| 1. |
- Chaplin-Kramer, R., et al.
(författare)
-
Transformation for inclusive conservation : Evidence on values, decisions, and impacts in protected areas
- 2023
-
Ingår i: Current Opinion in Environmental Sustainability. - : Elsevier. - 1877-3435 .- 1877-3443. ; 64
-
Tidskriftsartikel (refereegranskat)abstract
- As countries consider new area-based conservation targets under the Convention on Biological Diversity, protected areas (PAs) and their impacts on people and nature are coming under increasing scrutiny. We review the evidence base on PA impacts, combining the findings from existing rigorous impact evaluations with local case studies developed for this study. We identify characteristics of PA establishment and management that improve the sustainability of biodiversity conservation and justice for local communities. We find that recognizing and respecting local values and knowledge about natural resource stewardship, colearning, and comanagement are key to achieving positive impacts for nature and people. Transforming PA governance toward more inclusive conservation depends upon the ability of PAs to be designed and implemented around the values and needs of local people.
|
|
| 2. |
- Jimenez, A, et al.
(författare)
-
Human spermatid-specific thioredoxin-1 (Sptrx-1) is a two-domain protein with oxidizing activity
- 2002
-
Ingår i: FEBS Letters. - 0014-5793 .- 1873-3468. ; 530:1-3, s. 79-84
-
Tidskriftsartikel (refereegranskat)abstract
- Spermatid-specific thioredoxin-1 (Sptrx-1) is the first member of the thioredoxin family of proteins with a tissue-specific expression pattern, found exclusively in the tail of elongating spermatids and spermatozoa. We describe here further biochemical characterization of human Sptrx-1 protein structure and enzymatic activity. In gel filtration chromatography human Sptrx-1 eluates as a 400 kDa protein consistent with either an oligomeric form, not maintained by intermolecular disulfide bonding, and/or a highly asymmetrical structure. Analysis of circular dichroism spectra of fragments 1-360 and 361-469 and comparison to spectra of full-length Sptrx-1 supports a two-domain organization with a largely unstructured N-terminal domain and a folded thioredoxin-like C-terminal domain. Functionally, Sptrx-1 behaves as an oxidant in vitro when using selenite, but not oxidized glutathione, as electron acceptor. This oxidizing enzymatic activity suggests that Sptrx-1 might govern the stabilization (by disulfide cross-linking) of the different structures in the developing tail of spermatids and spermatozoa.
|
|
