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520 results on '"Hawes C."'

6. Invertebrate Responses to the Management of Genetically Modified Herbicide-Tolerant and Conventional Spring Crops. I. Soil-Surface-Active Invertebrates

Author

Brooks, D. R., Bohan, D. A., Champion, G. T., Haughton, A. J., Hawes, C., Heard, M. S., Clark, S. J., Dewar, A. M., Firbank, L. G., Perry, J. N., Rothery, P., Scott, R. J., Woiwod, I. P., Birchall, C., Skellern, M. P., Walker, J. H., Baker, P., Bell, D., Browne, E. L., Dewar, A. J. G., Fairfax, C. M., Garner, B. H., Haylock, L. A., Horne, S. L., Hulmes, S. E., Mason, N. S., Norton, L. R., Nuttall, P., Randle, Z., Rossall, M. J., Sands, R. J. N., Singer, E. J., and Walker, M. J.

Published
2003

9. Invertebrate Responses to the Management of Genetically Modified Herbicide-Tolerant and Conventional Spring Crops. II. Within-Field Epigeal and Aerial Arthropods

Author

Haughton, A. J., Champion, G. T., Hawes, C., Heard, M. S., Brooks, D. R., Bohan, D. A., Clark, S. J., Dewar, A. M., Firbank, L. G., Osborne, J. L., Perry, J. N., Rothery, P., Roy, D. B., Scott, R. J., Woiwod, I. P., Birchall, C., Skellern, M. P., Walker, J. H., Baker, P., Browne, E. L., Dewar, A. J. G., Garner, B. H., Haylock, L. A., Horne, S. L., Mason, N. S., Sands, R. J. N., and Walker, M. J.

Published
2003

36. Supramolecular structural influences from remote functionality in coordination complexes of 4-picolylamine ligands.

Author

Slyusarchuk, V. D., O'Brien, B. J., and Hawes, C. S.

Subjects
COORDINATION compounds, LIGANDS (Chemistry), INTERMOLECULAR interactions, HYDROGEN bonding, METHYLENE group, MORPHOLINE, COORDINATION polymers
Abstract

A series of nine cobalt(II), copper(II) and silver(I) coordination complexes of structurally similar picolylamine ligands, N-(4-picolyl)piperidine (L1) and N-(4-picolyl)morpholine (L2), have been prepared and analyzed. These consist of a dinuclear copper(II) complex [Cu2(OAc)4(L1)2] (1), tetranuclear copper(II) complexes [Cu4OCl6(L1)4]·MeCN·H2O (2) and [Cu4OCl7(L2)2 (L2H)]·2MeCN·9H2O (3), trichlorocobaltate complexes [CoCl3 (L1H)]·MeCN (4) and [CoCl3(L2H)] (5), silver coordination polymers poly-[AgL1]SbF6·0.5THF) (6), poly-[Ag(L2)]SbF6·0.5THF (7) and poly-[Ag(L1)(CO2CF3)] (9) and discrete dinuclear silver complex [Ag2(L2)2(THF)4](SbF6)2 (8). While the coordination and classical N–H···X hydrogen bonding in these species is related and largely independent of backbone functionality, differences in ligand composition dictate the d weak interactions and the supramolecular structure. In 1, 2, 4, 6 and 9 piperidine acts as a weak hydrogen bond donor, with C–H···Cl/O/F contacts mostly observed from the methylene groups adjacent to the amine. In the morpholine species 3, 5, 7 and 8 the tendency for morpholine to associate via reciprocated C–H···O interactions overrides the other crystal packing tendencies, changing both the local and extended structures. By studying both strong and weak packing interactions, this study presents a test case for the design of discrete and polymeric coordination compounds with finely tuned modes of intermolecular interaction. [ABSTRACT FROM AUTHOR]

Published
2022
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46. UK food and nutrition security during and after the COVID‐19 pandemic.

Author

Rivington, M., King, R., Duckett, D., Iannetta, P., Benton, T. G., Burgess, P.J., Hawes, C., Wellesley, L., Polhill, J. G., Aitkenhead, M., Lozada‐Ellison, L.‐M., Begg, G., Williams, A. G., Newton, A., Lorenzo‐Arribas, A., Neilson, R., Watts, C., Harris, J., Loades, K., and Stewart, D.

Subjects
RISK assessment, INTERPROFESSIONAL relations, ECOLOGY, FOOD security, CLIMATE change, CONSUMER attitudes, ECOSYSTEMS, CONVALESCENCE, ADULT education workshops, NUTRITION, COVID-19 pandemic, EMERGENCY management
Abstract

The COVID‐19 pandemic is a major shock to society in terms of health and economy that is affecting both UK and global food and nutrition security. It is adding to the 'perfect storm' of threats to society from climate change, biodiversity loss and ecosystem degradation, at a time of considerable change, rising nationalism and breakdown in international collaboration. In the UK, the situation is further complicated due to Brexit. The UK COVID‐19Food andNutritionSecurity project, lasting one year, is funded by the Economic and Social Research Council and is assessing the ongoing impact of COVID‐19 on the four pillars of food and nutrition security: access, availability, utilisation and stability. It examines the food system, how it is responding, and potential knock on effects on the UK's food and nutrition security, both in terms of the cascading risks from the pandemic and other threats. The study provides an opportunity to place the initial lessons being learnt from the on‐going responses to the pandemic in respect of food and nutrition security in the context of other long‐term challenges such as climate change and biodiversity loss. [ABSTRACT FROM AUTHOR]

Published
2021
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47. Living on the edge: the role of Atgolgin‐84A at the plant ER–Golgi interface.

Author

VIEIRA, V., PAIN, C., WOJCIK, S., SPATOLA ROSSI, T., DENECKE, J., OSTERRIEDER, A., HAWES, C., and KRIECHBAUMER, V.

Subjects
BIOLOGICAL transport, FLUORESCENT proteins, GOLGI apparatus, LASER microscopy, ENDOPLASMIC reticulum, MEMBRANE proteins
Abstract

Summary: The plant Golgi apparatus is responsible for the processing of proteins received from the endoplasmic reticulum (ER) and their distribution to multiple destinations within the cell. Golgi matrix components, such as golgins, have been identified and suggested to function as putative tethering factors to mediate the physical connections between Golgi bodies and the ER network. Golgins are proteins anchored to the Golgi membrane by the C‐terminus either through transmembrane domains or interaction with small regulatory GTPases. The golgin N‐terminus contains long coiled‐coil domains, which consist of a number of α‐helices wrapped around each other to form a structure similar to a rope being made from several strands, reaching into the cytoplasm. In animal cells, golgins are also implicated in specific recognition of cargo at the Golgi.Here, we investigate the plant golgin Atgolgin‐84A for its subcellular localization and potential role as a tethering factor at the ER–Golgi interface. For this, fluorescent fusions of Atgolgin‐84A and an Atgolgin‐84A truncation lacking the coiled‐coil domains (Atgolgin‐84AΔ1‐557) were transiently expressed in tobacco leaf epidermal cells and imaged using high‐resolution confocal microscopy. We show that Atgolgin‐84A localizes to a pre‐cis‐Golgi compartment that is also labelled by one of the COPII proteins as well as by the tether protein AtCASP. Upon overexpression of Atgolgin‐84A or its deletion mutant, transport between the ER and Golgi bodies is impaired and cargo proteins are redirected to the vacuole. Lay Description: The Golgi apparatus is a specialised compartment found in mammalian and plant cells. It is the post office of the cell and packages proteins into small membrane boxes for transport to their destination in the cell. The plant Golgi apparatus consist of many separate Golgi bodies and is responsible for the processing of proteins received from the endoplasmic reticulum (ER) and their distribution to multiple destinations within the cell. Specialised proteins called golgins have been suggested to tether Golgi bodies and the ER. Here we investigate the plant golgin Atgolgin‐84A for its exact within the Golgi body and its potential role as a tethering factor at the ER‐Golgi interface. For this, we have fused Atgolgin‐84A with a fluorescent protein from jellyfish and we are producing this combination in tobacco leaf cells. This allows us to see the protein using laser microscopy. We show that Atgolgin‐84A localises to a compartment between the ER and Golgi that is also labelled by the tether protein AtCASP. When Atgolgin‐84A is produced in high amounts in the cell, transport between the ER and Golgi bodies is inhibited and proteins are redirected to the vacuole. [ABSTRACT FROM AUTHOR]

Published
2020
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