about
Multiple M. tuberculosis phenotypes in mouse and guinea pig lung tissue revealed by a dual-staining approachBoosting BCG-primed responses with a subunit Apa vaccine during the waning phase improves immunity and imparts protection against Mycobacterium tuberculosisGlycolytic and Non-glycolytic Functions of Mycobacterium tuberculosis Fructose-1,6-bisphosphate Aldolase, an Essential Enzyme Produced by Replicating and Non-replicating BacilliA bispecific antibody based assay shows potential for detecting tuberculosis in resource constrained laboratory settingsLong-term survival and virulence of Mycobacterium leprae in amoebal cystsLeprosy in Children.A new Mycobacterium species causing diffuse lepromatous leprosy.A modified synthesis and serological evaluation of neoglycoproteins containing the natural disaccharide of PGL-I from Mycobacterium lepraeField-evaluation of a new lateral flow assay for detection of cellular and humoral immunity against Mycobacterium leprae.Identification of an Immunomodulating Agent from Mycobacterium lepraePostgenomic approach to identify novel Mycobacterium leprae antigens with potential to improve immunodiagnosis of infection.Antigenic specificity of the Mycobacterium leprae homologue of ESAT-6Comparative analysis of B- and T-cell epitopes of Mycobacterium leprae and Mycobacterium tuberculosis culture filtrate protein 10.IL-10 and NOS2 modulate antigen-specific reactivity and nerve infiltration by T cells in experimental leprosyPathogen-specific epitopes as epidemiological tools for defining the magnitude of Mycobacterium leprae transmission in areas endemic for leprosy.PARK2 mediates interleukin 6 and monocyte chemoattractant protein 1 production by human macrophages.Analysis of antibody responses to Mycobacterium leprae phenolic glycolipid I, lipoarabinomannan, and recombinant proteins to define disease subtype-specific antigenic profiles in leprosy.Insight toward early diagnosis of leprosy through analysis of the developing antibody responses of Mycobacterium leprae-infected armadillos.Gene set signature of reversal reaction type I in leprosy patients.O-mannosylation of the Mycobacterium tuberculosis adhesin Apa is crucial for T cell antigenicity during infection but is expendable for protection.Spatial analysis spotlighting early childhood leprosy transmission in a hyperendemic municipality of the Brazilian Amazon regionUse of protein microarrays to define the humoral immune response in leprosy patients and identification of disease-state-specific antigenic profiles.Lateral flow assay for simultaneous detection of cellular- and humoral immune responses.The presence of a galactosamine substituent on the arabinogalactan of Mycobacterium tuberculosis abrogates full maturation of human peripheral blood monocyte-derived dendritic cells and increases secretion of IL-10.Longitudinal immune profiles in type 1 leprosy reactions in Bangladesh, Brazil, Ethiopia and Nepal.Spatial epidemiology and serologic cohorts increase the early detection of leprosyNew biomarkers with relevance to leprosy diagnosis applicable in areas hyperendemic for leprosy.Gene expression profile and immunological evaluation of unique hypothetical unknown proteins of Mycobacterium leprae by using quantitative real-time PCR.Expression and characterization of recombinant interferon gamma (IFN-gamma) from the nine-banded armadillo (Dasypus novemcinctus) and its effect on Mycobacterium leprae-infected macrophages.From genome-based in silico predictions to ex vivo verification of leprosy diagnosis.Unexpectedly high leprosy seroprevalence detected using a random surveillance strategy in midwestern Brazil: A comparison of ELISA and a rapid diagnostic test.Detection of the tuberculosis antigenic marker mannose-capped lipoarabinomannan in pretreated serum by surface-enhanced Raman scattering.Importance of specimen pretreatment for the low-level detection of mycobacterial lipoarabinomannan in human serum.ML0405 and ML2331 are antigens of Mycobacterium leprae with potential for diagnosis of leprosy.ML1419c peptide immunization induces Mycobacterium leprae-specific HLA-A*0201-restricted CTL in vivo with potential to kill live mycobacteria.Further biochemical characterization of Mycobacterium leprae laminin-binding proteins.Deciphering the proteomic profile of Mycobacterium leprae cell envelope.The level of PPD-specific IFN-gamma-producing CD4+ T cells in the blood predicts the in vivo response to PPD.Identification of amino acids and domains required for catalytic activity of DPPR synthase, a cell wall biosynthetic enzyme of Mycobacterium tuberculosis.Immunization against full-length protein and peptides from the Lutzomyia longipalpis sand fly salivary component maxadilan protects against Leishmania major infection in a murine model.
P50
Q21090008-A7723080-C6DC-458F-BD15-B4A9294E5C94Q27315911-DA142DE1-34E9-4B6B-8F08-3BF04B383D37Q27674487-7D41855E-CF31-42E4-9C98-F480C80D7524Q28481078-EFC139A6-4D06-47F9-AC24-7C13DBD7121FQ28542771-6C9649B1-C4E8-452E-BBD9-AB7BFB8487ADQ30234659-3CF54336-FF07-4C4A-9373-7CCCD5C1483CQ33385581-EF9D4112-8D16-4CC6-96E1-1114BF907EDDQ33576460-34177289-3447-4917-BA32-5620787695E8Q33583641-8A382C4E-CEED-4EC2-82D3-8CAE2562C8EEQ33769064-11253AF8-91C2-411C-A84C-016EAE00DC30Q34034065-53C413C3-192E-4D80-A287-40C21625AB51Q34117932-16894986-72F5-407C-9606-AEB7964396F3Q34145568-8705E7AE-ECCE-48C3-BC6B-E21DE24E3F70Q34165767-4CA640E0-657A-4B90-A160-9A5F74D63A33Q34251374-E1FA72CB-5C3C-496E-A1A6-6ADD003783B7Q34563658-5444C297-CA94-4C25-A8CA-B7E300210D0DQ34738690-A4558EBF-E012-4434-AFFA-67B617D1D867Q34738846-35A9B86C-C95B-4AA8-BAD8-79A3673884FFQ34845804-BAC31A4B-1218-4441-99BE-B958440888D7Q35018095-D9100687-58D6-4F77-A81D-1F8AEEA814A8Q35091843-25D394EF-19F2-422E-A757-CE7A4FDE743DQ35217520-1577726C-D81D-4ACF-9722-1B536E257EACQ35226256-C495C9AB-7A9F-4C85-BA89-F0854B108612Q35762782-06371AEB-B0C1-4AD2-ABF9-E1F99F42EEFBQ35825015-1BA43667-4F32-40F9-9B4F-DC10AA6510B2Q35843218-18D39BFD-3995-47DE-BB4E-EE1930AD7D16Q35936136-C393E67A-40C7-46A8-AF4D-F228DA556E34Q36606784-D4A98236-D0CB-4614-ABD3-E80528B7275EQ36890945-2A4A4A60-F52F-42A1-B105-E2204975FC79Q37116579-F03BCF3D-53B3-4657-9018-13E7F7231C55Q37712219-A51180E4-4EED-43C2-BFB8-6FE3C5B5F25AQ38376927-E3011691-2BFB-4EE8-9C63-ED271FABE273Q40416538-DF485543-3344-4E4C-A7D7-70BAEE445774Q42219730-F3FACE48-B791-4834-A41A-FC379AF6296BQ42220548-A675CCB2-76A6-41F0-909A-B129FB540431Q42646609-7F36651B-E4B0-447F-A6F7-AB4A4FD378BEQ42659613-13A63A43-B8EA-4E42-A40D-90FE5E4C73D5Q44812803-733D66B1-4105-4447-9DB3-A74E2291B765Q46726125-4EC0006B-89E5-4CA4-83D6-38697AD42721Q47094812-5218425E-DD24-4AFE-A22D-857A66B04370
P50
description
microbiologist
@en
wetenschapper
@nl
name
John S Spencer
@nl
John S Spencer
@sl
John S. Spencer
@en
John S. Spencer
@es
type
label
John S Spencer
@nl
John S Spencer
@sl
John S. Spencer
@en
John S. Spencer
@es
prefLabel
John S Spencer
@nl
John S Spencer
@sl
John S. Spencer
@en
John S. Spencer
@es
P1053
G-6968-2017
P106
P21
P2798
P31
P3829
P496
0000-0002-8051-3038