37 research outputs found
Разработка программы продвижения продукции фирмы
Объектом иследования является - ООО" Аксиом" , как торговая организация, работающая на рынке часов фэшн-направления.
Цель работы - разработка программы продвижения часов фэшн-направления на рынке города Новосибирска.
В процессе исследования:
проанализировано состояние рынка часов города Новосибирска;
проведено исследование отношения потребителей к часам фэшн-направления, мотивов их покупки, покупательского поведения;
проведен анализ руночной среды и коммуникационной деятельности ООО " Аксиом" и сети "X-time";
В резульате исследования была разработана " Программа продвижения часов фэшн-направленияна рынке города Новосибирска".The object of research - Company " Axiom " , as a trade organization that works on the market hours fashion-direction .
The purpose work- program development promotion hours fashion- direction of the city of Novosibirsk market.
During research :
analyzed the state of the market hours of the city of Novosibirsk ;
Swipe study of consumer attitudes to watch the fashion trends , reasons for their purchases of consumer behavior ;
Swipe analysis runochnoy media and communication company " Axiom " and network "X-time";
The program of promotion watches fashion napravleniyana Novosibirsk market " was developed in the end of research
The Arabidopsis protein phosphatase PP2C38 negatively regulates the central immune kinase BIK1
Plants recognize pathogen-associated molecular patterns (PAMPs) via cell surface-localized pattern recognition receptors (PRRs), leading to PRR-triggered immunity (PTI). The Arabidopsis cytoplasmic kinase BIK1 is a downstream substrate of several PRR complexes. How plant PTI is negatively regulated is not fully understood. Here, we identify the protein phosphatase PP2C38 as a negative regulator of BIK1 activity and BIK1-mediated immunity. PP2C38 dynamically associates with BIK1, as well as with the PRRs FLS2 and EFR, but not with the co-receptor BAK1. PP2C38 regulates PAMP-induced BIK1 phosphorylation and impairs the phosphorylation of the NADPH oxidase RBOHD by BIK1, leading to reduced oxidative burst and stomatal immunity. Upon PAMP perception, PP2C38 is phosphorylated on serine 77 and dissociates from the FLS2/EFR-BIK1 complexes, enabling full BIK1 activation. Together with our recent work on the control of BIK1 turnover, this study reveals another important regulatory mechanism of this central immune component