Subjects -> BIOLOGY (Total: 3496 journals)
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PHYSIOLOGY (73 journals)

Showing 1 - 73 of 73 Journals sorted alphabetically
Acta Physiologiae Plantarum     Hybrid Journal   (Followers: 4)
Acta Physiologica     Hybrid Journal   (Followers: 7)
Acta Physiologica Hungarica     Full-text available via subscription   (Followers: 4)
Advances in Insect Physiology     Full-text available via subscription   (Followers: 2)
Advances in Physiology Education     Open Access   (Followers: 6)
AJP Cell Physiology     Hybrid Journal   (Followers: 19)
AJP Gastrointestinal and Liver Physiology     Hybrid Journal   (Followers: 8)
AJP Heart and Circulatory Physiology     Hybrid Journal   (Followers: 12)
AJP Lung Cellular and Molecular Physiology     Hybrid Journal   (Followers: 3)
AJP Regulatory Integrative and Comparative Physiology     Hybrid Journal   (Followers: 15)
AJP Renal Physiology     Hybrid Journal   (Followers: 8)
American Journal of Plant Physiology     Open Access   (Followers: 13)
Anatomy & Physiology : Current Research     Open Access   (Followers: 9)
Angiogenesis     Hybrid Journal   (Followers: 3)
Annual Review of Physiology     Full-text available via subscription   (Followers: 14)
Archives of Anatomy and Physiology     Open Access   (Followers: 2)
Archives of Insect Biochemistry and Physiology     Hybrid Journal   (Followers: 1)
Biochemistry & Physiology : Open Access     Open Access   (Followers: 2)
BMC Physiology     Open Access   (Followers: 4)
Brazilian Journal of Plant Physiology     Open Access   (Followers: 3)
Canadian Journal of Physiology and Pharmacology     Hybrid Journal   (Followers: 2)
Cellular Physiology and Biochemistry     Open Access   (Followers: 4)
Clinical and Experimental Pharmacology and Physiology     Hybrid Journal   (Followers: 8)
Clinical Physiology and Functional Imaging     Hybrid Journal  
Comparative Biochemistry and Physiology Part A: Molecular & Integrative Physiology     Hybrid Journal   (Followers: 8)
Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology     Hybrid Journal   (Followers: 4)
Comparative Biochemistry and Physiology Part C: Toxicology & Pharmacology     Hybrid Journal   (Followers: 6)
Comparative Biochemistry and Physiology Part D: Genomics and Proteomics     Hybrid Journal   (Followers: 2)
Comparative Exercise Physiology     Hybrid Journal   (Followers: 24)
Conservation Physiology     Open Access   (Followers: 3)
Current Opinion in Physiology     Hybrid Journal  
European Journal of Applied Physiology     Hybrid Journal   (Followers: 48)
Experimental Physiology     Hybrid Journal   (Followers: 11)
Fish Physiology     Full-text available via subscription   (Followers: 5)
Fish Physiology and Biochemistry     Hybrid Journal   (Followers: 3)
Frontiers in Physiology     Open Access   (Followers: 5)
Human Physiology     Hybrid Journal   (Followers: 5)
Journal of Animal Physiology and Animal Nutrition     Hybrid Journal   (Followers: 10)
Journal of Applied Physiology     Hybrid Journal   (Followers: 68)
Journal of Cellular Physiology     Hybrid Journal   (Followers: 8)
Journal of Comparative Physiology A: Neuroethology, Sensory, Neural, and Behavioral Physiology     Hybrid Journal   (Followers: 12)
Journal of Comparative Physiology B : Biochemical, Systemic, and Environmental Physiology     Hybrid Journal   (Followers: 5)
Journal of Evolutionary Biochemistry and Physiology     Hybrid Journal  
Journal of General Physiology     Full-text available via subscription   (Followers: 4)
Journal of Insect Physiology     Hybrid Journal   (Followers: 3)
Journal of Morphology     Hybrid Journal   (Followers: 7)
Journal of Neurophysiology     Hybrid Journal   (Followers: 28)
Journal of Physiology and Biochemistry     Hybrid Journal   (Followers: 3)
Journal of Physiology-Paris     Hybrid Journal   (Followers: 2)
Journal of Plant Physiology     Hybrid Journal   (Followers: 9)
Pathophysiology     Full-text available via subscription   (Followers: 2)
Pesticide Biochemistry and Physiology     Hybrid Journal   (Followers: 4)
Pflugers Archiv European Journal of Physiology     Hybrid Journal   (Followers: 3)
Physiologia Plantarum     Hybrid Journal  
Physiological and Molecular Plant Pathology     Hybrid Journal   (Followers: 3)
Physiological Entomology     Hybrid Journal   (Followers: 3)
Physiological Genomics     Hybrid Journal  
Physiological Measurement     Full-text available via subscription   (Followers: 5)
Physiological Reports     Open Access   (Followers: 3)
Physiological Reviews     Hybrid Journal   (Followers: 4)
Physiology     Hybrid Journal   (Followers: 3)
Physiology and Molecular Biology of Plants     Hybrid Journal  
Plant and Cell Physiology     Hybrid Journal   (Followers: 11)
Plant Physiology     Full-text available via subscription   (Followers: 24)
Plant Physiology and Biochemistry     Hybrid Journal   (Followers: 10)
Psychophysiology     Hybrid Journal   (Followers: 7)
Respiratory Physiology & Neurobiology     Hybrid Journal   (Followers: 4)
Reviews of Physiology, Biochemistry and Pharmacology     Hybrid Journal   (Followers: 4)
Russian Journal of Plant Physiology     Hybrid Journal   (Followers: 4)
Systems Biomedicine     Hybrid Journal  
The Journal of Physiological Sciences     Hybrid Journal   (Followers: 1)
The Journal of Physiology     Hybrid Journal   (Followers: 10)
Tree Physiology     Hybrid Journal   (Followers: 7)
Similar Journals
Journal Cover
Journal of General Physiology
Journal Prestige (SJR): 2.623
Citation Impact (citeScore): 3
Number of Followers: 4  
  Full-text available via subscription Subscription journal
ISSN (Print) 0022-1295 - ISSN (Online) 1540-7748
Published by Rockefeller University Press Homepage  [3 journals]
  • Membrane-mediated interaction drives mitochondrial ATPase assembly and
           cristae formation
    • Authors: Cui; Q.
      Pages: 777 - 780
      Abstract: Because of rapid progress in various imaging and structural biology techniques, it is increasingly recognized that components of cellular membranes self-organize into remarkable structures with rich architectural features. Striking examples include the immunological synapse (Grakoui et al.,...
      PubDate: 2018-06-04T06:54:59-07:00
      DOI: 10.1085/jgp.201812077
      Issue No: Vol. 150, No. 6 (2018)
  • The acid test for pH-dependent gating in cloned HV1 channels
    • Authors: Islas; L. D.
      Pages: 781 - 782
      Abstract: Cells interact with their milieu by means of cell membranes, and several ingenious mechanisms have evolved to mediate these interactions. Ion channels occupy a privileged position among these mechanisms, being responsible for regulated ion flux in response to changes...
      PubDate: 2018-06-04T06:54:59-07:00
      DOI: 10.1085/jgp.201812076
      Issue No: Vol. 150, No. 6 (2018)
  • The high-affinity calcium sensor synaptotagmin-7 serves multiple roles in
           regulated exocytosis
    • Authors: MacDougall, D. D; Lin, Z, Chon, N. L, Jackman, S. L, Lin, H, Knight, J. D, Anantharam, A.
      Pages: 783 - 807
      Abstract: Synaptotagmin (Syt) proteins comprise a 17-member family, many of which trigger exocytosis in response to calcium. Historically, most studies have focused on the isoform Syt-1, which serves as the primary calcium sensor in synchronous neurotransmitter release. Recently, Syt-7 has become a topic of broad interest because of its extreme calcium sensitivity and diversity of roles in a wide range of cell types. Here, we review the known and emerging roles of Syt-7 in various contexts and stress the importance of its actions. Unique functions of Syt-7 are discussed in light of recent imaging, electrophysiological, and computational studies. Particular emphasis is placed on Syt-7–dependent regulation of synaptic transmission and neuroendocrine cell secretion. Finally, based on biochemical and structural data, we propose a mechanism to link Syt-7’s role in membrane fusion with its role in subsequent fusion pore expansion via strong calcium-dependent phospholipid binding.
      Keywords: Biophysics, Cellular Physiology, Membrane Transport
      PubDate: 2018-06-04T06:54:59-07:00
      DOI: 10.1085/jgp.201711944
      Issue No: Vol. 150, No. 6 (2018)
  • Cardiomyopathy mutation (F88L) in troponin T abolishes length dependency
           of myofilament Ca2+ sensitivity
    • Authors: Reda, S. M; Chandra, M.
      Pages: 809 - 819
      Abstract: Recent clinical studies have revealed a new hypertrophic cardiomyopathy–associated mutation (F87L) in the central region of human cardiac troponin T (TnT). However, despite its implication in several incidences of sudden cardiac death in young and old adults, whether F87L is associated with cardiac contractile dysfunction is unknown. Because the central region of TnT is important for modulating the muscle length–mediated recruitment of new force-bearing cross-bridges (XBs), we hypothesize that the F87L mutation causes molecular changes that are linked to the length-dependent activation of cardiac myofilaments. Length-dependent activation is important because it contributes significantly to the Frank–Starling mechanism, which enables the heart to vary stroke volume as a function of changes in venous return. We measured steady-state and dynamic contractile parameters in detergent-skinned guinea pig cardiac muscle fibers reconstituted with recombinant guinea pig wild-type TnT (TnTWT) or the guinea pig analogue (TnTF88L) of the human mutation at two different sarcomere lengths (SLs): short (1.9 µm) and long (2.3 µm). TnTF88L increases pCa50 (–log [Ca2+]free required for half-maximal activation) to a greater extent at short SL than at long SL; for example, pCa50 increases by 0.25 pCa units at short SL and 0.17 pCa units at long SL. The greater increase in pCa50 at short SL leads to the abolishment of the SL-dependent increase in myofilament Ca2+ sensitivity (pCa50) in TnTF88L fibers, pCa50 being 0.10 units in TnTWT fibers but only 0.02 units in TnTF88L fibers. Furthermore, at short SL, TnTF88L attenuates the negative impact of strained XBs on force-bearing XBs and augments the magnitude of muscle length–mediated recruitment of new force-bearing XBs. Our findings suggest that the TnTF88L-mediated effects on cardiac thin filaments may lead to a negative impact on the Frank–Starling mechanism.
      Keywords: Biophysics
      PubDate: 2018-06-04T06:55:00-07:00
      DOI: 10.1085/jgp.201711974
      Issue No: Vol. 150, No. 6 (2018)
  • Ligand binding and activation properties of the purified bacterial cyclic
           nucleotide-gated channel SthK
    • Authors: Schmidpeter, P. A. M; Gao, X, Uphadyay, V, Rheinberger, J, Nimigean, C. M.
      Pages: 821 - 834
      Abstract: Cyclic nucleotide–modulated ion channels play several essential physiological roles. They are involved in signal transduction in photoreceptors and olfactory sensory neurons as well as pacemaking activity in the heart and brain. Investigations of the molecular mechanism of their actions, including structural and electrophysiological characterization, are restricted by the availability of stable, purified protein obtained from accessible systems. Here, we establish that SthK, a cyclic nucleotide–gated (CNG) channel from Spirochaeta thermophila, is an excellent model for investigating the gating of eukaryotic CNG channels at the molecular level. The channel has high sequence similarity with its eukaryotic counterparts and was previously reported to be activated by cyclic nucleotides in patch-clamp experiments with Xenopus laevis oocytes. We optimized protein expression and purification to obtain large quantities of pure, homogeneous, and active recombinant SthK protein from Escherichia coli. A negative-stain electron microscopy (EM) single-particle analysis indicated that this channel is a promising candidate for structural studies with cryo-EM. Using radioactivity and fluorescence flux assays, as well as single-channel recordings in lipid bilayers, we show that the protein is partially activated by micromolar concentrations of cyclic adenosine monophosphate (cAMP) and that channel activity is increased by depolarization. Unlike previous studies, we find that cyclic guanosine monophosphate (cGMP) is also able to activate SthK, but with much lower efficiency than cAMP. The distinct sensitivities to different ligands resemble eukaryotic CNG and hyperpolarization-activated and cyclic nucleotide–modulated channels. Using a fluorescence binding assay, we show that cGMP and cAMP bind to SthK with similar apparent affinities, suggesting that the large difference in channel activation by cAMP or cGMP is caused by the efficacy with which each ligand promotes the conformational changes toward the open state. We conclude that the functional characteristics of SthK reported here will permit future studies to analyze ligand gating and discrimination in CNG channels.
      Keywords: Biochemistry, Biophysics, Membrane Transport
      PubDate: 2018-06-04T06:55:00-07:00
      DOI: 10.1085/jgp.201812023
      Issue No: Vol. 150, No. 6 (2018)
  • Exotic properties of a voltage-gated proton channel from the snail
           Helisoma trivolvis
    • Authors: Thomas, S; Cherny, V. V, Morgan, D, Artinian, L. R, Rehder, V, Smith, S. M. E, DeCoursey, T. E.
      Pages: 835 - 850
      Abstract: Voltage-gated proton channels, HV1, were first reported in Helix aspersa snail neurons. These H+ channels open very rapidly, two to three orders of magnitude faster than mammalian HV1. Here we identify an HV1 gene in the snail Helisoma trivolvis and verify protein level expression by Western blotting of H. trivolvis brain lysate. Expressed in mammalian cells, HtHV1 currents in most respects resemble those described in other snails, including rapid activation, 476 times faster than hHV1 (human) at pHo 7, between 50 and 90 mV. In contrast to most HV1, activation of HtHV1 is exponential, suggesting first-order kinetics. However, the large gating charge of ~5.5 e0 suggests that HtHV1 functions as a dimer, evidently with highly cooperative gating. HtHV1 opening is exquisitely sensitive to pHo, whereas closing is nearly independent of pHo. Zn2+ and Cd2+ inhibit HtHV1 currents in the micromolar range, slowing activation, shifting the proton conductance–voltage (gH-V) relationship to more positive potentials, and lowering the maximum conductance. This is consistent with HtHV1 possessing three of the four amino acids that coordinate Zn2+ in mammalian HV1. All known HV1 exhibit pH-dependent gating that results in a 40-mV shift of the gH-V relationship for a unit change in either pHo or pHi. This property is crucial for all the functions of HV1 in many species and numerous human cells. The HtHV1 channel exhibits normal or supernormal pHo dependence, but weak pHi dependence. Under favorable conditions, this might result in the HtHV1 channel conducting inward currents and perhaps mediating a proton action potential. The anomalous pH-dependent gating of HtHV1 channels suggests a structural basis for this important property, which is further explored in this issue (Cherny et al. 2018. J. Gen. Physiol.
      Keywords: Biophysics, Membrane Transport, Molecular Physiology
      PubDate: 2018-06-04T06:55:00-07:00
      DOI: 10.1085/jgp.201711967
      Issue No: Vol. 150, No. 6 (2018)
  • Histidine168 is crucial for {Delta}pH-dependent gating of the human
           voltage-gated proton channel, hHV1
    • Authors: Cherny, V. V; Morgan, D, Thomas, S, Smith, S. M. E, DeCoursey, T. E.
      Pages: 851 - 862
      Abstract: We recently identified a voltage-gated proton channel gene in the snail Helisoma trivolvis, HtHV1, and determined its electrophysiological properties. Consistent with early studies of proton currents in snail neurons, HtHV1 opens rapidly, but it unexpectedly exhibits uniquely defective sensitivity to intracellular pH (pHi). The H+ conductance (gH)-V relationship in the voltage-gated proton channel (HV1) from other species shifts 40 mV when either pHi or pHo (extracellular pH) is changed by 1 unit. This property, called pH-dependent gating, is crucial to the functions of HV1 in many species and in numerous human tissues. The HtHV1 channel exhibits normal pHo dependence but anomalously weak pHi dependence. In this study, we show that a single point mutation in human hHV1—changing His168 to Gln168, the corresponding residue in HtHV1—compromises the pHi dependence of gating in the human channel so that it recapitulates the HtHV1 response. This location was previously identified as a contributor to the rapid gating kinetics of HV1 in Strongylocentrotus purpuratus. His168 mutation in human HV1 accelerates activation but accounts for only a fraction of the species difference. H168Q, H168S, or H168T mutants exhibit normal pHo dependence, but changing pHi shifts the gH-V relationship on average by
      Keywords: Biophysics, Membrane Transport, Protein Structure and Dynamics
      PubDate: 2018-06-04T06:55:00-07:00
      DOI: 10.1085/jgp.201711968
      Issue No: Vol. 150, No. 6 (2018)
  • Coupling between an electrostatic network and the Zn2+ binding site
           modulates Hv1 activation
    • Authors: De La Rosa, V; Bennett, A. L, Ramsey, I. S.
      Pages: 863 - 881
      Abstract: The voltage sensor (VS) domain in Hv1 proton channels mediates a voltage-dependent and H+-selective "aqueous" conductance (GAQ) that is potently modulated by extracellular Zn2+. Although two conserved His residues are required for Zn2+ effects on GAQ gating, the atomic structure of the Zn2+ coordination site and mechanism by which extracellular Zn2+ stabilizes a closed-state conformation remain unknown. Here we use His mutagenesis to identify residues that increase Zn2+ potency and are therefore likely to participate in first solvation shell interactions with Zn2+. Experimental Zn2+-mapping data were then used to constrain the structure of a new resting-state Hv1 model (Hv1 F). Molecular dynamics (MD) simulations show how protein and water atoms directly contribute to octahedral Zn2+ coordination spheres in Zn2+-bound and -unbound Hv1 F models. During MD simulations, we observed correlated movements of Zn2+-interacting side chains and residues in a highly conserved intracellular Coulombic network (ICN) that contains highly conserved Arg "gating charges" in S4 as well as acidic "counter-charges" in S2 and S3 and is known to control VS activation, suggesting that occupancy of the extracellular Zn2+ site is conformationally coupled to reorganization of the ICN. To test this hypothesis, we neutralized an ICN Glu residue (E153) and show that in addition to shifting GAQ activation to more negative voltages, E153A also decreases Zn2+ potency. We speculate that extracellular gating-modifier toxins and other ligands may use a generally similar long-range conformational coupling mechanism to modulate VS activation in related ion channel proteins.
      Keywords: Molecular Physiology, Protein Structure and Dynamics, Molecular Pharmacology
      PubDate: 2018-06-04T06:55:00-07:00
      DOI: 10.1085/jgp.201711822
      Issue No: Vol. 150, No. 6 (2018)
  • The AKAP Cypher/Zasp contributes to {beta}-adrenergic/PKA stimulation of
           cardiac CaV1.2 calcium channels
    • Authors: Yu, H; Yuan, C, Westenbroek, R. E, Catterall, W. A.
      Pages: 883 - 889
      Abstract: Stimulation of the L-type Ca2+ current conducted by CaV1.2 channels in cardiac myocytes by the β-adrenergic/protein kinase A (PKA) signaling pathway requires anchoring of PKA to the CaV1.2 channel by an A-kinase anchoring protein (AKAP). However, the AKAP(s) responsible for regulation in vivo remain unknown. Here, we test the role of the AKAP Cypher/Zasp in β-adrenergic regulation of CaV1.2 channels using physiological studies of cardiac ventricular myocytes from young-adult mice lacking the long form of Cypher/Zasp (LCyphKO mice). These myocytes have increased protein levels of CaV1.2, PKA, and calcineurin. In contrast, the cell surface density of CaV1.2 channels and the basal Ca2+ current conducted by CaV1.2 channels are significantly reduced without substantial changes to kinetics or voltage dependence. β-adrenergic regulation of these L-type Ca2+ currents is also significantly reduced in myocytes from LCyphKO mice, whether calculated as a stimulation ratio or as net-stimulated Ca2+ current. At 100 nM isoproterenol, the net β-adrenergic–Ca2+ current conducted by CaV1.2 channels was reduced to 39 ± 12% of wild type. However, concentration–response curves for β-adrenergic stimulation of myocytes from LCyphKO mice have concentrations that give a half-maximal response similar to those for wild-type mice. These results identify Cypher/Zasp as an important AKAP for β-adrenergic regulation of cardiac CaV1.2 channels. Other AKAPs may work cooperatively with Cypher/Zasp to give the full magnitude of β-adrenergic regulation of CaV1.2 channels observed in vivo.
      Keywords: Molecular Physiology, Signal Transduction
      PubDate: 2018-06-04T06:55:00-07:00
      DOI: 10.1085/jgp.201711818
      Issue No: Vol. 150, No. 6 (2018)
  • Correction: Otopetrin-1: A sour-tasting proton channel
    • Authors: Ramsey, I. S; DeSimone, J. A.
      Pages: 891 - 891
      Abstract: Vol. 150, No. 3, March 5, 2018. 10.1085/jgp.201812003 After publication of this article, several errors were brought to our attention, which we have corrected as follows, with bold indicating insertions and strikethrough indicating deletions. Both the HTML...
      PubDate: 2018-06-04T06:55:00-07:00
      DOI: 10.1085/jgp.20181200305102018c
      Issue No: Vol. 150, No. 6 (2018)
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Heriot-Watt University
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