AdaStereo: An Efficient Domain-Adaptive Stereo Matching Approach

Recently, records on stereo matching benchmarks are constantly broken by end-to-end disparity networks. However, the domain adaptation ability of these deep models is quite limited. Addressing such problem, we present a novel domain-adaptive approach called AdaStereo that aims to align multi-level representations for deep stereo matching networks. Compared to previous methods, our AdaStereo realizes a more standard, complete and effective domain adaptation pipeline. Firstly, we propose a non-adversarial progressive color transfer algorithm for input image-level alignment. Secondly, we design an efficient parameter-free cost normalization layer for internal feature-level alignment. Lastly, a highly related auxiliary task, self-supervised occlusion-aware reconstruction is presented to narrow the gaps in output space. We perform intensive ablation studies and break-down comparisons to validate the effectiveness of each proposed module. With no extra inference overhead and only a slight increase in training complexity, our AdaStereo models achieve state-of-the-art cross-domain performance on multiple benchmarks, including KITTI, Middlebury, ETH3D and DrivingStereo, even outperforming some state-of-the-art disparity networks finetuned with target-domain ground-truths. Moreover, based on two additional evaluation metrics, the superiority of our domain-adaptive stereo matching pipeline is further uncovered from more perspectives. Finally, we demonstrate that our method is robust to various domain adaptation settings, and can be easily integrated into quick adaptation application scenarios and real-world deployments.

Genetic manipulation of pyoverdine non-ribosomal peptide synthetases to identify genetic constraints to effective domain recombination

<p>Non-ribosomal peptide synthetases (NRPSs) synthesise small highly diverse peptides with a wide range of activities, such as antibiotics, anticancer drugs, and immunosuppressants. NRPS synthesis often resembles an assembly line, in which each module acts in a linear order to add one monomer to the growing peptide chain. In the basic mechanism of synthesis, an adenylation (A) domain within each module activates a specific monomer. Once activated, the monomer is attached to an immediately downstream thiolation (T) domain via a prosthetic phosphopantheine group, which acts as a flexible arm to pass the substrate between catalytic domains. A condensation (C) domain, upstream to the A-T domains, catalyses peptide bond formation between an acceptor substrate attached to the T domain and a donor substrate attached to the T domain of the upstream module. The peptide remains attached to the T domain of the acceptor substrate, and then acts as the donor substrate for the next C domain. When peptide synthesis reaches the final module, the peptide is released by a thioesterase (TE) domain. The linear mode of synthesis and discrete functional domains within each module gives the potential to generate new products by substituting domains or entire modules with ones that activate alternative substrates. Attempts to create new products using domain and module substitution often result in a loss of activity. The work in this thesis focuses on identifying barriers to effective domain substitution. The NRPS enzyme pvdD, which adds the final residue to the eleven residue non-ribosomal peptide pyoverdine, was developed as a model for domain substitution. The primary benefit for using this model is that pyoverdine creates easily detectible fluorescent products. The first set of experiments focused on testing the limitations of A domain and C-A domain substitutions to alter pyoverdine. Nine A domain and nine C-A domain substitution pvdD variants were constructed and used to complement a P. aeruginosa PAO1 pvdD deletion strain. The A domain substitutions that specified the wild type substrate were highly functional, whereas A domains that specified other substrates resulted in low levels of wild type pyoverdine production. This suggests the acceptor site substrate specificity of the C domain limited the success of A domain substitutions, rather than disruption of the C/A domain junction. In contrast, although C-A domain substitutions in pvdD in some cases synthesised novel pyoverdines, the majority lost function for unknown reasons. The high success rate A domain substitutions (when not limited by the acceptor site specificity of the C domain) suggested the addition of new C domains was a likely cause for loss of function. The second set of experiments investigated whether disrupting the protein interface between C domains and their upstream T domains may cause a loss in function of C-A domain substitutions. However, domain substitutions of T domains were found to have a high rate of success. Therefore, the results thus far confirmed that disrupting interactions of the C domain with A domains or T domains does not have a large affect on enzyme activity. An alternative explanation for the loss in function with C-A domain substitutions is that C domains translocated to a new enzyme are unable to process the new incoming donor peptide chain because of substrate specificity or steric constraints. To develop methods to circumvent limitations caused by the C domain, the final part of this thesis examined acceptor substrate specificity of C domains. Acceptor site substrate specificity was chosen over donor site specificity as it acts on only an amino acid rather than peptide chain. The substrate specificity was narrowed down to a small subsection of the C domain. This was an initial study of C domain substrate specificity, which may guide future development of relaxed specificity C domains.</p>

Genetic manipulation of pyoverdine non-ribosomal peptide synthetases to identify genetic constraints to effective domain recombination

<p>Non-ribosomal peptide synthetases (NRPSs) synthesise small highly diverse peptides with a wide range of activities, such as antibiotics, anticancer drugs, and immunosuppressants. NRPS synthesis often resembles an assembly line, in which each module acts in a linear order to add one monomer to the growing peptide chain. In the basic mechanism of synthesis, an adenylation (A) domain within each module activates a specific monomer. Once activated, the monomer is attached to an immediately downstream thiolation (T) domain via a prosthetic phosphopantheine group, which acts as a flexible arm to pass the substrate between catalytic domains. A condensation (C) domain, upstream to the A-T domains, catalyses peptide bond formation between an acceptor substrate attached to the T domain and a donor substrate attached to the T domain of the upstream module. The peptide remains attached to the T domain of the acceptor substrate, and then acts as the donor substrate for the next C domain. When peptide synthesis reaches the final module, the peptide is released by a thioesterase (TE) domain. The linear mode of synthesis and discrete functional domains within each module gives the potential to generate new products by substituting domains or entire modules with ones that activate alternative substrates. Attempts to create new products using domain and module substitution often result in a loss of activity. The work in this thesis focuses on identifying barriers to effective domain substitution. The NRPS enzyme pvdD, which adds the final residue to the eleven residue non-ribosomal peptide pyoverdine, was developed as a model for domain substitution. The primary benefit for using this model is that pyoverdine creates easily detectible fluorescent products. The first set of experiments focused on testing the limitations of A domain and C-A domain substitutions to alter pyoverdine. Nine A domain and nine C-A domain substitution pvdD variants were constructed and used to complement a P. aeruginosa PAO1 pvdD deletion strain. The A domain substitutions that specified the wild type substrate were highly functional, whereas A domains that specified other substrates resulted in low levels of wild type pyoverdine production. This suggests the acceptor site substrate specificity of the C domain limited the success of A domain substitutions, rather than disruption of the C/A domain junction. In contrast, although C-A domain substitutions in pvdD in some cases synthesised novel pyoverdines, the majority lost function for unknown reasons. The high success rate A domain substitutions (when not limited by the acceptor site specificity of the C domain) suggested the addition of new C domains was a likely cause for loss of function. The second set of experiments investigated whether disrupting the protein interface between C domains and their upstream T domains may cause a loss in function of C-A domain substitutions. However, domain substitutions of T domains were found to have a high rate of success. Therefore, the results thus far confirmed that disrupting interactions of the C domain with A domains or T domains does not have a large affect on enzyme activity. An alternative explanation for the loss in function with C-A domain substitutions is that C domains translocated to a new enzyme are unable to process the new incoming donor peptide chain because of substrate specificity or steric constraints. To develop methods to circumvent limitations caused by the C domain, the final part of this thesis examined acceptor substrate specificity of C domains. Acceptor site substrate specificity was chosen over donor site specificity as it acts on only an amino acid rather than peptide chain. The substrate specificity was narrowed down to a small subsection of the C domain. This was an initial study of C domain substrate specificity, which may guide future development of relaxed specificity C domains.</p>

New Tour on the Subdifferential of Supremum via Finite Sums and Suprema

This paper provides new characterizations for the subdifferential of the pointwise supremum of an arbitrary family of convex functions. The main feature of our approach is that the normal cone to the effective domain of the supremum (or to finite-dimensional sections of it) does not appear in our formulas. Another aspect of our analysis is that it emphasizes the relationship with the subdifferential of the supremum of finite subfamilies, or equivalently, finite weighted sums. Some specific results are given in the setting of reflexive Banach spaces, showing that the subdifferential of the supremum can be reduced to the supremum of a countable family.

SP4.2.8 Does Care quality commission need to change its inspection strategy after COVID-19?

Aim To see if the Care quality commission’s (CQC) overall inspection ratings and specific domain ratings had any association with COVID-19 related deaths. Methods We looked at CQC ratings of the Shelford group of trusts and 10 trusts with maximum number of deaths in the time period from the first wave till 23rd January 2021. We then looked at each of the 5 domains: safe, effective, caring, responsive, and well led, to see if they were in any way indicative of the number of deaths in that trust. Results Among the 19 trusts studied (one trust featured in both groups) only 1 had an overall outstanding rating; 10 were rated good, 8 required improvement. None were rated inadequate in any of the domains, 16 /19 were rated good in effective domain which means “there care, treatment and support achieves good outcomes”. In safe domain 13/ the 19 were rated as requires improvement which means that “a patient may not be protected from avoidable harm”. Conclusion COVID-19 is no respecter of the CQC ratings, even if the trust was rated as well led and had good ratings in all other domains it could still have the highest mortality figures from COVID in the UK. CQC probably needs to add a 6th domain to its future inspections to assess the readiness the trusts for future Pandemics.

INTEGRATED MARITIME PICTURE FOR EFFECTIVE DOMAIN AWARENESS

According to the IMO (International Maritime Organization) Definition of MDA (Maritime Domain Awareness) : “Effective understanding of anything associated with the maritime domain that could impact the security, safety, economy, or environment”. As per the geography, more than half of the countries in the world map are littoral states. Hence Maritime Domain Awareness is a great concern of many states (Bateman, S. (2011). However incidents that are reporting in maritime environments are evident that, it is not safe as we thought and causes serious influences to the national security of a state. Hence maritime security is great concern of littoral and non-littoral nations and emphasis have given for effective maritime detection as it is the gateway for a maritime interdiction and apprehension. How much our maritime environment is deserted and far from human activities, each and every bit of ocean environment is monitored by many agents of different nations for different perspectives and interests. However, in contradictory exploitation sea for crimes and criminalities is increase day by day and drug trafficking, human smuggling and human trafficking are some of the top listed criminalities. Even though mankind is capable to monitor every inch of ocean mass still sea is the main supply route for bulk of drugs and narcotics and reporting illegal migration is a common topic in many news forums. The real cause of this enigmatic situation is poor commitment by the states for effective mechanism to monitor and apprehend the culprits. For that sharing of information is important but obviously individuals are greedy on information for many reasons. As a result most of the monitoring stations are getting what they are interested but not the complete picture of maritime domain. Especially developing countries must focus for integration as funds for developed systems are the main constrain for them. Hence every bit of information is really important to build a complete picture to have a better understanding of the maritime environment.in this background this paper is to discuss an effective mechanism to integrate information and to share those with national and friendly international bodies to enhance decision making ability to effective interdiction to ensure safe seas.