Apple, Nokia and RIM – Rivalry and Co-operation between Three Mobile Phone Corporations

The purpose of this paper is to gather enough evidence to speculate the future of Nokia, Rim and Apple. The thesis goes over the history, current events and business model of each company. This paper includes differences between the companies and co-operation and rivalry, such as patent infringement cases. The study is limited to smartphones and their future. The result of this study is that Apple will continue its steady increase in market share, while Nokia will first decrease and after the launch of the Windows Phone it will rise again. RIM‟s result has not been as good as in past years and it has lost market share. The decrease of share price may lead to acquisition by a company interested in RIM technology.

Yritysten teknologisen keskittymisen tutkiminen patenttianalyysin avulla Case: Apple, HTC, Nokia, Samsung

Työssä tutkitaan neljän matkapuhelinvalmistajan teknologista keskittymistä patenttianalyysin avulla. Tavoitteena on tutkia, onko yritysten patentoinnissa eroja sekä mihin eri teknologian osa-alueisiin yritykset patentoivat ja mihin eivät. Tavoitteen taustalla on selvittää, voidaanko patenttiaineistosta saada viitteitä yrityksen ydinosaamisesta. Työ koostuu kolmesta rakenteellisesta osiosta. Teoria esittelee patentit ja patenttiviittaukset. Patenttiaineisto on kerätty Lappeenrannan teknillisen yliopiston patenttipalvelimelta ja sitä on analysoitu tietokanta- sekä tilastollisen käsittelyn ohjelmalla. Tuloksista tehdyt analyysit yhdistetään teoriaan, jonka pohjalta tehdään johtopäätöksiä sekä suoritetaan vertailua yritysten kesken liittyen tutkimuskysymyksiin. Lopuksi arvioidaan aineiston ja tulosten luotettavuutta sekä esitetään mahdollisia jatkotutkimusaiheita.

The Structure and Function of αI Domains in Collagen Receptor and Leukocyte Integrins

Integrins are heterodimeric, signaling transmembrane adhesion receptors that connect the intracellular actin microfilaments to the extracellular matrix composed of collagens and other matrix molecules. Bidirectional signaling is mediated via drastic conformational changes in integrins. These changes also occur in the integrin αI domains, which are responsible for ligand binding by collagen receptor and leukocyte specific integrins. Like intact integrins, soluble αI domains exist in the closed, low affinity form and in the open, high affinity form, and so it is possible to use isolated αI domains to study the factors and mechanisms involved in integrin activation/deactivation. Integrins are found in all mammalian tissues and cells, where they play crucial roles in growth, migration, defense mechanisms and apoptosis. Integrins are involved in many human diseases, such as inflammatory, cardiovascular and metastatic diseases, and so plenty of effort has been invested into developing integrin specific drugs. Humans have 24 different integrins, four of which are collagen receptor (α1β1, α2β1, α10β1, α11β1) and five leukocyte specific integrins (αLβ2, αMβ2, αXβ2, αDβ2, αEβ7). These two integrin groups are quite unselective having both primary and secondary ligands. This work presents the first systematic studies performed on these integrin groups to find out how integrin activation affects ligand binding and selectivity. These kinds of studies are important not only for understanding the partially overlapping functions of integrins, but also for drug development. In general, our results indicated that selectivity in ligand recognition is greatly reduced upon integrin activation. Interestingly, in some cases the ligand binding properties of integrins have been shown to be cell type specific. The reason for this is not known, but our observations suggest that cell types with a higher integrin activation state have lower ligand selectivity, and vice versa. Furthermore, we solved the three-dimensional structure for the activated form of the collagen receptor α1I domain. This structure revealed a novel intermediate conformation not previously seen with any other integrin αI domain. This is the first 3D structure for an activated collagen receptor αI domain without ligand. Based on the differences between the open and closed conformation of the αI domain we set structural criteria for a search for effective collagen receptor drugs. By docking a large number of molecules into the closed conformation of the α2I domain we discovered two polyketides, which best fulfilled the set structural criteria, and by cell adhesion studies we showed them to be specific inhibitors of the collagen receptor integrins.