Results 31 to 40 of about 30,399 (190)
Aquaporin-11 (AQP11) is the latest member of the mammalian water channel protein family to be described. Recent in vivo studies have shown that mutation at Cys227 causes renal failure.
Saki Takahashi +5 more
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Order Statistics Theory of Unfolding of Multimeric Proteins [PDF]
Dynamic force spectroscopy has become indispensable for the exploration of the mechanical properties of proteins. In force-ramp experiments, performed by utilizing a time-dependent pulling force, the peak forces for unfolding transitions in a multimeric protein (D)(N) are used to map the free energy landscape for unfolding for a protein domain D.
Zhmurov, A., Dima, R.I., Barsegov, V.
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Evolutionary diversification of the multimeric states of proteins [PDF]
Significance Rather than operating as single units, most proteins assemble as multimers, usually with all subunits derived from the same gene. In contrast to patterns of gene structure and genome organization, which typically exhibit substantial increases in complexity from unicellular to multicellular organisms, the structural complexity of ...
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Structure-Function Relationship of Inclusion Bodies of a Multimeric Protein [PDF]
High level expression of recombinant proteins in bacteria often results in their aggregation into inclusion bodies. Formation of inclusion bodies poses a major bottleneck in high-throughput recovery of recombinant protein. These aggregates have amyloid-like nature and can retain biological activity. Here, effect of expression temperature on the quality
Anupam Singh +3 more
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Functional multimerization of mucolipin channel proteins
AbstractMCOLN1 encodes mucolipin‐1 (TRPML1), a member of the transient receptor potential TRPML subfamily of channel proteins. Mutations in MCOLN1 cause mucolipidosis‐type IV (MLIV), a lysosomal storage disorder characterized by severe neurologic, ophthalmologic, and gastrointestinal abnormalities.
Curcio Morelli, Cyntia +6 more
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ASPPs multimerize protein phosphatase 1
Abstract Protein Phosphatase 1 (PP1) activity is thought to be spatiotemporally defined by hundreds of different regulatory subunits, but their mechanisms of action are largely unknown. The Ankyrin repeat, SH3-domain, and Proline-rich region containing Proteins (ASPPs) bind and localize PP1 to cell-cell junctions ...
Derek T. Wei +6 more
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Intracellular signaling regulators can be concentrated into membrane-free, higher ordered protein assemblies to initiate protective responses during stress — a process known as phase transition. Here, we show that a phase transition of the Caenorhabditis
Nicholas D Peterson +5 more
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Proteins of the TRIM5 family, such as TRIM5α and the related TRIMCyp, are cytoplasmic factors that can inhibit incoming retroviruses. This type of restriction requires a direct interaction between TRIM5 proteins and capsid proteins that are part of ...
Berthoux Lionel +2 more
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Cochlin, intraocular pressure regulation and mechanosensing. [PDF]
Fluid shear modulates many biological properties. How shear mechanosensing occurs in the extracellular matrix (ECM) and is transduced into cytoskeletal change remains unknown. Cochlin is an ECM protein of unknown function.
Manik Goel +5 more
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Effects of multimerization on the temporal variability of protein complex abundance [PDF]
Abstract We explore whether the process of multimerization can be used as a means to regulate noise in the abundance of functional protein complexes. Additionally, we analyze how this process affects the mean level of these functional units, response time of a gene, and temporal correlation between the numbers of expressed proteins and of the
Antti Häkkinen +4 more
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