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- BookRaif Geha, Luigi Notarangelo, Harvard Medical School.Contents:
X-linked agammaglobulinemia
CD40 ligand deficiency
Activation-induced cytidine deaminase deficiency
Common variable immunodeficiency
X-linked severe combined immunodeficiency
Adenosine deaminase deficiency
Omenn syndrome
MHC class II deficiency
DiGeorge syndrome
Acquired immune deficiency syndrome (AIDS)
Graft-versus-host disease
MHC class I deficiency
X-linked lymphoproliferative syndrome
Hemophagocytic lymphohistiocytosis
Chediak-higashi syndrome
Wiskott-Aldrich syndrome
Autoimmune polyendocrinopathy-candidiasis-ectodermal dystrophy (APECED)
Immune dysregulation, polyendocrinopathy, enteropathy X-linked disease
Autoimmune lymphoproliferative syndrome (ALPS)
Hyper IgE syndrome
Ataxia telangiectasis
Warts, hypogrammaglobulinemia, infections, and myelokathexis syndrome (WHIM syndrome)
X-linked hypohidrotic ectodermal dysplasia and immunodeficiency
Interferon-{u01B4} receptor deficiency
Severe congenital neutropenia
Chronic granulomatous disease
Leukocyte adhesion deficiency
Recurrent herpes simplex encephalitis
Interleukin 1 receptor-associated kinase 4 deficiency
Congenital asplenia
Hereditary angioedema
Deficiency of the C8 complement component
Hereditary periodic fever syndromes
Systemic juvenile idiopathic arthritis
Rheumatoid arthritis
Systemic lupus erythematosus
Crohn's disease
Multiple sclerosis
Autoimmune hemolytic anemia
Myasthenia gravis
Pemphigus vulgaris
Celiac disease
Acute infectious mononucleosis
Hemolytic disease of the new born
Toxic shock syndrome
Lepromatous leprosy
Allergic asthma
Drug-induced serum sickness
Contact sensitivity to poison ivy
Dedicator of cytokinesis 8 deficiency
Activated P13KD syndrome (APDS)
Increased susceptibility to Candida infections
LPS-responsive beige-like anchor (LRBA) deficiency
T cell signaling defects
ChannelopathiesDigital Access TandFonline 2016Limited to 3 simultaneous usersPrintLocationVersionCall NumberItems - ArticleScouten WH, De Graaf-Hess AC, De Kok A, Grande HJ, Visser AJ, Veeger C.Eur J Biochem. 1978 Mar;84(1):17-25.Fluorescence energy transfer has been employed to estimate the minimum distance between each of the active sites of the 4 component enzymes of the pyruvate dehydrogenase multienzyme complex from Azotobacter vinelandii. No energy transfer was seen between thiochrome diphosphate, bound to the pyruvate decarboxylase active site, and the FAD of the lipoamide dehydrogenase active site. Likewise, several fluorescent sulfhydryl labels, which were specifically bound to the lipoyl moiety of lipoyl transacetylase, showed no energy transfer to either the flavin or thiochrome diphosphate. These observations suggest that all the active centers of the complex are quite far apart (greater than or equal to 40 nm), at least during some stages of catalysis. These results do not preclude the possibility that the distances change during catalysis. Several of the fluorescent probes used possessed multiple fluorescent lifetimes, as shown by determination of lifetime averages by both phase and modulation measurements on a phase fluorimeter. These lifetimes are shown to result from multiple factors, not necessarily related to multiple protein conformations.