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Hashing has recently sparked a great revolution in cross-modal retrieval because of its low storage cost and high query speed. Recent cross-modal hashing methods often learn unified or equal-length hash codes to represent the multi-modal data and make them intuitively comparable. However, such representations could inherently sacrifice their representation scalability because the data from different modalities may not have one-to-one correspondence and could be encoded more efficiently by different hash codes of unequal lengths. To mitigate these problems, this paper exploits a related and relatively unexplored problem: encode the heterogeneous data with varying hash lengths and generalize the cross-modal retrieval in various challenging scenarios. To this end, a generalized and flexible cross-modal hashing framework, termed Matrix Tri-Factorization Hashing (MTFH), is proposed to work seamlessly in various settings including paired or unpaired multi-modal data, and equal or varying hash length encoding scenarios. MTFH exploits an efficient objective function to flexibly learn modality-specific hash codes with different length settings, while synchronously learning two semantic correlation matrices for heterogeneous data comparable. As a result, the derived hash codes are more semantically meaningful for various challenging cross-modal retrieval tasks. Extensive experiments evaluated on public benchmark datasets highlight the superiority of MTFH under various retrieval scenarios and show its competitive performance with the state-of-the-arts.
This article was published in the following journal.
Name: IEEE transactions on pattern analysis and machine intelligence
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A secreted matrix metalloproteinase that is the predominant proteolytic activity in the enamel matrix. The enzyme has a high specificity for dental enamel matrix protein AMELOGENIN.
A transmembrane domain-containing matrix metalloproteinase. It is synthesized as an inactive zymogen that is activated by the proteolytic action of PROPROTEIN CONVERTASES. Matrix metalloproteinase 16 plays a direct role in the cleavage of proteins in the pericellular environment. In addition it can function indirectly by enzymatically activating the proprotein form of other MATRIX METALLOPROTEINASES such as the zymogen of MATRIX METALLOPROTEINASE 2.
A secreted matrix metalloproteinase that is believed to play a role in EXTRACELLULAR MATRIX remodeling and cell fate determination during normal and pathological processes. Matrix metalloproteinase 11 was originally isolated in primary BREAST NEOPLASMS and may be involved in the process of tumorigenesis.
A transmembrane domain-containing matrix metalloproteinase. It is synthesized as an inactive zymogen that is activated by the action of PROPROTEIN CONVERTASES such as FURIN. Matrix metalloproteinase 14 plays a direct role in the cleavage of proteins in the pericellular environment. In addition it can function indirectly by enzymatically activating the proprotein form of MATRIX METALLOPROTEINASE 15.
The residual framework structure of the CELL NUCLEUS that maintains many of the overall architectural features of the cell nucleus including the nuclear lamina with NUCLEAR PORE complex structures, residual CELL NUCLEOLI and an extensive fibrogranular structure in the nuclear interior. (Advan. Enzyme Regul. 2002; 42:39-52)