Dataset Information

Nudging the N170 forward with prior stimulation-Bridging the gap between N170 and recognition potential.

ABSTRACT: Evoked response potentials are often divided up into numerous components, each with their own body of literature. But is there less variety than we might suppose? In this study, we nudge one component into looking like another. Both the N170 and recognition potential (RP) are N1 components in response to familiar objects. However, the RP is often measured with a forward mask that ends at stimulus onset whereas the N170 is often measured with no masking at all. This study investigates how inter-stimulus interval (ISI) may delay and distort the N170 into an RP by manipulating the temporal gap (ISI) between forward mask and target. The results revealed reverse relationships between the ISI on the one hand, and the N170 latency, single-trial N1 jitter (an approximation of N1 width) and reaction time on the other hand. Importantly, we find that scalp topographies have a unique signature at the N1 peak across all conditions, from the longest gap (N170) to the shortest (RP). These findings prove that the mask-delayed N1 is still the same N170, even under conditions that are normally associated with a different component like the RP. In general, our results suggest greater synthesis in the study of event related potential components.

SUBMITTER: Luo C

PROVIDER: S-EPMC8837586 | biostudies-literature | 2022 Mar

REPOSITORIES: biostudies-literature

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Nudging the N170 forward with prior stimulation-Bridging the gap between N170 and recognition potential.

Luo Canhuang C Chen Wei W VanRullen Rufin R Zhang Ye Y Gaspar Carl Michael CM

Human brain mapping 20211117 4

Evoked response potentials are often divided up into numerous components, each with their own body of literature. But is there less variety than we might suppose? In this study, we nudge one component into looking like another. Both the N170 and recognition potential (RP) are N1 components in response to familiar objects. However, the RP is often measured with a forward mask that ends at stimulus onset whereas the N170 is often measured with no masking at all. This study investigates how inter-s ...[more]

PMID: 34786780

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Project description:The Na(+)-glucose cotransporter hSGLT1 is a member of a class of membrane proteins that harness Na(+) electrochemical gradients to drive uphill solute transport. Although hSGLT1 belongs to one gene family (SLC5), recent structural studies of bacterial Na(+) cotransporters have shown that Na(+) transporters in different gene families have the same structural fold. We have constructed homology models of hSGLT1 in two conformations, the inward-facing occluded (based on vSGLT) and the outward open conformations (based on Mhp1), mutated in turn each of the conserved gates and ligand binding residues, expressed the SGLT1 mutants in Xenopus oocytes, and determined the functional consequences using biophysical and biochemical assays. The results establish that mutating the ligand binding residues produces profound changes in the ligand affinity (the half-saturation concentration, K(0.5)); e.g., mutating sugar binding residues increases the glucose K(0.5) by up to three orders of magnitude. Mutation of the external gate residues increases the Na(+) to sugar transport stoichiometry, demonstrating that these residues are critical for efficient cotransport. The changes in phlorizin inhibition constant (K(i)) are proportional to the changes in sugar K(0.5), except in the case of F101C, where phlorizin K(i) increases by orders of magnitude without a change in glucose K(0.5). We conclude that glucose and phlorizin occupy the same binding site and that F101 is involved in binding to the phloretin group of the inhibitor. Substituted-cysteine accessibility methods show that the cysteine residues at the position of the gates and sugar binding site are largely accessible only to external hydrophilic methanethiosulfonate reagents in the presence of external Na(+), demonstrating that the external sugar (and phlorizin) binding vestibule is opened by the presence of external Na(+) and closes after the binding of sugar and phlorizin. Overall, the present results provide a bridge between kinetics and structural studies of cotransporters.

Dataset Information

Nudging the N170 forward with prior stimulation-Bridging the gap between N170 and recognition potential.

Publications

Nudging the N170 forward with prior stimulation-Bridging the gap between N170 and recognition potential.

Similar Datasets

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