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C Wooding

Researcher at Imperial College London

Publications -  35
Citations -  3543

C Wooding is an academic researcher from Imperial College London. The author has contributed to research in topics: Locus (genetics) & Genetic linkage. The author has an hindex of 25, co-authored 35 publications receiving 3429 citations. Previous affiliations of C Wooding include Hammersmith Hospital & Medical Research Council.

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Clinical studies of multiple endocrine neoplasia type 1 (MEN1)

TL;DR: Investigation of multiple endocrine neoplasia type 1 patients found that parathyroid tumours were the first manifestation of MEN1 in 87% of patients, and amongst the pituitary and pancreatic tumours, somatotrophinomas and gastrinomas were more common in patients above the age of 40 years, whilst insulinomas occurred more frequently in patients below the ageof 40 years.
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Characterization of Mutations in Patients with Multiple Endocrine Neoplasia Type 1

TL;DR: The results provide the basis for a molecular-genetic screening approach that will supplement the clinical evaluation and genetic counseling of members of MEN1 families and SSCP was found to be a sensitive and specific mutational screening method that detected >85% of the mutations.
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Calcium-sensing receptor mutations in familial benign hypercalcemia and neonatal hyperparathyroidism.

TL;DR: The single-stranded conformational polymorphism identification of CaR mutations may help in the distinction of FBH from mild primary hyperparathyroidism which can be clinically difficult.
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Association of parathyroid tumors in multiple endocrine neoplasia type 1 with loss of alleles on chromosome 11.

TL;DR: It is concluded that a single inherited locus on chromosome 11, band q13, causesMEN-1 and that the monoclonal development of parathyroid and pancreatic tumors in patients with MEN-1 involves similar allelic deletions on chromosomes 11.
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Repacking of the transmembrane domains of P‐glycoprotein during the transport ATPase cycle

TL;DR: It is suggested that ATP binding, not hydrolysis, drives the major conformational change associated with solute translocation in P‐glycoprotein, and biochemical data suggest that these rearrangements may involve rotation of transmembrane α‐helices.