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1.

001-es BibID:BIBFORM003917
Első szerző:Csősz Éva (biokémikus, molekuláris biológus)
Cím:Substrate preference of transglutaminase 2 revealed by logistic regression analysis and intrinsic disorder examination / Csősz, É., Bagossi, P., Nagy, Z., Dosztányi, Zs., Simon, I., Fésüs, L.
Dátum:2008
Megjegyzések:Tissue transglutaminase (TG2) catalyzes the Ca(2+)-dependent posttranslational modification of proteins via formation of isopeptide bonds between their glutamine and lysine residues. Although substrate specificity of TG2 has been studied repeatedly at the sequence level, no clear consensus sequences have been determined so far. With the use of the extensive structural information on TG2 substrate proteins listed in TRANSDAB Wiki database, a slight preference of TG2 for glutamine and lysine residues situated in turns could be observed. When the spatial environment of the favored glutamine and lysine residues was analyzed with logistic regression, the presence of specific amino acid patterns was identified. By using the occurrence of the predictor amino acids as selection criteria, several polypeptides were predicted and later identified as novel in vitro substrates for TG2. By studying the sequence of TG2 substrate proteins lacking available crystal structure, the strong favorable influence on substrate selection of the presence of substrate glutamine and lysine residues in intrinsically disordered regions could also be revealed. The collected structural data have provided novel understanding of how this versatile enzyme selects its substrates in various cell compartments and tissues.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Journal of Molecular Biology 383 : 2 (2008), p. 390-402. -
További szerzők:Bagossi Péter (1966-2011) (biokémikus, vegyész) Nagy Zoltán (számítástechnikus) Dosztányi Zsuzsanna Simon István Fésüs László (1947-) (orvos biokémikus)
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2.

001-es BibID:BIBFORM019817
Első szerző:Fang, Bin
Cím:Structural and kinetic analysis of caspase-3 reveals role for s5 binding site in substrate recognition / Bin Fang, Peter I. Boross, Jozsef Tozser, Irene T. Weber
Dátum:2006
ISSN:0022-2836
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Journal of Molecular Biology 360 : 3 (2006), p. 654-666. -
További szerzők:Boross Péter (1972-) (biokémikus, vegyész) Tőzsér József (1959-) (molekuláris biológus, biokémikus, vegyész) Weber, Irene T.
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3.

001-es BibID:BIBFORM073127
035-os BibID:(WoS)000439402200002 (Scopus)85043977696
Első szerző:Fuxreiter Mónika (kutató vegyész)
Cím:Fuzziness in Protein Interactions : a Historical Perspective / Fuxreiter Monika
Dátum:2018
ISSN:0022-2836
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Journal Of Molecular Biology. - 430 : 16 (2018), p. 2278-2287. -
Pályázati támogatás:GINOP-2.3.2-15-2016-00044
GINOP
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4.

001-es BibID:BIBFORM073722
Első szerző:Grant, William B.
Cím:Why vitamin D clinical trials should be based on 25-hydroxyvitamin D concentrations / Grant William B., Boucher Barbara J., Bhattoa Harjit P., Lahore Henry
Dátum:2018
ISSN:0960-0760
Megjegyzések:Many health benefits are attributed to vitamin D, with those findings supported mostly by observational outcome studies of relationships to serum 25-hydroxyvitamin D [25(OH)D]. However, many randomized controlled trials (RCTs) aiming to confirm those findings have failed, perhaps because serum 25(OH)D is an index of UVB exposure and non-vitamin D mechanisms or because disease reduces serum 25(OH)D content. But the most likely reason for that failure is inappropriate design, conduct, analysis, and interpretation of RCTs. Most RCTs used principles designed to test pharmaceutical drugs; that design incorporates the assumptions that the RCT is the sole source of the agent and that dose-response relationships are linear. However, neither assumption is true for vitamin D, since neither vitamin D dose-responses or health outcome-serum 25(OH)D concentration relationships are linear?larger changes being induced with low rather than high baseline 25(OH)D values. Here, we propose a hybrid observational approach to vitamin D RCT design, based primarily on serum 25(OH)D concentration, requiring an understanding of serum 25(OH)D concentration-health outcome relationships, measuring baseline 25(OH)D values, recruiting non-replete subjects, measuring serum 25(OH)D during the trial for adjustment of supplemental doses for achievement of pretrial selection of target 25(OH)D values, where possible, and analyzing health outcomes in relation to those data rather than solely to vitamin D dosages.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Vitamin D
Randomized controlled trial
clinical trial
25-hydroxyvitamin D
observational study
Megjelenés:Journal Of Steroid Biochemistry And Molecular Biology. - 177 (2018), p. 266-269. -
További szerzők:Boucher, Barbara Bhattoa Harjit Pal (1973-) (laboratóriumi szakorvos) Lahore, Henry
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5.

001-es BibID:BIBFORM067622
Első szerző:Grant, William B.
Cím:Seasonal variations of U.S. mortality rates : roles of solar ultraviolet-B doses, vitamin D, gene expression, and infections / Grant William B., Bhattoa Harjit Pal, Boucher Barbara J.
Dátum:2017
Megjegyzések:Death rates in the U.S. show a pronounced seasonality. The broad seasonal variation shows about 25% higher death rates in winter than in summer with an additional few percent increase associated with the Christmas and New Year's holidays. A pronounced increase in death rates also starts in mid-September, shortly after the school year begins. The causes of death with large contributions to the observed seasonality include diseases of the circulatory system; the respiratory system; the digestive system; and endocrine, nutritional, and metabolic diseases. Researchers have identified several factors showing seasonal variation that could possibly explain the seasonal variations in mortality rate. These factors include seasonal variations in solar ultraviolet-B(UVB) doses and serum 25-hydroxyvitamin D [25(OH)D] concentrations, gene expression, ambient temperature and humidity, UVB effects on environmental pathogen load, environmental pollutants and allergens, and photoperiod (or length of day). The factors with the strongest support in this analysis are seasonal variations in solar UVB doses and 25(OH)D concentrations. In the U.S., population mean 25(OH)D concentrations range from 21 ng/mL in March to 28 ng/mL in August. Measures to ensure that all people had 25(OH)D concentrations >36 ng/mL year round would probably reduce death rates significantly.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Vitamin D
Cardiovascular disease
Mortality rate
Season
Respiratory tract infections
Temperature
Gene expression
Megjelenés:The Journal of Steroid Biochemistry and Molecular Biology 173 (2017), p. 5-12. -
További szerzők:Bhattoa Harjit Pal (1973-) (laboratóriumi szakorvos) Boucher, Barbara
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6.

001-es BibID:BIBFORM096180
035-os BibID:(WoS)000709464800005 (Scopus)85107471683
Első szerző:Hardenberg, Maarten
Cím:Observation of an α-synuclein liquid droplet state and its maturation into Lewy body-like assemblies / Maarten C. Hardenberg, Tessa Sinnige, Sam Casford, Samuel T. Dada, Chetan Poudel, Elizabeth A. Robinson, Monika Fuxreiter, Clemens F. Kaminksi, Gabriele S. Kaminski-Schierle, Ellen A. A. Nollen, Christopher M. Dobson, Michele Vendruscolo
Dátum:2021
ISSN:1674-2788 1759-4685
Megjegyzések:Misfolded α-synuclein is a major component of Lewy bodies, which are a hallmark of Parkinson's disease (PD). A large body of evidence shows that α-synuclein can aggregate into amyloid fibrils, but the relationship between α-synuclein self-assembly and Lewy body formation remains unclear. Here, we show, both in vitro and in a Caenorhabditis elegans model of PD, that α-synuclein undergoes liquid?liquid phase separation by forming a liquid droplet state, which converts into an amyloid-rich hydrogel with Lewy-body-like properties. This maturation process towards the amyloid state is delayed in the presence of model synaptic vesicles in vitro. Taken together, these results suggest that the formation of Lewy bodies may be linked to the arrested maturation of α-synuclein condensates in the presence of lipids and other cellular components.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Parkinson's disease
liquid?liquid phase separation
α-synuclein
Megjelenés:Journal of Molecular Cell Biology. - 13 : 4 (2021), p. 282-294. -
További szerzők:Sinnige, Tessa Casford, Sam Dada, Samuel T. Poudel, Chetan Robinson, Elizabeth A. Fuxreiter Mónika (1969-) (kutató vegyész) Kaminksi, Clemens F. Kaminski-Schierle, Gabriele S. Nollen, Ellen A. A. Dobson, Christopher M. Vendruscolo, Michele
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7.

001-es BibID:BIBFORM108790
035-os BibID:(Scopus)85148381582 (WoS)000944102100001
Első szerző:Hoffka Gyula (vegyész)
Cím:Self-inhibited state of Venezuelan equine encephalitis virus (VEEV) nsP2 cysteine protease : a crystallographic and molecular dynamics analysis / Gyula Hoffka, George T. Lountos, Danielle Needle, Alexander Wlodawer, David S. Waugh, József Tőzsér, János András Mótyán
Dátum:2023
ISSN:0022-2836
Megjegyzések:The Venezuelan equine encephalitis virus (VEEV) belongs to the Togaviridae family and is pathogenic to both humans and equines. The VEEV non-structural protein 2 (nsP2) is a cysteine protease (nsP2pro) that processes the polyprotein and thus it is a drug target for inhibitor discovery. The atomic structure of the VEEV nsP2 catalytic domain was previously characterized by both X-ray crystallography and computational studies. A modified nsP2pro harboring a N475A mutation in the N terminus was observed to exhibit an unexpected conformation: the N-terminal residues bind to the active site, mimicking binding of a substrate. The large conformational change of the N terminus was assumed to be induced by the N475A mutation, as N475 has an important role in stabilization of the N terminus and the active site. This conformation was first observed in the N475A mutant, but we also found it while determining a crystal structure of the catalytically active nsP2pro containing the wild-type N475 active site residue and K741A/K767A surface entropy reduction mutations. This suggests that the N475A mutation is not a prerequisite for self-inhibition. Here, we describe a high resolution (1.46 ?A) crystal structure of a truncated nsP2pro (residues 463-785, K741A/K767A) and analyze the structure further by molecular dynamics to study the active and self-inhibited conformations of nsP2pro and its N475A mutant. A comparison of the different conformations of the N-terminal residues sheds a light on the interactions that play an important role in the stabilization of the enzyme.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Venezuelan equine encephalitis virus
protease
alphavirus
crystallography
molecular dynamics
Megjelenés:Journal Of Molecular Biology. - 435 : 6 (2023), p. 1-20. -
További szerzők:Lountos, George T. Needle, Danielle Wlodawer, Alexander Waugh, David S. Tőzsér József (1959-) (molekuláris biológus, biokémikus, vegyész) Mótyán János András (1981-) (biokémikus, molekuláris biológus)
Pályázati támogatás:TKP2021-EGA-20 (Biotechnology)
Egyéb
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8.

001-es BibID:BIBFORM040663
Első szerző:Liu, Fengling
Cím:Kinetic, Stability, and Structural Changes in High-resolution Crystal Structures of HIV-1 Protease with Drug-resistant Mutations L24I, I50V, and G73S / Liu Fengling, Boross Peter I., Wang Yuan-Fang, Tozser Jozsef, Louis John M., Harrison Robert W., Weber Irene T.
Dátum:2005
ISSN:0022-2836
Megjegyzések:The crystal structures, dimer stabilities, and kinetics have been analyzed for wild-type human immunodeficiency virus type 1 (HIV-1) protease (PR) and resistant mutants PR(L24I), PR(I50V), and PR(G73S) to gain insight into the molecular basis of drug resistance. The mutations lie in different structural regions. Mutation I50V alters a residue in the flexible flap that interacts with the inhibitor, L24I alters a residue adjacent to the catalytic Asp25, and G73S lies at the protein surface far from the inhibitor-binding site. PR(L24I) and PR(I50V), showed a 4% and 18% lower k(cat)/K(m), respectively, relative to PR. The relative k(cat)/K(m) of PR(G73S) varied from 14% to 400% when assayed using different substrates. Inhibition constants (K(i)) of the antiviral drug indinavir for the reaction catalyzed by the mutant enzymes were about threefold and 50-fold higher for PR(L24I) and PR(I50V), respectively, relative to PR and PR(G73S). The dimer dissociation constant (K(d)) was estimated to be approximately 20 nM for both PR(L24I) and PR(I50V), and below 5 nM for PR(G73S) and PR. Crystal structures of the mutants PR(L24I), PR(I50V) and PR(G73S) were determined in complexes with indinavir, or the p2/NC substrate analog at resolutions of 1.10-1.50 Angstrom. Each mutant revealed distinct structural changes relative to PR. The mutated residues in PR(L24I) and PR(I50V) had reduced intersubunit contacts, consistent with the increased K(d) for dimer dissociation. Relative to PR, PR(I50V) had fewer interactions of Val50 with inhibitors, in agreement with the dramatically increased K(i). The distal mutation G73S introduced new hydrogen bond interactions that can transmit changes to the substrate-binding site and alter catalytic activity. Therefore, the structural alterations observed for drug-resistant mutations were in agreement with kinetic and stability changes.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Journal Of Molecular Biology. - 354 : 4 (2005), p. 789-800. -
További szerzők:Boross Péter (1972-) (biokémikus, vegyész) Wang, Yuan-Fang Tőzsér József (1959-) (molekuláris biológus, biokémikus, vegyész) Louis, John M. Harrison, Robert W. Weber, Irene T.
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9.

001-es BibID:BIBFORM019933
Első szerző:Liu, Fengling
Cím:Mechanism of drug resistance revealed by the crystal structure of the unliganded HIV-1 protease with F53L mutation / Fengling Liu, Andrey Y. Kovalevsky, John M. Louis, Peter I. Boross, Yuan-Fang Wang, Robert W. Harrison, Irene T. Weber
Dátum:2006
ISSN:0022-2836
Megjegyzések:Mutations in HIV-1 protease (PR) that produce resistance to antiviral PR inhibitors are a major problem in AIDS therapy. The mutation F53L arising from antiretroviral therapy was introduced into the flexible flap region of the wild-type PR to study its effect and potential role in developing drug resistance. Compared to wild-type PR, PR(F53L) showed lower (15%) catalytic efficiency, 20-fold weaker inhibition by the clinical drug indinavir, and reduced dimer stability, while the inhibition constants of two peptide analog inhibitors were slightly lower than those for PR. The crystal structure of PR(F53L) was determined in the unliganded form at 1.35 Angstrom resolution in space group P4(1)2(1)2. The tips of the flaps in PR(F53L) had a wider separation than in unliganded wild-type PR, probably due to the absence of hydrophobic interactions of the side-chains of Phe53 and Ile50'. The changes in interactions between the flaps agreed with the reduced stability of PR(F53L) relative to wild-type PR. The altered flap interactions in the unliganded form of PR(F53L) suggest a distinct mechanism for drug resistance, which has not been observed in other common drug-resistant mutants.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Journal of Molecular Biology. - 358 : 5 (2006), p. 1191-1199. -
További szerzők:Kovalevsky, Andrey Yu Louis, John M. Wang, Yuan-Fang Harrison, Robert W. Weber, Irene T. Boross Péter (1972-) (biokémikus, vegyész)
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10.

001-es BibID:BIBFORM088307
035-os BibID:(WoS)000532698400027 (Scopus)85081971258
Első szerző:Miskei Márton (molekuláris biológus, genetikus)
Cím:Sequence-Based Prediction of Fuzzy Protein Interactions / Miskei Marton, Attila Horvath, Michele Vendruscolo, Monika Fuxreiter
Dátum:2020
ISSN:0022-2836
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Matematikai és természettudományok - Kémiai tudományok
Megjelenés:Journal Of Molecular Biology. - 432 : 7 (2020), p. 2289-2303. -
További szerzők:Horváth Attila (1988-) (programtervező informatikus) Vendruscolo, Michele Fuxreiter Mónika (1969-) (kutató vegyész)
Pályázati támogatás:MTA-DE Lendület
MTA
Fehérjedinamikai Kutatócsoport
GINOP-2.3.2-15-2016-00044
GINOP
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11.

001-es BibID:BIBFORM001535
Első szerző:Olivares, Isabel
Cím:HIV-1 protease dimer interface mutations that compensate for viral reverse transcriptase instability in infectious virions / Olivares I., Mulky A., Boross P., Tőzsér J., Kappes J. C., López-Galindez C., Menéndez-Arias L.
Dátum:2007
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Journal of Molecular Biology 372 : 2 (2007), p. 369-381. -
További szerzők:Mulky, Alok Boross Péter (1972-) (biokémikus, vegyész) Tőzsér József (1959-) (molekuláris biológus, biokémikus, vegyész) Kappes, John C. López-Galindez, Cecilio Menéndez-Arias, Luis
Internet cím:elektronikus változat
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12.

001-es BibID:BIBFORM067627
Első szerző:Pludowski, Pawel
Cím:Vitamin D supplementation guidelines / Pawel Pludowski, Michael F. Holick, William B. Grant, Jerzy Konstantynowicz, Mario R. Mascarenhas, Afrozul Haq, Vladyslav Povoroznyuk, Nataliya Balatska, Ana Paula Barbosa, Tatiana Karonova, Ema Rudenka, Waldemar Misiorowski, Irina Zakharova, Alena Rudenka, Jacek Łukaszkiewicz, Ewa Marcinowska-Suchowierska, Natalia Laszcz, Pawel Abramowicz, Harjit P. Bhattoa, Sunil J. Wimalawansa
Dátum:2018
Megjegyzések:Research carried out during the past two-decades extended the understanding of actions of vitamin D, from regulating calcium and phosphate absorption and bone metabolism to many pleiotropic actions in organs and tissues in the body. Most observational and ecological studies report association of higher serum 25-hydroxyvitamin D [25(OH)D] concentrations with improved outcomes for several chronic, communicable and non-communicable diseases. Consequently, numerous agencies and scientific organizations have developed recommendations for vitamin D supplementation and guidance on optimal serum 25(OH)D concentrations. The bone-centric guidelines recommend a target 25(OH)D concentration of 20 ng/mL (50 nmol/L), and age-dependent daily vitamin D doses of 400?800 IU. The guidelines focused on pleiotropic effects of vitamin D recommend a target 25(OH)D concentration of 30 ng/mL (75 nmol/L), and age-, body weight-, disease-status, and ethnicity dependent vitamin D doses ranging between 400 and 2000 IU/day. The wise and balanced choice of the recommendations to follow depends on one's individual health outcome concerns, age, body weight, latitude of residence, dietary and cultural habits, making the regional or nationwide guidelines more applicable in clinical practice. While natural sources of vitamin D can raise 25(OH)D concentrations, relative to dietary preferences and latitude of residence, in the context of general population, these sources are regarded ineffective to maintain the year-round 25(OH)D concentrations in the range of 30?50 ng/mL (75?125 nmol/L). Vitamin D self-administration related adverse effects, such as hypercalcemia and hypercalciuria are rare, and usually result from taking extremely high doses of vitamin D for a prolonged time.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Vitamin D
25(OH)D
Pleiotropic
Extra-skeletal effects
Global
Recommendations
Megjelenés:The Journal of Steroid Biochemistry and Molecular Biology 175 (2018), p. 125-135. -
További szerzők:Holick, Michael F. Grant, William B. Konstantynowicz, Jerzy Mascarenhas, Mario R. Haq, Afrozul Povoroznyuk, Vladyslav Balatska, Nataliya Barbosa, Ana Paula Karonova, Tatiana Rudenka, Ema Misiorowski, Waldemar Zakharova, Irina Rudenka, Alena Łukaszkiewicz, Jacek Marcinowska-Suchowierska, Ewa Laszcz, Natalia Abramowicz, Pawel Bhattoa Harjit Pal (1973-) (laboratóriumi szakorvos) Wimalawansa, Sunil J.
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