., Durandy, A., & Hammarström, L. L. G. (2008) · Springer eBooks · doi:10.1007/978-3-540-78936-9_3 · Cited by 38 · see citing works

The Tyrosine Kinase BMX Is an Essential Mediator of Inflammatory Arthritis in a Kinase-Independent Manner

Gottar, M., Dodeller, F., Huesken, D., Iourgenko, V., Mickanin, C., Labow, M., Gaveriaux, S., Kinzel, B., Müeller, M., Alitalo, K. K., et al. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1002813 · Cited by 36 · see citing works

Activation Loop Dynamics Determine the Different Catalytic Efficiencies of B Cell– and T Cell–Specific Tec Kinases

Joseph, R. E., Kleino, I., Wales, T. E., Xie, Q., Fulton, D. B., Engen, J. R., Berg, L. J., & Andreotti, A. H. (2013) · Science Signaling · doi:10.1126/scisignal.2004298 · Cited by 36 · see citing works

Phylogeny of Tec Family Kinases: Identification of a Premetazoan Origin of Btk, Bmx, Itk, Tec, Txk, and the Btk Regulator SH3BP5

Ortutay, C., Nore, B. F., Vihinen, M., & Smith, C. I. E. (2008) · Advances in genetics · doi:10.1016/s0065-2660(08)00803-1 · Cited by 34 · see citing works

Genetics of hypogammaglobulinemia: what do we really know?

Conley, M. E. (2009) · Current Opinion in Immunology · doi:10.1016/j.coi.2009.07.003 · Cited by 34 · see citing works

Three Newly Approved Drugs for Chronic Lymphocytic Leukemia: Incorporating Ibrutinib, Idelalisib, and Obinutuzumab into Clinical Practice

Sanford, D., Wierda, W. G., Burger, J. A., Keating, M. J., & O'Brien, S. M. (2015) · Clinical Lymphoma Myeloma & Leukemia · doi:10.1016/j.clml.2015.02.019 · Cited by 34 · see citing works

Effects of BTK signalling in pathogenic microorganism infections

Ye, B., Zhou, C., Guo, H., & Zheng, M. (2019) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.14548 · Cited by 33 · see citing works

Agammaglobulinemia: causative mutations and their implications for novel therapies

Berglöf, A., Turunen, J. J., Gissberg, O., Bestas, B., Blomberg, K. E. M., & Smith, C. E. (2013) · Expert Review of Clinical Immunology · doi:10.1586/1744666x.2013.850030 · Cited by 32 · see citing works

Adult-onset presentations of genetic immunodeficiencies: genes can throw slow curves

Nelson, K. S., & Lewis, D. B. (2010) · Current Opinion in Infectious Diseases · doi:10.1097/qco.0b013e32833bc1b0 · Cited by 32 · see citing works

PON-Sol2: Prediction of Effects of Variants on Protein Solubility

Yang, Y., Zeng, L., & Vihinen, M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22158027 · Cited by 32 · see citing works

Differential Sensitivity to Itk Kinase Signals for T Helper 2 Cytokine Production and Chemokine-Mediated Migration

Sahu, N., Mueller, C., Fischer, A., & August, A. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.180.6.3833 · Cited by 32 · see citing works

XLA-associated Neutropenia Treatment

Jacobs, Z., Guajardo, J. R., & Anderson, K. M. (2008) · Journal of Pediatric Hematology/Oncology · doi:10.1097/mph.0b013e3181758947 · Cited by 31 · see citing works

Impact of amino acid substitution in the kinase domain of Bruton tyrosine kinase and its association with X-linked agammaglobulinemia

Mohammad, T., Amir, M., Prasad, K., Batra, S., Kumar, V., Hussain, A., Rehman, M. T., Alajmi, M. F., & Hassan, M. I. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.08.057 · Cited by 30 · see citing works

Characterization of Bruton's tyrosine kinase mutations in Mexican patients with X-linked agammaglobulinemia

López‐Herrera, G., Berrón‐Ruiz, L., Mogica‐Martínez, D., Espinosa-Rosales, F. J., & Santos‐Argumedo, L. (2007) · Molecular Immunology · doi:10.1016/j.molimm.2007.07.022 · Cited by 29 · see citing works

Bruton tyrosine kinase inhibitor ONO/GS-4059: from bench to bedside

Wu, J., Zhang, M., & Liu, D. (2016) · Oncotarget · doi:10.18632/oncotarget.12786 · Cited by 28 · see citing works

Increased Pro-inflammatory Cytokine Production After Lipopolysaccharide Stimulation in Patients with X-linked Agammaglobulinemia

González-Serrano, M. E., Estrada‐García, I., Mogica‐Martínez, D., Garay, A. G. G., López‐Herrera, G., Berrón‐Ruiz, L., Espinosa‐Padilla, S. E., Yamazaki‐Nakashimada, M. A., Vargas‐Hernández, A., Santos‐Argumedo, L., et al. (2012) · Journal of Clinical Immunology · doi:10.1007/s10875-012-9706-z · Cited by 27 · see citing works

Secondary Resistant Mutations to Small Molecule Inhibitors in Cancer Cells

Hamid, A. B., & Petreaca, R. C. (2020) · Cancers · doi:10.3390/cancers12040927 · Cited by 26 · see citing works

Neutralizing SARS-CoV-2 Antibodies in Commercial Immunoglobulin Products Give Patients with X-Linked Agammaglobulinemia Limited Passive Immunity to the Omicron Variant

Lindahl, H., Klingström, J., Rodrigues, R. D. S., Christ, W., Chen, P., Ljunggren, H., Buggert, M., Aleman, S., Smith, C. I. E., & Bergman, P. (2022) · Journal of Clinical Immunology · doi:10.1007/s10875-022-01283-9 · Cited by 25 · see citing works

A minimally hypomorphic mutation in Btk resulting in reduced B cell numbers but no clinical disease

Conley, M. E., Farmer, D. M., Dobbs, K., Howard, V., Aiba, Y., Shurtleff, S. A., & Kurosaki, T. (2008) · Clinical & Experimental Immunology · doi:10.1111/j.1365-2249.2008.03593.x · Cited by 25 · see citing works

Genotype-Phenotype Correlation in Bruton's Tyrosine Kinase Deficiency

Teimourian, S., Nasseri, S., Pouladi, N., Yeganeh, M., & Aghamohammadi, A. (2008) · Journal of Pediatric Hematology/Oncology · doi:10.1097/mph.0b013e318180bb45 · Cited by 23 · see citing works

Atypical X-linked agammaglobulinaemia caused by a novel BTK mutation in a selective immunoglobulin M deficiency patient

Lim, L., Chang, J., Wang, I.-F., Chang, W., Hwang, D., & Chen, H. (2013) · BMC Pediatrics · doi:10.1186/1471-2431-13-150 · Cited by 23 · see citing works

From development to clinical success: the journey of established and next-generation BTK inhibitors

Gupta, S., Sharma, A., Shukla, A. K., Mishra, A., & Singh, A. K. (2025) · Investigational New Drugs · doi:10.1007/s10637-025-01513-y · Cited by 24 · see citing works

Primary Immunodeficiency Disorders Among North Indian Children

Gupta, D., Thakral, D., Kumar, P., Kabra, S. K., Lodha, R., Kumari, R., Mohanty, S. K., Chakraborty, S., Bagri, N. K., & Mitra, D. K. (2019) · The Indian Journal of Pediatrics · doi:10.1007/s12098-019-02971-y · Cited by 22 · see citing works

Novel mouse model resistant to irreversible BTK inhibitors: a tool identifying new therapeutic targets and side effects

Estupiñan, H. Y., Bouderlique, T., He, C., Berglöf, A., Gupta, D., Saher, O., Cruz, M. Á. D., Peña‐Pérez, L., Yu, L., Zain, R., et al. (2020) · Blood Advances · doi:10.1182/bloodadvances.2019001319 · Cited by 22 · see citing works

Human Variome Project Quality Assessment Criteria for Variation Databases

Vihinen, M., Hancock, J. M., Maglott, D. R., Landrum, M., Schaafsma, G. C. P., & Taschner, P. E. M. (2016) · Human Mutation · doi:10.1002/humu.22976 · Cited by 21 · see citing works

X-linked agammaglobulinemia in a 10-year-old boy with a novel non-invariant splice-site mutation in Btk gene

Maekawa, K., Yamada, M., Okura, Y., Sato, Y., Yamada, Y., Kawamura, N., & Ariga, T. (2010) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2010.01.004 · Cited by 21 · see citing works

Identification of a Btk mutation in a dysgammaglobulinemic patient with reduced B cells: XLA diagnosis or not?

Graziani, S., Matteo, G. D., Benini, L., Cesare, S. D., Chiriacò, M. S., Chini, L., Chianca, M., Iorio, F. D., Rocca, M. L., Iannini, R., et al. (2008) · Clinical Immunology · doi:10.1016/j.clim.2008.05.012 · Cited by 21 · see citing works

Breaking good: the inexorable rise of BTK inhibitors in the treatment of chronic lymphocytic leukaemia

Hutchinson, C. V., & Dyer, M. J. S. (2014) · British Journal of Haematology · doi:10.1111/bjh.12895 · Cited by 20 · see citing works

Clinical and mutational features of X-linked agammaglobulinemia in Mexico

García-García, E., Staines-Boone, A. T., Vargas‐Hernández, A., González-Serrano, M. E., Carrillo‐Tapia, E., Mogica‐Martínez, D., Berrón‐Ruiz, L., Segura-Méndez, N. H., Espinosa-Rosales, F. J., Yamazaki‐Nakashimada, M. A., et al. (2016) · Clinical Immunology · doi:10.1016/j.clim.2016.02.010 · Cited by 20 · see citing works

Sex differences in susceptibility to substance use disorder: Role for X chromosome inactivation and escape?

Krueger, K., Lamenza, F. F., Gu, H. H., El‐Hodiri, H. M., Wester, J. C., Oberdick, J., Fischer, A. J., & Oghumu, S. (2023) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2023.103859 · Cited by 18 · see citing works

SH2-Dependent Autophosphorylation within the Tec Family Kinase Itk

Joseph, R. E., Severin, A. J., Min, L., Fulton, D. B., & Andreotti, A. H. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.06.023 · Cited by 18 · see citing works

Crystal structure of the Bruton’s tyrosine kinase PH domain with phosphatidylinositol

Murayama, K., Kato-Murayama, M., Mishima-Tsumagari, C., Akasaka, R., Shirouzu, M., Fukui, Y., & Yokoyama, S. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.09.055 · Cited by 18 · see citing works

Mutations in Bruton’s tyrosine kinase impair IgA responses

Mitsuiki, N., Yang, X., Bartol, S. J. W., Großerichter-Wagener, C., Kosaka, Y., Takada, H., Imai, K., Kanegane, H., Mizutani, S., van der Burg, M., et al. (2015) · International Journal of Hematology · doi:10.1007/s12185-015-1732-1 · Cited by 18 · see citing works

Splice-Correction Strategies for Treatment of X-Linked Agammaglobulinemia

Bestas, B., Turunen, J. J., Blomberg, K. E. M., Wang, Q., Månsson, R., Andaloussi, S. E., Berglöf, A., & Smith, C. I. E. (2015) · Current Allergy and Asthma Reports · doi:10.1007/s11882-014-0510-0 · Cited by 18 · see citing works

Metastatic colorectal cancer and severe hypocalcemia following irinotecan administration in a patient with X-linked agammaglobulinemia: a case report

Li, M., Chen, W., Sun, X., Wang, Z., Zou, X., Wei, H., Wang, Z., & Chen, W. (2019) · BMC Medical Genetics · doi:10.1186/s12881-019-0880-1 · Cited by 17 · see citing works

Hematopoietic stem cell gene editing rescues B-cell development in X-linked agammaglobulinemia

Bahal, S., Zinicola, M., Moula, S. E., Whittaker, T. E., Schejtman, A., Naseem, A., Blanco, E., Vetharoy, W., Hu, Y., Rai, R., et al. (2024) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2024.03.003 · Cited by 15 · see citing works

Autosomal recessive agammaglobulinemia associated with an IGLL1 gene missense mutation

Gemayel, K. T., Litman, G. W., & Sriaroon, P. (2016) · Annals of Allergy Asthma & Immunology · doi:10.1016/j.anai.2016.07.038 · Cited by 15 · see citing works

Autoimmunity in Primary Immunodeficiencies (PID)

Padron, G. T., & Hernandez-Trujillo, V. P. (2022) · Clinical Reviews in Allergy & Immunology · doi:10.1007/s12016-022-08942-0 · Cited by 15 · see citing works

Comprehensive genetic testing for primary immunodeficiency disorders in a tertiary hospital: 10-year experience in Auckland, New Zealand

Woon, S., & Ameratunga, R. (2016) · Allergy Asthma and Clinical Immunology · doi:10.1186/s13223-016-0169-2 · Cited by 14 · see citing works

Phylogenetic Profiles Reveal Structural and Functional Determinants of Lipid-binding

Hong, Y., Chalkia, D., Ko, K. D., Bhardwaj, G., Chang, G. S., van Rossum, D. B., & Patterson, R. L. (2009) · Journal of Proteomics & Bioinformatics · doi:10.4172/jpb.1000071 · Cited by 13 · see citing works

Clinical and genetic features of the patients with X‐Linked agammaglobulinemia from Turkey: Single‐centre experience

Esenboğa, S., Cağdaş, D. N., Ozgur, T. T., Çetinkaya, P. G., Turkdemir, L. M., Sanal, Ö., VanDerBurg, M., & Tezcan, İ. (2018) · Scandinavian Journal of Immunology · doi:10.1111/sji.12647 · Cited by 13 · see citing works

Tubulointerstitial nephritis complicating IVIG therapy for X-linked agammaglobulinemia

Sugimoto, K., Nishi, H., Miyazawa, T., Wada, N., Izu, A., Enya, T., Okada, M., & Takemura, T. (2014) · BMC Nephrology · doi:10.1186/1471-2369-15-109 · Cited by 12 · see citing works

Immunopathology and Immunomodulation

Metodiev, K. (2015) · InTech eBooks · doi:10.5772/59217 · Cited by 12 · see citing works

Uncovering Low-Level Maternal Gonosomal Mosaicism in X-Linked Agammaglobulinemia: Implications for Genetic Counseling

Riviere, J. G., Franco‐Jarava, C., Martínez‐Gallo, M., Aguiló‐Cucurull, A., Blasco, L. C., Paramonov, I., Antolı́n, M., Martín‐Nalda, A., Soler‐Palacín, P., & Colobrán, R. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.00046 · Cited by 11 · see citing works

Clinical features and mutational analysis of X-linked agammaglobulinemia patients in Malaysia

Chear, C. T., Ismail, I. H., Chan, K. C., Noh, L. M., Kassim, A., Latiff, A. H. A., Gill, S. S., Ramly, N. H., Tan, K. K., Sundaraj, C., et al. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1252765 · Cited by 10 · see citing works

Mutations of Bruton's tyrosine kinase gene in Brazilian patients with X-linked agammaglobulinemia

Ramalho, V. D., Júnior, E. B. O., Tani, S. M., Júnior, P. R., & Vilela, M. M. S. (2010) · Brazilian Journal of Medical and Biological Research · doi:10.1590/s0100-879x2010007500079 · Cited by 10 · see citing works

Primary immunodeficiency in J apan; epidemiology, diagnosis, and pathogenesis

Takada, H. (2013) · Pediatrics International · doi:10.1111/ped.12224 · Cited by 10 · see citing works

Medicinal perspectives and structure-activity relationship studies of pyrimidine based Bruton’s tyrosine kinase inhibitors as potential anticancer agents

Jha, K. T., Shome, A., Chahat, Chawla, V., & Chawla, P. A. (2023) · Process Biochemistry · doi:10.1016/j.procbio.2023.07.018 · Cited by 9 · see citing works

X-Linked Agammaglobulinemia

(2012) · Springer eBooks · doi:10.1007/978-1-4614-1037-9_248 · Cited by 9 · see citing works

X-linked Agammaglobulinemia With Normal Immunoglobulin and Near-Normal Vaccine Seroconversion

Preece, K., & Lear, G. (2015) · PEDIATRICS · doi:10.1542/peds.2014-3907 · Cited by 9 · see citing works

BTKbase, mutation database for X-linked agammaglobulinemia (XLA)

Vihinen, M. (1998) · Nucleic Acids Research · doi:10.1093/nar/26.1.242 · Cited by 149 · see citing works

WRN mutations in Werner syndrome

Moser, M. J., Oshima, J., & Monnat, R. J. (1999) · Human Mutation · doi:10.1002/(sici)1098-1004(1999)13:4 · Cited by 91 · see citing works

BTKbase: XLA-mutation registry

Vihinen, M., Brooimans, R. A., Kwan, S., Lehväslaiho, H., Litman, G. W., Ochs, H. D., Resnick, I. B., Schwaber, J. H., Vořechovský, I., & Rjh, S. (1996) · Immunology Today · doi:10.1016/0167-5699(96)30058-3 · Cited by 49 · see citing works

BTKbase: a database of XLA-causing mutations

Vihinen, M. (1995) · Immunology Today · doi:10.1016/0167-5699(95)80027-1 · Cited by 86 · see citing works

X‐linked agammaglobulinemia (XLA): A genetic tyrosine kinase (Btk) disease

Mattsson, P. T., Vihinen, M., & Smith, C. I. E. (1996) · BioEssays · doi:10.1002/bies.950181009 · Cited by 74 · see citing works