Faculty Opinions recommendation of Efficient, pH-dependent RNA ligation by the VS ribozyme in trans.

2004 ◽  
Author(s):  
Scott Silverman
Keyword(s):  
Vs Ribozyme ◽  
In Trans ◽  
Rna Ligation ◽  
Ph Dependent

Efficient, pH-Dependent RNA Ligation by the VS Ribozyme in Trans†

Biochemistry ◽  
2004 ◽  
Vol 43 (4) ◽  
pp. 1118-1125 ◽  
Author(s):  
Aileen C. McLeod ◽  
David M. J. Lilley
Keyword(s):  
Vs Ribozyme ◽  
In Trans ◽  
Rna Ligation ◽  
Ph Dependent

scholarly journals RNA ligation precedes the retrotransposition of U6/LINE-1 chimeric RNA

2019 ◽  
Vol 116 (41) ◽  
pp. 20612-20622 ◽  
Author(s):  
John B. Moldovan ◽  
Yifan Wang ◽  
Stewart Shuman ◽  
Ryan E. Mills ◽  
John V. Moran
Keyword(s):  
Messenger Rnas ◽  
Small Nuclear Rna ◽  
Cell Extracts ◽  
Chimeric Rnas ◽  
In Trans ◽  
Cyclic Phosphate ◽  
Rna Ligation ◽  
Chimeric Rna ◽  
In Cis

Long interspersed element-1 (LINE-1 or L1) amplifies via retrotransposition. Active L1s encode 2 proteins (ORF1p and ORF2p) that bind their encoding transcript to promote retrotransposition in cis. The L1-encoded proteins also promote the retrotransposition of small-interspersed element RNAs, noncoding RNAs, and messenger RNAs in trans. Some L1-mediated retrotransposition events consist of a copy of U6 RNA conjoined to a variably 5′-truncated L1, but how U6/L1 chimeras are formed requires elucidation. Here, we report the following: The RNA ligase RtcB can join U6 RNAs ending in a 2′,3′-cyclic phosphate to L1 RNAs containing a 5′-OH in vitro; depletion of endogenous RtcB in HeLa cell extracts reduces U6/L1 RNA ligation efficiency; retrotransposition of U6/L1 RNAs leads to U6/L1 pseudogene formation; and a unique cohort of U6/L1 chimeric RNAs are present in multiple human cell lines. Thus, these data suggest that U6 small nuclear RNA (snRNA) and RtcB participate in the formation of chimeric RNAs and that retrotransposition of chimeric RNA contributes to interindividual genetic variation.

Author response for "TIM-3 and CEACAM1 do not interact in cis and in trans"

2020 ◽  
Author(s):  
Annika De Sousa Linhares ◽  
Florian Kellner ◽  
Sabrina Jutz ◽  
Gerhard J. Zlabinger ◽  
Hans-Joachim Gabius ◽  
...  
Keyword(s):  
Author Response ◽  
In Trans ◽  
In Cis

The Reaction of Thiol Compounds with the Vitamin-K Dependent Clotting Factors

1969 ◽  
Vol 21 (03) ◽  
pp. 573-579 ◽  
Author(s):  
P Fantl
Keyword(s):  
Prothrombin Time ◽  
Vitamin K ◽  
Anaerobic Conditions ◽  
Clotting Factors ◽  
Thiol Compounds ◽  
Aerobic Conditions ◽  
One Stage ◽  
Factor Ii ◽  
Ph Dependent ◽  
The One

SummaryTreatment of human and dog oxalated plasma with 0.2 to 1.0 × 10−1 M 2.3-dithiopropanol (BAL) or dithiothreitol (DTT) at 2–4° C for 30 min results in the reduction of the vitamin-K dependent clotting factors II, VII, IX and X to the respective-SH derivatives. The reaction is pH dependent. Under aerobic conditions the delayed one stage prothrombin time can be partly reversed. Under anaerobic conditions a gradual prolongation of the one stage prothrombin time occurs without reversal.In very diluted plasma treated with the dithiols, prothrombin can be converted into thrombin if serum as source of active factors VII and X is added. In contrast SH factors VII, IX and X are inactive in the specific tests. Reoxidation to active factors II, VII, IX and X takes place during adsorption and elution of the SH derivatives. The experiments have indicated that not only factor II but also factors VII, IX and X have active-S-S-centres.

Resection Control in Trans-sphenoidal Surgery of Pituitary Macroadenoma by Intraoperative High-Field MRI

Skull Base ◽  
2005 ◽  
Vol 15 (S 2) ◽  
Author(s):  
Boris von Keller ◽  
R. Fahlbusch ◽  
O. Ganslandt ◽  
C. Nimsky
Keyword(s):  
High Field ◽  
Pituitary Macroadenoma ◽  
High Field Mri ◽  
Resection Control ◽  
In Trans

Internal Comparison of Open Microscopic versus Endoscopic Approach in Trans-sphenoidal Surgery

Skull Base ◽  
2009 ◽  
Vol 19 (03) ◽  
Author(s):  
Abdulrazag Ajlan ◽  
Anthony Zeitouni ◽  
Denis Sirhan
Keyword(s):  
Endoscopic Approach ◽  
In Trans ◽  
Internal Comparison

Our experiences in Trans-Obturator Tape surgery after performing 150 cases

2007 ◽  
Vol 148 (35) ◽  
pp. 1649-1655
Author(s):  
Roland Csorba ◽  
Rudolf Lampé ◽  
Dezső Simó ◽  
György Bacskó ◽  
Róbert Póka
Keyword(s):  
In Trans

Európában a felnőtt nők közel 30 százaléka szenved a vizelet-visszatartás zavarától. A néhány éve megjelent Trans-Obturator Tape (TOT) műtét egy újabb lehetőséget ad a stresszinkontinencia műtéti gyógyítására. Betegek és módszerek: A kivizsgálás részletes anamnézisfelvételből, stressz- és Q-tip-tesztet is magában foglaló, általános és nőgyógyászati fizikális vizsgálatból, illetve a QUID- (The Questionnaire for Urinary lncontinence Diagnosis) kérdőív kitöltéséből állt. Nem egyértelmű esetekben urodinámiás vizsgálat történt. A szerzők százötven betegen végeztek Trans-Obturator Tape beültetést. A műtét eredményességének értékelését szintén QUID-kérdőívek segítségével végezték. Eredmények: A betegek átlagéletkora 50,8 év volt (SD = 8,64). 69 páciensnek (46%) volt tisztán stresszinkontinenciája, 33 betegnek (22%) késztetéses inkontinenciája, míg 48 esetben (32%) stresszdominanciával kevert inkontinenciát mutattak ki. Az átlagos követési idő 16 hónap (4–26 hónap) volt. A stresszinkontinencia átlagos preoperatív súlyossági pontértéke 11,78, az urge-komponensé 6,63 volt. Az átlagos műtéti idő 25 perc volt. 150 műtét kapcsán szövődményt 4 esetben észleltek. 12 betegnek volt szüksége katéter viselésére 24 órán túl, a leghosszabb katéterezési idő 5 nap volt. Az átlagos ápolási idő 4,76 nap (SD = 0,8) volt. A posztoperatív kérdőívek elemzésekor a stresszkomponensre vonatkozó átlagos súlyossági pont 2,22, az urge-komponensé 2,59 volt. Az elégedettségi felmérésben 46 beteg nagyon jónak (47,4%), 39 jónak (40,2%), 7 közepesnek (7,2%), 3 gyengének (3,1%), 2 beteg pedig eredménytelennek (2,1%) ítélte meg a beavatkozást. Következtetések: A módszer avatott kezekben kiemelkedő hatékonyságú, minimálinvazív, gyors műtét, mely rövid kórházi ápolással és kevés szövődménnyel jár.

Rationalizing the pH-Activity Response for Escherichia Coli’s Glycinamide Ribonucleotidetransformylase Through Computational Methods

2019 ◽  
Author(s):  
Adrian Roitberg ◽  
Pancham Lal Gupta
Keyword(s):  
Transfer Reaction ◽  
Catalytic Mechanism ◽  
Ph Dependence ◽  
Ph Effects ◽  
Dependent Manner ◽  
E Coli ◽  
Gar Tfase ◽  
Activity Curve ◽  
Ph Dependent ◽  
Formyl Transfer

<div>Human Glycinamide ribonucleotide transformylase (GAR Tfase), a regulatory enzyme in the de novo purine biosynthesis pathway, has been established as an anti-cancer target. GAR Tfase catalyzes the formyl transfer reaction from the folate cofactor to the GAR ligand. In the present work, we study E. coli GAR Tfase, which has high sequence similarity with the human GAR Tfase with most functional residues conserved. E. coli GAR Tfase exhibits structural changes and the binding of ligands that varies with pH which leads to change the rate of the formyl transfer reaction in a pH-dependent manner. Thus, the inclusion of pH becomes essential for the study of its catalytic mechanism. Experimentally, the pH-dependence of the kinetic parameter kcat is measured to evaluate the pH-range of enzymatic activity. However, insufficient information about residues governing the pH-effects on the catalytic activity leads to ambiguous assignments of the general acid and base catalysts and consequently its catalytic mechanism. In the present work, we use pH-replica exchange molecular dynamics (pH-REMD) simulations to study the effects of pH on E. coli GAR Tfase enzyme. We identify the titratable residues governing the pH-dependent conformational changes in the system. Furthermore, we filter out the protonation states which are essential in maintaining the structural integrity, keeping the ligands bound and assisting the catalysis. We reproduce the experimental pH-activity curve by computing the population of key protonation states. Moreover, we provide a detailed description of residues governing the acidic and basic limbs of the pH-activity curve.</div>

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