Mikael C Bauer's research while affiliated with Lund University and other places

... Aspartic acid is found at +7 in QxQ motif family sequences. Methionine, the second sulfur-containing amino acid, has been found in the sequences at +3 and has been described as metal-binding earlier [53,54]. ...

... Experimentally, the pKa values of titratable residues in the unfolded state were measured for some proteins using NMR spectroscopy, site-directed mutagenesis and CD temperature-denaturation measurements. [21][22][23][24] Most of these experiments have indicated that the pKa values of acidic residues are lowered in unfolded state compared with intrinsic pKas. 21,22,25 These studies are used in this work to benchmark DelPhiPKa along with 3D models of unfolded states. ...

... These two global regulators coordinately control the glycolytic pathway and redox balance. In other bacteria, lactate dehydrogenase expression is important during anaerobic metabolism and is regulated by redox-sensing transcription factors [44][45][46]. How the intracellular cAMP levels of C. glutamicum are controlled in response to environmental changes merits further investigation for the understanding of the global regulatory role of GlxR. ...

... The protective mechanism of a high pH buffer on paramyosin stability is unknown. It is postulated that at high pH, the net charge of the protein increases enhancing the electrostatic repulsion between protein molecules to reduce their aggregation in the aqueous solution [35]. ...

... Kv6.1 interacts with CaM in a calcium-dependent manner (O'Connell et al., 2010). The in teraction is mediated through a C-terminal binding motif that is exclusively found in Kv6.1 and not in other KvS members (Figure 8). ...

... When split into two fragments from the loop connecting the α-helix and β-strand 3, the two fragments A (1-40 aa) and B (41-56 aa) can reconstitute at a 1:1 ratio to the native GB1 fold, albeit with a nick in the loop. [26][27][28][29][30] This non-covalent "GB1" fold has a dissociation constant Kd of ~9×10 -6 M. 26 In our previous work, we engineered a loop elongation variant of GB1, termed as GL5CC, where 5 residues were inserted into the unstructured loop and residues 42/44 were mutated to cysteines. 31,32 When split into fragments G N (residue 1-42) and G C (residues 43-61), G N and G C can reconstitute into GB1's native fold (Fig. 1A). ...

... Secretagogin-positive cells are often found in vicinity to the ventricular system with dendrites oriented along the pial surface, which might display a role in releasing neuroactive substances into the cerebrospinal fluid (Mulder et al., 2009(Mulder et al., , 2010. Further assumed functions are a neuroendocrine role in vesicle exocytosis (Bauer et al., 2011), microtubules dynamics (Maj et al., 2010(Maj et al., , 2012, and a possible neuroprotective role against the neurodegeneration as in Alzheimer disease (Attems et al., 2008). Altered secretagogin expression has been described to possibly reflect cellular dysfunction of locus coeruleus neurons in Alzheimer disease (Zahola et al., 2019). ...

... To test zinc binding to ZIP4-ECD, we conducted zinc titration in the presence of a zinc-specific fluorescence probe, FluoZin-1, of which fluorescence intensity increases upon zinc binding [17]. Zinc-specific fluorescence probes have been used in estimating zinc-binding affinity of a variety of proteins through competition titration [18,19]. As shown in Supplementary Figure S1A, we firstly measured the zinc-binding affinity of FluoZin-1 under our experimental condition. ...

... The interactions among CRAC2A and STIM1 or Orai1 involve the coiled-coil domain, as well as the proline/lysine rich segment of the former, and considering Orai1, map to the N-terminal domain with K85 and K87 serving as critical interaction sites (Figure 1) [21]. It is worth mentioning that the sites of CRACR2A-STIM1 and CRACR2A-Orai1 interaction overlap with these described to bind calmodulin (CaM) in the presence of Ca 2+ , explicitly including hOrai1 and the lysin-rich domain of hSTIM1 [21,83]. CRAC2A associations with both basic components of the CRAC channel complex are associated with a stringent dependence on the activation state, as these are promoted successively to store depletion yet exclusively under Ca 2+ -free conditions, while otherwise strong binding between the mentioned domains of STIM1/Orai1 and CRACR2A was reported to vanquish if exposed to buffer solutions supplemented with 2 mM Ca 2+ [21]. ...

... Several studies have also shown that millimolar ATP could inhibit the activity of NAD + -substrate enzymes, such as SIRT1 (Kang et al., 2017), PARP (Toledano et al., 2012), and CD38 (Takasawa et al., 1993). In addition, AXP competes the binding of NAD + to the NAD + /NADH sensing transcription factors such as Rex (Wang et al., 2008) or NadR (Grose et al., 2005). These reports suggested that the activities of these important enzymes and transcription factors might be determined actually by the NAD + /AXP ratio, but not the NAD + level. ...