Micro-foundations of dynamic capabilities to facilitate university technology transfer.

Within the university-industry ecosystem, improvement and innovation of technology transfer involve implementing appropriate dynamic capabilities. To answer the question-What are the micro-foundations of dynamic capabilities in university technology transfer?-this study investigates in-depth organizational-level dynamic capabilities in transferring university-based knowledge to business and society. Two qualitative case studies were deployed at organizational entities at Vrije Universiteit Amsterdam: the Industry Alliance Office, and the Demonstrator Lab. These two organizations stimulate science- and business-oriented university technology transfer. In this context, the micro-foundations of the dynamic capabilities "sensing", "seizing" and "reconfiguring" are identified and discussed. For "sensing", which is the university's ability to explore the opportunities in the ecosystem, the micro-foundations are "selecting internal competency" and "sensing external partners". For "seizing", which supports universities in managing complementarity with industry and society, micro-foundations include "resource co-allocation" and "collaborative business model". The micro-foundations of "reconfiguring", through which universities maintain evolutionary fitness in the innovation ecosystem, are "strategic renewal", "establishing a university technology transfer-friendly environment", and "asset orchestration". This study provides researchers with a better understanding of how dynamic capabilities facilitate university technology transfer. Industrial practitioners and policymakers can consider the suggestions of the present study when pursuing collaboration with universities.

Combined pituitary hormone deficiency caused by compound heterozygosity for two novel mutations in the POU domain of the Pit1/POU1F1 gene.

The POU homeodomain containing transcriptional activator POU1F1, formerly called Pit1 or GHF-1, is required for the embryological determination and postnatal secretory function of the GH-, PRL-, and TSH-producing cells in the anterior pituitary. Several mutations in the gene encoding POU1F1 have been described, resulting in a syndrome of combined pituitary hormone deficiency involving these three hormones. Most of the patients with this phenotype have either a dominant negative mutation in codon 271 (R271W) or are homozygous for a recessive mutation in the POU1F1 gene; to date only one case has been reported with compound heterozygosity for two point mutations. Here, we describe a boy with severe deficiencies of GH, PRL, and TSH who had compound heterozygosity for two novel point mutations in the POU1F1 gene: a 1-bp deletion frameshift mutation (747delA), the first one described to date in this gene, which leads to a nonfunctional truncated protein lacking the entire DNA recognition helix of the POU homeodomain, and a missense mutation in the C-terminal end of the fourth alpha-helix of the POU-specific domain (W193R),which causes a 500-fold reduction in the ability to bind to DNA and activate transcription.